|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-511 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 699.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLG 93
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTR 173
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 174 VLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQMVG-D 252
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGrE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 253 KKKHFDYQPAPKGETVLSVQGLtalhpSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEC 332
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEGL-----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 333 IDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSdfSLQGFRRaWKWLNPHKEQASVKAMIQQLAIKVSDPQLPI 412
Cdd:COG1129 316 VRIRSPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLA--SLDRLSR-GGLLDRRRERALAEEYIKRLRIKTPSPEQPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 413 TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
490
....*....|....*....
gi 496059540 493 TADVPRHAVTRETLIAAST 511
Cdd:COG1129 473 VGELDREEATEEAIMAAAT 491
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-511 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 529.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVeSPS---SGQIIMDGIPVTLNSTHQAE 90
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGISIIFQELNLFPNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSK 170
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQMV 250
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 251 G-DKKKHFDYQPAPKGETVLSVQGLTALHP--SGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQS-GSV 326
Cdd:PRK13549 241 GrELTALYPREPHTIGEVILEVRNLTAWDPvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 327 QLNGECIDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSdfSLQGFRRaWKWLNPHKEQASVKAMIQQLAIKVS 406
Cdd:PRK13549 321 FIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLA--ALDRFTG-GSRIDDAAELKTILESIQRLKVKTA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 407 DPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILV 486
Cdd:PRK13549 398 SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLV 477
|
490 500
....*....|....*....|....*
gi 496059540 487 MADGRITADVPRHAVTRETLIAAST 511
Cdd:PRK13549 478 MHEGKLKGDLINHNLTQEQVMEAAL 502
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-506 |
3.30e-175 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 502.63 E-value: 3.30e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 13 ESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL 92
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 GISIIFQELNLFPNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDT 172
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQMVGD 252
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 253 K-KKHFDYQPAPKGETVLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGE 331
Cdd:COG3845 241 EvLLRVEKAPAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 332 CIDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSDFSLQGFRRAWkWLNPHKEQASVKAMIQQLAIKVSDPQLP 411
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRYRRPPFSRGG-FLDRKAIRAFAEELIEEFDVRTPGPDTP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 412 ITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGR 491
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
490
....*....|....*
gi 496059540 492 ITADVPRHAVTRETL 506
Cdd:COG3845 480 IVGEVPAAEATREEI 494
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-509 |
1.99e-170 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 490.67 E-value: 1.99e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGI 94
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMANEFFQK-GKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTR 173
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 174 VLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQMVGDK 253
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 254 -KKHFDYQPAPKGETVLSVQGLTalhpsgGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEC 332
Cdd:PRK10762 242 lEDQYPRLDKAPGEVRLKVDNLS------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 333 IDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSdfSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPI 412
Cdd:PRK10762 316 VVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLT--ALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 413 TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
490
....*....|....*..
gi 496059540 493 TADVPRHAVTRETLIAA 509
Cdd:PRK10762 474 SGEFTREQATQEKLMAA 490
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-513 |
1.18e-166 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 480.95 E-value: 1.18e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 19 ETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISIIF 98
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 99 QELNLFPNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMD 178
Cdd:PRK11288 86 QELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 179 EPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERP-VNDASIPWIIEQMVG-DKKKH 256
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdMAQVDRDQLVQAMVGrEIGDI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 257 FDYQPAPKGETVLSVQGLTalhpsgGYKL-NDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDK 335
Cdd:PRK11288 246 YGYRPRPLGEVRLRLDGLK------GPGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 336 AHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSdfSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPITSL 415
Cdd:PRK11288 320 RSPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINIS--ARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 416 SGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
490
....*....|....*...
gi 496059540 496 VPRHAVTRETLIAASTPQ 513
Cdd:PRK11288 478 LAREQATERQALSLALPR 495
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-510 |
3.27e-151 |
|
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: 441.57 E-value: 3.27e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGV--ESPSSGQIIMDGIPVTLNSTHQAEKLGI 94
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMANEFFQKGKI-NEKYQYALAKSLLERLELDVDPYT-PLEELGIGHQQLVEIARALSKDT 172
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRmAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQMVGD 252
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 253 KKKH-FDYQPAPKGETVLSVQGLTALHPSGGY--KLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ-SGSVQL 328
Cdd:TIGR02633 241 EITSlYPHEPHEIGDVILEARNLTCWDVINPHrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 329 NGECIDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSdfSLQGFRRAWKwLNPHKEQASVKAMIQQLAIKVSDP 408
Cdd:TIGR02633 321 NGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLS--VLKSFCFKMR-IDAAAELQIIGSAIQRLKVKTASP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 409 QLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMA 488
Cdd:TIGR02633 398 FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIG 477
|
490 500
....*....|....*....|..
gi 496059540 489 DGRITADVPRHAVTRETLIAAS 510
Cdd:TIGR02633 478 EGKLKGDFVNHALTQEQVLAAA 499
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-509 |
1.72e-148 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 434.60 E-value: 1.72e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSS--GQIIMDGIPVTLNSTHQAEKLGI 94
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRV 174
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 175 LIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIP--WIIEQMVGD 252
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRADEVTedRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 253 KKKHfDYQP-APK-GETVLSVQGLTALHP--SGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ--SGSV 326
Cdd:NF040905 241 DLED-RYPErTPKiGEVVFEVKNWTVYHPlhPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 327 QLNGECIDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSdfSLQGFRRAWkWLNPHKEQASVKAMIQQLAIKVS 406
Cdd:NF040905 320 FKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLA--NLGKVSRRG-VIDENEEIKVAEEYRKKMNIKTP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 407 DPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILV 486
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYV 476
|
490 500
....*....|....*....|...
gi 496059540 487 MADGRITADVPRHAVTRETLIAA 509
Cdd:NF040905 477 MNEGRITGELPREEASQERIMRL 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-514 |
2.63e-135 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 401.47 E-value: 2.63e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGI 94
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMANEFFQK----GKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSK 170
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQMV 250
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 251 G-DKKKHF----DYQPAPKGETVLSVQGLTALHPSggyKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGS 325
Cdd:PRK09700 243 GrELQNRFnamkENVSNLAHETVFEVRNVTSRDRK---KVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 326 VQLNGECIDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSDF-SLQGFRRAWKWLNPHKEQASVKAMIQQLAIK 404
Cdd:PRK09700 320 IRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSlKDGGYKGAMGLFHEVDEQRTAENQRELLALK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 405 VSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRI 484
Cdd:PRK09700 400 CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRI 479
|
490 500 510
....*....|....*....|....*....|.
gi 496059540 485 LVMADGRITADVP-RHAVTRETLIAASTPQD 514
Cdd:PRK09700 480 AVFCEGRLTQILTnRDDMSEEEIMAWALPQE 510
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-496 |
7.63e-131 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 389.09 E-value: 7.63e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 22 DLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISIIFQEL 101
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 102 NLFPNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPT 181
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 182 SALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQMVG-DKKKHFDYQ 260
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGrSLTQRFPDK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 261 PAPKGETVLSVQGLTAL-HPSggykLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQ 339
Cdd:PRK10982 243 ENKPGEVILEVRNLTSLrQPS----IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 340 SRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSDfsLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPITSLSGGN 419
Cdd:PRK10982 319 EAINHGFALVTEERRSTGIYAYLDIGFNSLISN--IRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGN 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 420 QQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADV 496
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIV 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-508 |
7.67e-126 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 377.08 E-value: 7.67e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISI 96
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMNVMDNIFMAnefFQKGKINEKYQYALAKSLLERLELDVDPYTpleeLGIGHQQLVEIARALSKDTRVLI 176
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG---LPKRQASMQKMKQLLAALGCQLDLDSSAGS----LEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 177 MDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDASIPWIIEQM------- 249
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAItpaarek 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 250 -VGDKKKHFDYQPA-----PKGETVLSVQGLTalhpsgGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQS 323
Cdd:PRK15439 244 sLSASQKLWLELPGnrrqqAAGAPVLTVEDLT------GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 324 GSVQLNGECIDKAHFQSRLKKGLALVPEDRQGEGVVQMMSIQSNMTLSDFSLQGFrrawkWLNPHKEQASVKAMIQQLAI 403
Cdd:PRK15439 318 GRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVCALTHNRRGF-----WIKPARENAVLERYRRALNI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 404 KVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADR 483
Cdd:PRK15439 393 KFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADR 472
|
490 500
....*....|....*....|....*
gi 496059540 484 ILVMADGRITADVPRHAVTRETLIA 508
Cdd:PRK15439 473 VLVMHQGEISGALTGAAINVDTIMR 497
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
265-492 |
1.92e-77 |
|
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: 240.80 E-value: 1.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 265 GETVLSVQGLtalhpSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKK 344
Cdd:cd03215 1 GEPVLEVRGL-----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 345 GLALVPEDRQGEGVVQMMSIQSNMTLSDFslqgfrrawkwlnphkeqasvkamiqqlaikvsdpqlpitsLSGGNQQKVV 424
Cdd:cd03215 76 GIAYVPEDRKREGLVLDLSVAENIALSSL-----------------------------------------LSGGNQQKVV 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 425 LGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-234 |
4.44e-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: 221.15 E-value: 4.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISII 97
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQelnlfpnmnvmdnifmaneffqkgkinekyqyalaksllerleldvdpytpleeLGIGHQQLVEIARALSKDTRVLIM 177
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-514 |
9.59e-63 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 213.23 E-value: 9.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPS---SGQIIMDGIPVTLNSTHQA 89
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 EKLgISIIFQE--LNLFPnMNVMDNIfmaNEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARA 167
Cdd:COG1123 82 GRR-IGMVFQDpmTQLNP-VTVGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 168 LSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND------- 239
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEilaapqa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 240 -ASIPWIieqmvgDKKKHFDYQPAPKGETVLSVQGLTALHPSGGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKG 314
Cdd:COG1123 237 lAAVPRL------GAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 315 LVGLMPCQSGSVQLNGECIDKAHFQSR--LKKGLALVPEDRQGegvvqmmSIQSNMTLSDfSLQGFRRAWKWLNPHKEQA 392
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRSLreLRRRVQMVFQDPYS-------SLNPRMTVGD-IIAEPLRLHGLLSRAERRE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 393 SVKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSS 471
Cdd:COG1123 383 RVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFIS 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 472 SELDEVMALADRILVMADGRI-----TADV---PRHAVTREtLIAASTPQD 514
Cdd:COG1123 463 HDLAVVRYIADRVAVMYDGRIvedgpTEEVfanPQHPYTRA-LLAAVPSLD 512
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-234 |
1.70e-52 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 178.01 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISII 97
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEFFQKGKIN-------EKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSK 170
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLlararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-232 |
1.71e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.25 E-value: 1.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGisII 97
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIG--YV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEFFqkgKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
14-234 |
2.43e-49 |
|
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: 170.22 E-value: 2.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLG 93
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNI------------FMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQL 161
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVlvaaharlgrglLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 162 VEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-255 |
1.12e-44 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 157.33 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGisII 97
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG--VL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEFFQ-KGKINEKyqyaLAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLI 176
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGlFDEELKK----RIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 177 MDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR--------FISERPVNDaSIPWIIEQ 248
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKvvaqgsldELREEIGEE-NLEDAFVA 234
|
....*..
gi 496059540 249 MVGDKKK 255
Cdd:COG4555 235 LIGSEEG 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-231 |
1.37e-43 |
|
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: 152.17 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGisII 97
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG--YL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIfmaneffqkgkinekyqyalaksllerleldvdpytpleELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:cd03230 79 PEEPSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRF 231
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-234 |
1.42e-42 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 151.05 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISII 97
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEFFQKGKINEKYQ--YALAKSLLERLEldvdpyTPLEELGIGHQQLVEIARALSKDTRVL 175
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLErvYELFPRLKERRK------QLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 176 IMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-230 |
1.82e-42 |
|
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: 150.36 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsTHQAEKLGISII 97
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMAnefFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:cd03259 78 FQDYALFPHLTVAENIAFG---LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 178 DEPTSALS-------QSEVKVLFnvieqlKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03259 155 DEPLSALDaklreelREELKELQ------RELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-230 |
9.53e-41 |
|
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: 146.10 E-value: 9.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQAEKL 92
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 G--ISIIFQELNLFPNMNVMDNIFMANEFFQKGKINEKYQyalAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSK 170
Cdd:cd03255 81 RrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRER---AEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKR-RGVTIIYISHRlEELMEIGDYITIFRDGR 230
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD-PELAEYADRIIELRDGK 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-234 |
2.67e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.19 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYP----GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQA 89
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISsLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 ----EKLGIsiIFQELNLFPNMNVMDNIFMANEFfqkGKINEKYQYALAKSLLERLEL----DVDPYtpleELGIGHQQL 161
Cdd:COG1136 82 rlrrRHIGF--VFQFFNLLPELTALENVALPLLL---AGVSRKERRERARELLERVGLgdrlDHRPS----QLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 162 VEIARALSKDTRVLIMDEPTSAL-SQSEVKVLfNVIEQL-KRRGVTIIYISHRlEELMEIGDYITIFRDGRFISE 234
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLdSKTGEEVL-ELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-238 |
4.80e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 147.94 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsTHQAEKLG 93
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT---GLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIfmanEFFQKG-KINEKYQYALAKSLLERLELDvdpytPLE-----EL-GiGHQQLVEIAR 166
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENV----AFGLRMrGVPKAEIRARVAELLELVGLE-----GLAdryphQLsG-GQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 167 ALSKDTRVLIMDEPTSALS-------QSEVKVLfnvieqLKRRGVTIIYISHRLEELMEIGDYITIFRDGRF-------- 231
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDaklreemREELRRL------QRELGITFIYVTHDQEEALALADRIAVMNDGRIeqvgtpee 222
|
....*..
gi 496059540 232 ISERPVN 238
Cdd:COG3842 223 IYERPAT 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-230 |
1.10e-39 |
|
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: 141.94 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQAEKLGISI 96
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMNVMDNIFMAneffqkgkinekyqyalaksllerleldvdpytpleeLGIGHQQLVEIARALSKDTRVLI 176
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 177 MDEPTSAL---SQSEVKVLfnvIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03229 124 LDEPTSALdpiTRREVRAL---LKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
266-509 |
8.42e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 8.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTAlhpsgGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfqsr 341
Cdd:COG1121 4 MPAIELENLTV-----SYGgrpvLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 342 lKKGLALVPedrqgegvvQMMSIQSN--MTLSDF---SLQGFRRAWKWLNPHKEQASVKAM----IQQLAikvsdpQLPI 412
Cdd:COG1121 74 -RRRIGYVP---------QRAEVDWDfpITVRDVvlmGRYGRRGLFRRPSRADREAVDEALervgLEDLA------DRPI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 413 TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
250
....*....|....*..
gi 496059540 493 TADVPRHAVTRETLIAA 509
Cdd:COG1121 218 AHGPPEEVLTPENLSRA 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-230 |
1.69e-38 |
|
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: 139.91 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 19 ETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgISI 96
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQ--ELNLFpNMNVMDNI-F-MANEFFQKGKINEKYQYALAKSLLERLeLDVDPYTpleeLGIGHQQLVEIARALSKDT 172
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVaFgLENLGLPEEEIEERVEEALELVGLEGL-RDRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-239 |
2.30e-36 |
|
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: 141.19 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 2 QQQDIVTPHSVESEVIIETHDLSRVYP-----GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIM 76
Cdd:COG1123 245 AARGRAAPAAAAAEPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 77 DGIPVTLNSTHQAEKLG--ISIIFQ--ELNLFPNMNVMDNIFMANEFFqkGKINEKYQYALAKSLLERLELDVD-----P 147
Cdd:COG1123 325 DGKDLTKLSRRSLRELRrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLH--GLLSRAERRERVAELLERVGLPPDladryP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 148 YtpleELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIF 226
Cdd:COG1123 403 H----ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVM 478
|
250
....*....|...
gi 496059540 227 RDGRFISERPVND 239
Cdd:COG1123 479 YDGRIVEDGPTEE 491
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-230 |
2.41e-36 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 133.81 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAE-KLGISI 96
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMNVMDNIFMANEFFQkgKINEKYQYALAKSLLERLEL-DVDPYTPLeELGIGHQQLVEIARALSKDTRVL 175
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVK--GMSKAEAEERALELLEKVGLaDKADAYPA-QLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 176 IMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-230 |
2.74e-36 |
|
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: 133.56 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQaeklgISII 97
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDnifMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:cd03269 76 PEERGLYPKMKVID---QLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-231 |
6.07e-36 |
|
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: 132.76 E-value: 6.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsTHQAEKLGISII 97
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT---DLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEF--FQKGKINEKYQYAlAKSL-LERLeLDVDPytplEELGIGHQQLVEIARALSKDTRV 174
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLrkVPKDEIDERVREV-AELLqIEHL-LDRKP----KQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 175 LIMDEPTSAL-------SQSEVKVLfnvieqLKRRGVTIIYISHRLEELMEIGDYITIFRDGRF 231
Cdd:cd03301 152 FLMDEPLSNLdaklrvqMRAELKRL------QQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-238 |
6.47e-36 |
|
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: 132.98 E-value: 6.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHqaeklg 93
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIFMANEF--FQKGKINEKyqyalAKSLLERLELD--VDPYtPlEELGIGHQQLVEIARALS 169
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELqgVPKAEARER-----AEELLELVGLSgfENAY-P-HQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 170 KDTRVLIMDEPTSAL-------SQSEvkvlfnVIEQLKRRGVTIIYISHRLEELMEIGDYITIF--RDGRFISERPVN 238
Cdd:cd03293 148 VDPDVLLLDEPFSALdaltreqLQEE------LLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEVD 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-240 |
7.92e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 133.23 E-value: 7.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgISI 96
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQ--ELNLFpNMNVMDNI-F-MANEFFQKGKINEKYQYALAKSLLERLeLDVDPYtpleELGIGHQQLVEIARALSKDT 172
Cdd:COG1122 80 VFQnpDDQLF-APTVEEDVaFgPENLGLPREEIRERVEEALELVGLEHL-ADRPPH----ELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDA 240
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
268-505 |
1.13e-35 |
|
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: 133.06 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTAlHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEciDKAHFQSRLKKGLA 347
Cdd:COG4555 1 MIEVENLSK-KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE--DVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 LVPEDRqgegvvqmmSIQSNMTLSDFsLQGFRRAWKwLNPHKEQASVKAMIQQLAIkVSDPQLPITSLSGGNQQKVVLGK 427
Cdd:COG4555 78 VLPDER---------GLYDRLTVREN-IRYFAELYG-LFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 428 ALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRET 505
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
285-506 |
1.13e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.88 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEvigIYGLLG---AGRTELFKGLVGLMPCQSGSVQLNGEciDKAHFQSRLKKGLALVPEDrqgegvvqm 361
Cdd:COG1131 16 LDGVSLTVEPGE---IFGLLGpngAGKTTTIRMLLGLLRPTSGEVRVLGE--DVARDPAEVRRRIGYVPQE--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTLSDFsLQGFRRAWKwLNPHKEQASVKAMIQQLAIKvSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:COG1131 82 PALYPDLTVREN-LRFFARLYG-LPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 442 TRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRETL 506
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-230 |
3.31e-35 |
|
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: 128.90 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 19 ETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlGISIIF 98
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 99 QelnlfpnmnvmdnifmaneffqkgkinekyqyalaksllerleldvdpytpleeLGIGHQQLVEIARALSKDTRVLIMD 178
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 179 EPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-239 |
3.62e-34 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 128.51 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHqaeKLGISII 97
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEFFQKGK--INEKYQYALAKSLLERLElDVDPytplEELGIGHQQLVEIARALSKDTRVL 175
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKaeIKERVAEALDLVQLEGYA-NRKP----SQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 176 IMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRF--------ISERPVND 239
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIqqigtpeeIYEEPANR 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-238 |
5.49e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.35 E-value: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsTHQAEKLGISII 97
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT---DLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNI-F---MANefFQKGKINEKYQYAlAKSL-LERLeLDVDPytplEELGIGHQQLVEIARALSKDT 172
Cdd:COG3839 81 FQSYALYPHMTVYENIaFplkLRK--VPKAEIDRRVREA-AELLgLEDL-LDRKP----KQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 173 RVLIMDEPTSALSQ-------SEVKVLFnvieqlKRRGVTIIYISHRLEELMEIGDYITIFRDGRF--------ISERPV 237
Cdd:COG3839 153 KVFLLDEPLSNLDAklrvemrAEIKRLH------RRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIqqvgtpeeLYDRPA 226
|
.
gi 496059540 238 N 238
Cdd:COG3839 227 N 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
33-182 |
6.22e-34 |
|
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: 125.45 E-value: 6.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlNSTHQAEKLGISIIFQELNLFPNMNVMDN 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 113 IFMANEFFQKGKINEKYQyalAKSLLERLELDVDPYTPLEELGI----GHQQLVEIARALSKDTRVLIMDEPTS 182
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR---AEEALEKLGLGDLADRPVGERPGtlsgGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-232 |
1.04e-33 |
|
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: 127.45 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYpGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSthqAEKLGISII 97
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP---PEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIfmaneffqkgkinekyQYALAKSLLERLELDVDPYTPLEELGIGH-------------QQLVEI 164
Cdd:cd03299 77 PQNYALFPHMTVYKNI----------------AYGLKKRKVDKKEIERKVLEIAEMLGIDHllnrkpetlsggeQQRVAI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 165 ARALSKDTRVLIMDEPTSALsqsEVKVLFNVIEQLKR----RGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:cd03299 141 ARALVVNPKILLLDEPFSAL---DVRTKEKLREELKKirkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
268-506 |
1.09e-33 |
|
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: 127.85 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTAlhpsgGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLK 343
Cdd:COG1120 1 MLEAENLSV-----GYGgrpvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 344 KgLALVPedrqgegvvQMMSIQSNMTLSDFSLQG---FRRAWKWLNPHKEQASVKAM----IQQLAIKvsdpqlPITSLS 416
Cdd:COG1120 76 R-IAYVP---------QEPPAPFGLTVRELVALGrypHLGLFGRPSAEDREAVEEALertgLEHLADR------PVDELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 417 GGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQ-QGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
250
....*....|..
gi 496059540 496 -VPRHAVTRETL 506
Cdd:COG1120 220 gPPEEVLTPELL 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-230 |
1.22e-33 |
|
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: 127.30 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL--GI 94
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMA--------NEFFQKGKINEKyqyALAKSLLERLELDVDPYTPLEELGIGHQQLVEIAR 166
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwRSLFGLFPKEEK---QRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 167 ALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-211 |
2.25e-33 |
|
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: 125.98 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL--GI 94
Cdd:cd03292 1 IEFINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMANEFFQKG--KINEKyqyalAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDT 172
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPprEIRKR-----VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISH 211
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
17-230 |
4.44e-33 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 125.70 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL 92
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 G--ISIIFQE----LNlfPNMNVMDNIFMANEFFQKGKINEKYQYALAKsLLERLELDVD-----PYtpleELGIGHQQL 161
Cdd:cd03257 81 RkeIQMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLL-LLVGVGLPEEvlnryPH----ELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 162 VEIARALSKDTRVLIMDEPTSALsqsEVKVLFNVIEQLKR----RGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSAL---DVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
30-232 |
6.69e-33 |
|
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: 126.22 E-value: 6.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL---GISIIFQELNLFPN 106
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 107 MNVMDNIFMANEFfqKGkINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQ 186
Cdd:cd03294 117 RTVLENVAFGLEV--QG-VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496059540 187 SEVKVLFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:cd03294 194 LIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
17-236 |
1.23e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 124.72 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAE---KLG 93
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 IsiIFQELNLFPNMNVMDNIFMANEffQKGKINEKYQYALAKSLLERLEL----DVDPytplEELGIGHQQLVEIARALS 169
Cdd:COG1126 81 M--VFQQFNLFPHLTVLENVTLAPI--KVKKMSKAEAEERAMELLERVGLadkaDAYP----AQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 170 KDTRVLIMDEPTSALSQSEVK-VLfNVIEQLKRRGVTIIYISHrlEelM----EIGDYITIFRDGRFISERP 236
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGeVL-DVMRDLAKEGMTMVVVTH--E--MgfarEVADRVVFMDGGRIVEEGP 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-230 |
1.28e-32 |
|
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: 124.32 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGI 94
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMAnEFFQKGKinekyqyALAKSLLER-LELdvdpYTPLEEL---------GiGHQQLVEI 164
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLG-AYARRDR-------AEVRADLERvYEL----FPRLKERrrqragtlsG-GEQQMLAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 165 ARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
17-230 |
1.53e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.78 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL--G 93
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIF------------MANEFFQKgkinekyQYALAKSLLERLELDVDPYTPLEELGIGHQQL 161
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLagrlgrtstwrsLLGLFPPE-------DRERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 162 VEIARALSKDTRVLIMDEPTSAL----SQSevkvlfnVIEQLKR----RGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLdpktARQ-------VMDLLRRiareDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
269-504 |
1.83e-32 |
|
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: 123.70 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTAlhpsgGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKK 344
Cdd:cd03224 1 LEVENLNA-----GYGksqiLFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 345 GLALVPEDRQgegVVQMMSIQSNMTLSDFSLQGFRRAWKWlnphkeqASV-------KAMIQQLAikvsdpqlpiTSLSG 417
Cdd:cd03224 76 GIGYVPEGRR---IFPELTVEENLLLGAYARRRAKRKARL-------ERVyelfprlKERRKQLA----------GTLSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 418 GNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVP 497
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
....*..
gi 496059540 498 RHAVTRE 504
Cdd:cd03224 216 AAELLAD 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
285-492 |
1.86e-32 |
|
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: 122.12 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfqSRLKKGLALVPEDrqgegvvqmMSI 364
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYLPEE---------PSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFsLQgfrrawkwlnphkeqasvkamiqqlaikvsdpqlpitsLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03230 85 YENLTVREN-LK--------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059540 445 IDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-230 |
2.56e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.61 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ----AEKL 92
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 GisiifqelnLFPNMNVMDNIfmanEFF------QKGKINEKyqyalAKSLLERLELDVDPYTPLEELGIGHQQLVEIAR 166
Cdd:COG4152 81 G---------LYPKMKVGEQL----VYLarlkglSKAEAKRR-----ADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 167 ALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-238 |
4.10e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.66 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYP----GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHqa 89
Cdd:COG1116 4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 eklgISIIFQELNLFPNMNVMDNIFMANEFfqkGKINEKYQYALAKSLLERLEL----DVDPYtpleELGIGHQQLVEIA 165
Cdd:COG1116 82 ----RGVVFQEPALLPWLTVLDNVALGLEL---RGVPKAERRERARELLELVGLagfeDAYPH----QLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 166 RALSKDTRVLIMDEPTSAL-------SQSEvkvlfnVIEQLKRRGVTIIYISHRLEELMEIGDYITIF--RDGRFISERP 236
Cdd:COG1116 151 RALANDPEVLLMDEPFGALdaltrerLQDE------LLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEID 224
|
..
gi 496059540 237 VN 238
Cdd:COG1116 225 VD 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-238 |
4.48e-32 |
|
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: 122.67 E-value: 4.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAG-----VESPSSGQIIMDGIPV-TLNSTHQAEK 91
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 92 LGISIIFQELNLFPnMNVMDNIFMAneffQK--GKINEKYQYALAKSLLERLELDVDPYTPLEELGI--GHQQLVEIARA 167
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYG----LRlhGIKLKEELDERVEEALRKAALWDEVKDRLHALGLsgGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 168 LSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRgVTIIYISHRLEELMEIGDYITIFRDGRFISERPVN 238
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-256 |
4.67e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.60 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 9 PHSVESEVIIETHDLSRvyPGVValDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ 88
Cdd:COG1129 248 RAAAPGEVVLEVEGLSV--GGVV--RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 89 AEKLGISII---FQELNLFPNMNVMDNIFMAN--EFFQKGKINEKYQYALAKSLLERLELDV-DPYTPLEELGIGHQQLV 162
Cdd:COG1129 324 AIRAGIAYVpedRKGEGLVLDLSIRENITLASldRLSRGGLLDRRRERALAEEYIKRLRIKTpSPEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 163 EIARALSKDTRVLIMDEPT-----SAlsQSEVkvlFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPV 237
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTrgidvGA--KAEI---YRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDR 478
|
250
....*....|....*....
gi 496059540 238 NDASIPWIIEQMVGDKKKH 256
Cdd:COG1129 479 EEATEEAIMAAATGGAAAA 497
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-234 |
9.46e-32 |
|
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: 121.17 E-value: 9.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSThQAEKLGISII 97
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-ALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQElnLFPNMNVMDNIfmanEFFQKGKINEKyqyALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:cd03268 80 APG--FYPNLTARENL----RLLARLLGIRK---KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-510 |
9.97e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 128.26 E-value: 9.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKS----TMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL---GISIIFQE-- 100
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnRIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 101 --LNlfPNMNVMDNIfmANEFFQKGKINEKYQYALAKSLLERLELDvDPYTPLE----ELGIGHQQLVEIARALSKDTRV 174
Cdd:COG4172 103 tsLN--PLHTIGKQI--AEVLRLHRGLSGAAARARALELLERVGIP-DPERRLDayphQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 175 LIMDEPTSALS---QSEVKVLfnvIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND----------- 239
Cdd:COG4172 178 LIADEPTTALDvtvQAQILDL---LKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAElfaapqhpytr 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 240 ---ASIPwiieqmVGDKKkhfdyQPAPKGETVLSVQGLTALHP--SGGYK--------LNDVTFSLSKGEVIGIYGLLGA 306
Cdd:COG4172 255 kllAAEP------RGDPR-----PVPPDAPPLLEARDLKVWFPikRGLFRrtvghvkaVDGVSLTLRRGETLGLVGESGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 307 GRTELFKGLVGLMPCQsGSVQLNGECIDKAHFQS--RLKKGLALVPEDRQGegvvqmmSIQSNMTLSDFSLQGFRRawkw 384
Cdd:COG4172 324 GKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRAlrPLRRRMQVVFQDPFG-------SLSPRMTVGQIIAEGLRV---- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 385 LNPHKEQASVKAMIQQLAIKVsdpQLPITSL-------SGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLI 457
Cdd:COG4172 392 HGPGLSAAERRARVAEALEEV---GLDPAARhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLL 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 458 GKM-AQQGLAVMFSSSELDEVMALADRILVMADGRI-----TADV---PRHAVTREtLIAAS 510
Cdd:COG4172 469 RDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVveqgpTEQVfdaPQHPYTRA-LLAAA 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-230 |
1.29e-31 |
|
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: 119.80 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgIS 95
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFpNMNVMDNIfmaneffqkgkinekyqyalaksllerleldvdpytpleeLGIGHQQLVEIARALSKDTRVL 175
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 176 IMDEPTSAL-SQSEvKVLFNVIEQLkRRGVTIIYISHRLeELMEIGDYITIFRDGR 230
Cdd:cd03228 119 ILDEATSALdPETE-ALILEALRAL-AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-232 |
1.52e-31 |
|
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: 121.07 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGis 95
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFPNMNVMDNIfmanEFFQ--KGkINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTR 173
Cdd:cd03263 79 YCPQFDALFDELTVREHL----RFYArlKG-LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 174 VLIMDEPTSAL---SQSEVkvlFNVIEQLkRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:cd03263 154 VLLLDEPTSGLdpaSRRAI---WDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
285-494 |
1.66e-31 |
|
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: 120.72 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEcidkahFQSRLKKGLALVPedrqgegvvQMMSI 364
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIGYVP---------QRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLS--DF---SLQGFRRAWKWLNpHKEQASVKAMIQQLAI-KVSDPQlpITSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:cd03235 80 DRDFPISvrDVvlmGLYGHKGLFRRLS-KADKAKVDEALERVGLsELADRQ--IGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMaDGRITA 494
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVA 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-245 |
1.86e-31 |
|
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: 121.24 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL- 92
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 -GISIIFQELNLFPNMNVMDNIfmanEFF--QKGKINEKYQYALAKSLLERLEL-DVDPYTPlEELGIGHQQLVEIARAL 168
Cdd:COG1127 82 rRIGMLFQGGALFDSLTVFENV----AFPlrEHTDLSEAEIRELVLEKLELVGLpGAADKMP-SELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 169 SKDTRVLIMDEPTSAL----SqsevKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND---A 240
Cdd:COG1127 157 ALDPEILLYDEPTAGLdpitS----AVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEllaS 232
|
....*
gi 496059540 241 SIPWI 245
Cdd:COG1127 233 DDPWV 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-234 |
2.13e-31 |
|
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: 120.55 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVY----PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVtlNSTHQAEKL 92
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV--VKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 GISIIFQELNLFPNMNVMDNIfmanEFF----------QKGKINEKYQYALAKSLLERleldvdpytPLEELGIGHQQLV 162
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENL----EYFaglyglkgdeLTARLEELADRLGMEELLDR---------RVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 163 EIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-232 |
2.46e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.56 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEklgISI 96
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---INM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMNVMDNIF--MANEFFQKGKINEKYQYALakSLLERLEL-DVDPYtpleELGIGHQQLVEIARALSKDTR 173
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAfgLKQDKLPKAEIASRVNEML--GLVHMQEFaKRKPH----QLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 174 VLIMDEPTSALSQS-EVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:PRK11607 170 LLLLDEPMGALDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-214 |
4.35e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.77 E-value: 4.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL--G 93
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIFMANEF--FQKGKINEKYQYALAK-SLLERleLDVDPytplEELGIGHQQLVEIARALSK 170
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVtgKSRKEIRRRVREVLDLvGLSDK--AKALP----HELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLE 214
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-492 |
5.47e-31 |
|
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: 126.07 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVES--PSSGQII----------------MDGI 79
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 80 PVTL-NSTHQAEKLG---------------ISIIFQE-LNLFPNMNVMDNIFMA-NEFFQKGKinEKYQYALakSLLERL 141
Cdd:TIGR03269 81 PCPVcGGTLEPEEVDfwnlsdklrrrirkrIAIMLQRtFALYGDDTVLDNVLEAlEEIGYEGK--EAVGRAV--DLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 142 ELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEIG 220
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 221 DYITIFRDGRFISERPVNDASIPWIieQMVGDKKKHFDYQpapKGETVLSVQGLTALHPS---GGYKLND-VTFSLSKGE 296
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAVFM--EGVSEVEKECEVE---VGEPIIKVRNVSKRYISvdrGVVKAVDnVSLEVKEGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 297 VIGIYGLLGAGRTELFKGLVGLMPCQSGS--VQLNGECID----KAHFQSRLKKGLALVpedRQGEGVVQMMSIQSNMTL 370
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDmtkpGPDGRGRAKRYIGIL---HQEYDLYPHRTVLDNLTE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 371 SdfslqgfrrawKWLNPHKEQASVKAMIQQLAIKVSD-------PQLPiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTR 443
Cdd:TIGR03269 389 A-----------IGLELPDELARMKAVITLKMVGFDEekaeeilDKYP-DELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 444 GIDVGAKTDVYHLIGK----MAQQGLAVmfsSSELDEVMALADRILVMADGRI 492
Cdd:TIGR03269 457 TMDPITKVDVTHSILKareeMEQTFIIV---SHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
17-239 |
6.96e-31 |
|
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: 119.61 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL 92
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 --GISIIFQELNLFPNMNVMDNIFMAnefFQKGKINEKYQYALAKSLLERLELD--VDPYtPlEELGIGHQQLVEIARAL 168
Cdd:cd03258 81 rrRIGMIFQHFNLLSSRTVFENVALP---LEIAGVPKAEIEERVLELLELVGLEdkADAY-P-AQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 169 SKDTRVLIMDEPTSAL----SQSEVKVLFNVieqLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:cd03258 156 ANNPKVLLCDEATSALdpetTQSILALLRDI---NRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
18-239 |
9.73e-31 |
|
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: 119.14 E-value: 9.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLG--IS 95
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFPNMNVMDNI-FMANEFFQ--KGKINEKyqyALAKslLERLEL--DVDPYTplEELGIGHQQLVEIARALSK 170
Cdd:cd03261 81 MLFQSGALFDSLTVFENVaFPLREHTRlsEEEIREI---VLEK--LEAVGLrgAEDLYP--AELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
266-495 |
1.17e-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: 118.93 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTAlhpsgGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSR 341
Cdd:COG0410 1 MPMLEVENLHA-----GYGgihvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 342 LKKGLALVPEDRqgeGVVQMMSIQSNMTLSDFSLQGfRRAWKW-------LNPHkeqasVKAMIQQLAikvsdpqlpiTS 414
Cdd:COG0410 76 ARLGIGYVPEGR---RIFPSLTVEENLLLGAYARRD-RAEVRAdlervyeLFPR-----LKERRRQRA----------GT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRG-----IDvgaktDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMAD 489
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGlapliVE-----EIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLER 211
|
....*.
gi 496059540 490 GRITAD 495
Cdd:COG0410 212 GRIVLE 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
47-233 |
1.31e-30 |
|
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: 118.17 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 47 VLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipVTLNSTHQA-----EKLGISIIFQELNLFPNMNVMDNIfmanEFFQ 121
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKinlppQQRKIGLVFQQYALFPHLNVRENL----AFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 122 KGKINEKYQYALAKsLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKR 201
Cdd:cd03297 101 KRKRNREDRISVDE-LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|...
gi 496059540 202 R-GVTIIYISHRLEELMEIGDYITIFRDGRFIS 233
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-234 |
3.18e-30 |
|
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: 118.22 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV-TLNSTHQAEKlgIS 95
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSRRELARR--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFPNMNVMDNIFMA-----NEFFQKGKINEkyqyALAKSLLERLELDVDPYTPLEEL-GiGHQQLVEIARALS 169
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGryphlGLFGRPSAEDR----EAVEEALERTGLEHLADRPVDELsG-GERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 170 KDTRVLIMDEPTSAL---SQSEVkvlFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:COG1120 154 QEPPLLLLDEPTSHLdlaHQLEV---LELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-222 |
9.06e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 115.65 E-value: 9.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGisII 97
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA--YL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIfmanEFFQKGKiNEKYQYALAKSLLERLELdvdpyTPLEELGIGH-----QQLVEIARALSKDT 172
Cdd:COG4133 81 GHADGLKPELTVRENL----RFWAALY-GLRADREAIDEALEAVGL-----AGLADLPVRQlsagqKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEEL-----MEIGDY 222
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELaaarvLDLGDF 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
269-509 |
1.13e-29 |
|
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: 116.28 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKgLAL 348
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 349 V---PEDrqgegvvQMMSiqsnMTLSD---FSL--QGF------RRAWKWLnphkeqASVKamIQQLAikvsdpQLPITS 414
Cdd:COG1122 80 VfqnPDD-------QLFA----PTVEEdvaFGPenLGLpreeirERVEEAL------ELVG--LEHLA------DRPPHE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:COG1122 135 LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
250
....*....|....*.
gi 496059540 495 D-VPRHAVTRETLIAA 509
Cdd:COG1122 215 DgTPREVFSDYELLEE 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-230 |
1.52e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 116.63 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLG 93
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIFMA-----NEFFQKGKIN-------EKYQYALAKSLLERLELDVDPYTPLEELGIGHQQL 161
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVAqhqqlKTGLFSGLLKtpafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 162 VEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
285-495 |
2.00e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 114.07 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKgLALVPedrqgegvvqmmsi 364
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 qsnmtlsdfslqgfrrawkwlnphkeQASVKAMIQQLAIKvsdpqlPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03214 80 --------------------------QALELLGLAHLADR------PFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 445 IDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03214 128 LDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-493 |
2.19e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 121.33 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 20 THDLSRVYPGVVALDSVNYRVYR-NKVnVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipvtlnsthqaeklGISIIF 98
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPgDRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------------GLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 99 --QELNLFPNMNVMDNIFMANEFFQK--------------------------GKINEKYQYAL---AKSLLERLEL-DVD 146
Cdd:COG0488 66 lpQEPPLDDDLTVLDTVLDGDAELRAleaeleeleaklaepdedlerlaelqEEFEALGGWEAearAEEILSGLGFpEED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 147 PYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTsalsqsevkvlfN------VI---EQLKRRGVTIIYISH-R--LE 214
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPT------------NhldlesIEwleEFLKNYPGTVLVVSHdRyfLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 215 EL----MEI---------GDYiTIFRDGR-----------------------FISERPVN-----------DAsipwiIE 247
Cdd:COG0488 214 RVatriLELdrgkltlypGNY-SAYLEQRaerleqeaaayakqqkkiakeeeFIRRFRAKarkakqaqsriKA-----LE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 248 QM------VGDKKKHFDYQPAPK-GETVLSVQGLTAlhpsgGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLV 316
Cdd:COG0488 288 KLereeppRRDKTVEIRFPPPERlGKKVLELEGLSK-----SYGdktlLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 317 GLMPCQSGSVQLnGECIDKAHF-QSRlkkgLALVPEDRqgegVVQmmsiqsnmTLSDFSlqgfrrawkwlnPHKEQASVK 395
Cdd:COG0488 363 GELEPDSGTVKL-GETVKIGYFdQHQ----EELDPDKT----VLD--------ELRDGA------------PGGTEQEVR 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 396 AMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTdvyhligkMAQQGL-----AVMFS 470
Cdd:COG0488 414 GYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLE--------ALEEALddfpgTVLLV 485
|
570 580
....*....|....*....|....*.
gi 496059540 471 SSE---LDEVmalADRILVMADGRIT 493
Cdd:COG0488 486 SHDryfLDRV---ATRILEFEDGGVR 508
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-262 |
2.50e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.33 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipVTLNSTHQAEKLGISII 97
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--RDLFTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNI-FmaneFFQKGKINEKYQYALAKSLLERLELDvdpytPLE-----ELGIGHQQLVEIARALSKD 171
Cdd:COG1118 81 FQHYALFPHMTVAENIaF----GLRVRPPSKAEIRARVEELLELVQLE-----GLAdrypsQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 172 TRVLIMDEPTSALsQSEVK-----VLFNVIEQLkrrGVTIIYISHRLEELMEIGDYITIFRDGRfiserpvndasipwiI 246
Cdd:COG1118 152 PEVLLLDEPFGAL-DAKVRkelrrWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGR---------------I 212
|
250
....*....|....*.
gi 496059540 247 EQmVGDKKKHFDyQPA 262
Cdd:COG1118 213 EQ-VGTPDEVYD-RPA 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-234 |
2.60e-29 |
|
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: 115.33 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISII 97
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEFFQKGKineKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSK---KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-230 |
3.58e-29 |
|
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: 115.09 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGV-VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQAEKLGIS 95
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IifQELNLFPNMNVMDNIFM--ANEFFQKGKINEKyqyalAKSLLERLELdvDPYTPLE----ELGIGHQQLVEIARALS 169
Cdd:cd03295 81 I--QQIGLFPHMTVEENIALvpKLLKWPKEKIRER-----ADELLALVGL--DPAEFADryphELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 170 KDTRVLIMDEPTSALS-------QSEVKvlfnvieQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03295 152 ADPPLLLMDEPFGALDpitrdqlQEEFK-------RLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGE 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
269-492 |
4.31e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 114.14 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGG-YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfQSRLKKGLA 347
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTD--RKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 LVPedrqgegvvqmmsiQSNMTLSDFS----------LQGFRRawkwlnpHKEQASVKAMIQQLAI-KVSDpqLPITSLS 416
Cdd:cd03263 79 YCP--------------QFDALFDELTvrehlrfyarLKGLPK-------SEIKEEVELLLRVLGLtDKAN--KRARTLS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 417 GGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMaQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03263 136 GGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-231 |
1.17e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVtlnsthQAEKLG 93
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNL---FPnMNVMDnIFMANEFFQKG--KINEKYQYALAKSLLERLELdvDPY--TPLEEL-GiGHQQLVEIA 165
Cdd:COG1121 77 IGYVPQRAEVdwdFP-ITVRD-VVLMGRYGRRGlfRRPSRADREAVDEALERVGL--EDLadRPIGELsG-GQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 166 RALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRF 231
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-238 |
3.66e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 12 VESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnstHQ-AE 90
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT----HVpAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGISIIFQELNLFPNMNVMDNIFMANEFfQK---GKINEKYQYALAKSLLERLElDVDPytplEELGIGHQQLVEIARA 167
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVFENVAFGLRM-QKtpaAEITPRVMEALRMVQLEEFA-QRKP----HQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 168 LSKDTRVLIMDEPTSALS-------QSEVKvlfnvieQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRF-------- 231
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDyklrkqmQNELK-------ALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIeqdgtpre 231
|
....*..
gi 496059540 232 ISERPVN 238
Cdd:PRK09452 232 IYEEPKN 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-236 |
4.14e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.54 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnSTHQAEKLG 93
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIFMANEFFqkgKINEKYQYALAKSLLE--RLELDVDpyTPLEELGIGHQQLVEIARALSKD 171
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYF---GMSTREIEAVIPSLLEfaRLESKAD--ARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 172 TRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE-RP 236
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEgRP 256
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-230 |
5.67e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 111.66 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsTHQAEKLGISII 97
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT---DVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFM------ANEFFQKGKINEKyqyalAKSLLERLELD--VDPYTPleELGIGHQQLVEIARALS 169
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFglrvkpRSERPPEAEIRAK-----VHELLKLVQLDwlADRYPA--QLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 170 KDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-234 |
7.36e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.45 E-value: 7.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 19 ETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgISIIF 98
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 99 QELNLfpnMNVMDnifmaneffqkgkinekyqyalaksLLERleldvdpytPLEELGIGHQQLVEIARALSKDTRVLIMD 178
Cdd:cd03214 80 QALEL---LGLAH-------------------------LADR---------PFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 179 EPTSAL---SQSEVkvlFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03214 123 EPTSHLdiaHQIEL---LELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
285-491 |
1.02e-27 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 110.25 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKgLALV---PEDrqgegvvQM 361
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVfqnPDD-------QF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 msiqSNMTLSD---FSLQGFRrawkwLNPHKEQASVKAMIQQLAIKvSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:cd03225 89 ----FGPTVEEevaFGLENLG-----LPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGR 491
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-232 |
1.33e-27 |
|
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: 116.86 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT---LNSTHQAekl 92
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqidPASLRRQ--- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 gISIIFQELNLFpNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELGI---GHQ-QLVEIARAL 168
Cdd:COG2274 551 -IGVVLQDVFLF-SGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYD--TVVGEGGSnlsGGQrQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 169 SKDTRVLIMDEPTSAL-SQSEVKVLfNVIEQLkRRGVTIIYISHRLeELMEIGDYITIFRDGRFI 232
Cdd:COG2274 627 LRNPRILILDEATSALdAETEAIIL-ENLRRL-LKGRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
269-495 |
1.37e-27 |
|
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: 110.60 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHpsGGYK-LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLA 347
Cdd:cd03219 1 LEVRGLTKRF--GGLVaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 lvpedR--QGEGVVQMMSIQSNMTLSdFSLQGFRRAWKWLNPHKEQASVKAMIQQLAI----KVSDpqLPITSLSGGNQQ 421
Cdd:cd03219 79 -----RtfQIPRLFPELTVLENVMVA-AQARTGSGLLLARARREEREARERAEELLERvglaDLAD--RPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 422 KVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-223 |
1.79e-27 |
|
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: 109.55 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 19 ETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHqaeklgISIIF 98
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 99 QELNL---FPnMNVMDniFMANEFFQK---GKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDT 172
Cdd:cd03235 75 QRRSIdrdFP-ISVRD--VVLMGLYGHkglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYI 223
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
285-494 |
1.92e-27 |
|
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: 109.29 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfqsrlKKGLALVPEDRqgeGVVQMMSI 364
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYLPEER---GLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMtLSDFSLQGfrrawkwLNPHKEQASVKAMIQQLAIkvSDPQL-PITSLSGGNQQKVVLGKALMTQPQVVFLDEPTR 443
Cdd:cd03269 88 IDQL-VYLAQLKG-------LKKEEARRRIDEWLERLEL--SEYANkRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 444 GIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-234 |
2.73e-27 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 109.38 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlgISII 97
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR--IGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFM-ANEFFQKGKINEKYqyalAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLI 176
Cdd:cd03265 79 FQDLSVDDELTGWENLYIhARLYGVPGAERRER----IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 177 MDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
285-495 |
6.81e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 108.22 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHFQSRLKKGLALVPEdrqGEGVVQMMSI 364
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRRLGFVSD---STGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNmtlsdfsLQGFRRAWKwLNPHKEQASVKAMIQQLAIKvsdPQL--PITSLSGGNQQKVVLGKALMTQPQVVFLDEPT 442
Cdd:cd03266 96 REN-------LEYFAGLYG-LKGDELTARLEELADRLGME---ELLdrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 443 RGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03266 165 TGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-234 |
1.40e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.51 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLG 93
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQelNLFPNMNVMDNIFMANEFFqkgKINEKYQYALAKSLLE--RLELDVDpyTPLEELGIGHQQLVEIARALSKD 171
Cdd:PRK13537 84 VVPQFD--NLDPDFTVRENLLVFGRYF---GLSAAAARALVPPLLEfaKLENKAD--AKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 172 TRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-239 |
1.59e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 107.97 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP----GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlG 93
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQE----LNlfPNMNVMDNIFMANEFFQKGKINEKyqyalAKSLLERLELDVD--PYTPlEELGIGHQQLVEIARA 167
Cdd:COG1124 81 VQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREER-----IAELLEQVGLPPSflDRYP-HQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 168 LSKDTRVLIMDEPTSAL---SQSEVkvlFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:COG1124 153 LILEPELLLLDEPTSALdvsVQAEI---LNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
269-510 |
1.83e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 107.58 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahfqsrlkkg 345
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 lalvPEDRQGEGVVQMM------SIQSNMTLSD-----FSLQGFRRAwkwlnphkeQASVKAMIQQLAIkvsDPQL---- 410
Cdd:COG1124 72 ----RRRKAFRRRVQMVfqdpyaSLHPRHTVDRilaepLRIHGLPDR---------EERIAELLEQVGL---PPSFldry 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 411 PItSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMAD 489
Cdd:COG1124 136 PH-QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
250 260
....*....|....*....|....*....
gi 496059540 490 GRITADV--------PRHAVTREtLIAAS 510
Cdd:COG1124 215 GRIVEELtvadllagPKHPYTRE-LLAAS 242
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-230 |
1.88e-26 |
|
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: 112.93 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQAEKlgIS 95
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdLDPASWRRQ--IA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFPnMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELGI----GHQQLVEIARALSKD 171
Cdd:COG4988 415 WVPQNPYLFA-GTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLD--TPLGEGGRglsgGQAQRLALARALLRD 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 172 TRVLIMDEPTSAL-SQSEvKVLFNVIEQLkRRGVTIIYISHRLeELMEIGDYITIFRDGR 230
Cdd:COG4988 492 APLLLLDEPTAHLdAETE-AEILQALRRL-AKGRTVILITHRL-ALLAQADRILVLDDGR 548
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-232 |
6.01e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.03 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 19 ETHDLSRVYPGVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipvtlNSTHQAEKLG-ISI 96
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----KPIKAKERRKsIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELN--LFPNmNVMDNIFMANEffQKGKINEKyqyalAKSLLERLEL----DVDPYTpleeLGIGHQQLVEIARALSK 170
Cdd:cd03226 76 VMQDVDyqLFTD-SVREELLLGLK--ELDAGNEQ-----AETVLKDLDLyalkERHPLS----LSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
281-494 |
6.81e-26 |
|
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: 108.66 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 281 GGYKLnDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahFQSRlkKGLALVPEDRQGEGVVQ 360
Cdd:TIGR02142 10 GDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL----FDSR--KGIFLPPEKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSIQSNMTLSDFSLQGFRRAwkwlNPHKEQASVKAMIQQLAIkvsDPQL--PITSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:TIGR02142 83 EARLFPHLSVRGNLRYGMKRA----RPSERRISFERVIELLGI---GHLLgrLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-234 |
7.16e-26 |
|
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: 105.39 E-value: 7.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 28 PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIP---VTLNSTHQaeklGISIIFQELNLF 104
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdISRKSLRS----MIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 105 PNmNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEE----LGIGHQQLVEIARALSKDTRVLIMDEP 180
Cdd:cd03254 90 SG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYD--TVLGEnggnLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 181 TSAL-SQSEVKVLfNVIEQLkRRGVTIIYISHRLEELMEiGDYITIFRDGRFISE 234
Cdd:cd03254 167 TSNIdTETEKLIQ-EALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-239 |
8.21e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 107.96 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTH-QAEK 91
Cdd:PRK11153 2 IELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTaLSEKElRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 92 LGISIIFQELNLFPNMNVMDNIFMANEF--FQKGKINEKyqyalAKSLLERLEL----DVDPytplEELGIGHQQLVEIA 165
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELagTPKAEIKAR-----VTELLELVGLsdkaDRYP----AQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 166 RALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-349 |
9.63e-26 |
|
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: 108.28 E-value: 9.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 29 GVVALDsVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipVTLNSTHQ-----AEKLGISIIFQELNL 103
Cdd:TIGR02142 10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--RTLFDSRKgiflpPEKRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 104 FPNMNVMDNIfmaneffqkgkinekyQYALAKSLLErlELDVDPYTPLEELGIGH-------------QQLVEIARALSK 170
Cdd:TIGR02142 87 FPHLSVRGNL----------------RYGMKRARPS--ERRISFERVIELLGIGHllgrlpgrlsggeKQRVAIGRALLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPvndasipwiIEQM 249
Cdd:TIGR02142 149 SPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP---------IAEV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 250 VGDKKkhFDYQPAPKGETVLSVQ--------GLTALHPSGGYKL------------------NDVTFSLSKGEVIGIYGL 303
Cdd:TIGR02142 220 WASPD--LPWLAREDQGSLIEGVvaehdqhyGLTALRLGGGHLWvpenlgptgarlrlrvpaRDVSLALQKPEATSIRNI 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496059540 304 LGAGRTELF---KGLVGLMpCQSGSVQLNGECIDKAHFQSRLKKGLALV 349
Cdd:TIGR02142 298 LPARVVEIEdsdIGRVGVV-LESGGKTLWARITRWARDELGIAPGTPVF 345
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-234 |
1.46e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.17 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAE-KLGIS 95
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFPNMNVMDNIfMANEFFQKGKINEKYQyALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVL 175
Cdd:PRK09493 81 MVFQQFYLFPHLTALENV-MFGPLRVRGASKEEAE-KQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 176 IMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYItIFRDGRFISE 234
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRL-IFIDKGRIAE 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
13-228 |
1.66e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.12 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 13 ESEVIIETHDLSRVYP----------GVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV 81
Cdd:COG4608 3 MAEPLLEVRDLKKHFPvrgglfgrtvGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 82 TLNSTHQAEKL--GISIIFQE----LNlfPNMNVMDNI---FMANEFFQKGKINEKyqyalAKSLLERLELDVDPYT--P 150
Cdd:COG4608 83 TGLSGRELRPLrrRMQMVFQDpyasLN--PRMTVGDIIaepLRIHGLASKAERRER-----VAELLELVGLRPEHADryP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 151 LEELGiGHQQLVEIARALSKDTRVLIMDEPTSALSQS-EVKVLfNVIEQLKRR-GVTIIYISH----------R-----L 213
Cdd:COG4608 156 HEFSG-GQRQRIGIARALALNPKLIVCDEPVSALDVSiQAQVL-NLLEDLQDElGLTYLFISHdlsvvrhisdRvavmyL 233
|
250
....*....|....*
gi 496059540 214 EELMEIGDYITIFRD 228
Cdd:COG4608 234 GKIVEIAPRDELYAR 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-232 |
1.79e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL----- 92
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIrllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 GISIIFQELNLFPNMNVMDNIFMANefFQKGKINEKYQYALAKSLLERLELD--VDPYtPLEeLGIGHQQLVEIARALSK 170
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAP--CKVLGLSKEQAREKAMKLLARLRLTdkADRF-PLH-LSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-234 |
2.03e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.73 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISI 96
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMNVMDNIFMANEFFQ--KGKINEKyqyalakslLERLeldvdpytpLEELGIGH------QQL------- 161
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKlsKKEREER---------LEEL---------LEEFGITHlrkskaYSLsggerrr 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 162 VEIARALSKDTRVLIMDEPTSA---LSQSEVKvlfNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGvdpIAVADIQ---KIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-239 |
2.03e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.09 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ--AE 90
Cdd:COG1135 1 MIELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGISIIFQELNLFPNMNVMDNIFMANEF--FQKGKINEKyqyalAKSLLERLEL----DVDPytplEELGIGHQQLVEI 164
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIagVPKAEIRKR-----VAELLELVGLsdkaDAYP----SQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 165 ARALSKDTRVLIMDEPTSAL----SQSevkVLfNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:COG1135 152 ARALANNPKVLLCDEATSALdpetTRS---IL-DLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
285-491 |
6.63e-25 |
|
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: 101.11 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsrlkkglalVPEDRQGEGVVqmmsI 364
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE---------LPPLRRRIGMV----F 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QsnmtlsDFSLqgfrrawkwlNPHKeqaSVKAMIQqlaikvsdpqLPitsLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03229 83 Q------DFAL----------FPHL---TVLENIA----------LG---LSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059540 445 IDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGR 491
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-228 |
1.13e-24 |
|
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: 104.36 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYP---GVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESP---SSGQIIMDGIPVTLNSTHQA 89
Cdd:COG0444 1 LLEVRNLKVYFPtrrGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 EKL---GISIIFQE----LNlfPNMNVmDNIFManEFFQK-GKINEKYQYALAKSLLERLELD-----VDPYtPleelgi 156
Cdd:COG0444 81 RKIrgrEIQMIFQDpmtsLN--PVMTV-GDQIA--EPLRIhGGLSKAEARERAIELLERVGLPdperrLDRY-P------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 157 gHQ------QLVEIARALSKDTRVLIMDEPTSAL---SQSEVkvlFNVIEQLKR-RGVTIIYISHRLE------------ 214
Cdd:COG0444 149 -HElsggmrQRVMIARALALEPKLLIADEPTTALdvtIQAQI---LNLLKDLQReLGLAILFITHDLGvvaeiadrvavm 224
|
250
....*....|....*..
gi 496059540 215 ---ELMEIGDYITIFRD 228
Cdd:COG0444 225 yagRIVEEGPVEELFEN 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-274 |
1.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.96 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgIS 95
Cdd:PRK13652 3 LIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF-VG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQelnlfpnmNVMDNIFMA-----------NEFFQKGKINEKYQYALAKSLLERLeLDVDPYtpleELGIGHQQLVEI 164
Cdd:PRK13652 82 LVFQ--------NPDDQIFSPtveqdiafgpiNLGLDEETVAHRVSSALHMLGLEEL-RDRVPH----HLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 165 ARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDasip 243
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE---- 224
|
250 260 270
....*....|....*....|....*....|.
gi 496059540 244 wIIEQMVGDKKKHFDYQPAPKGETVLSVQGL 274
Cdd:PRK13652 225 -IFLQPDLLARVHLDLPSLPKLIRSLQAQGI 254
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-235 |
1.52e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 27 YPG-VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV---TLNSTHQAeklgISIIFQELN 102
Cdd:COG1132 349 YPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdlTLESLRRQ----IGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 103 LFpNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLE--LDvdpyTPLEELGI----GHQQLVEIARALSKDTRVLI 176
Cdd:COG1132 425 LF-SGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPdgYD----TVVGERGVnlsgGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 177 MDEPTSAL-SQSEVKVlFNVIEQLkRRGVTIIYISHRLEELMEiGDYITIFRDGRfISER 235
Cdd:COG1132 500 LDEATSALdTETEALI-QEALERL-MKGRTTIVIAHRLSTIRN-ADRILVLDDGR-IVEQ 555
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
268-492 |
1.94e-24 |
|
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: 101.43 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKA--HFQSRL 342
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 KKGLALVPEDrqgegvvQMMSIQSNMTLSDFSLQGFRRAwkwlNPHKEQASVKAMIQQLAIKVSDP-----QLPiTSLSG 417
Cdd:cd03257 81 RKEIQMVFQD-------PMSSLNPRMTIGEQIAEPLRIH----GKLSKKEARKEAVLLLLVGVGLPeevlnRYP-HELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 418 GNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
269-492 |
2.04e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 100.66 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTaLHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsRLKKGLAL 348
Cdd:COG4619 1 LELEGLS-FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP-EWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 349 VPEDrqgegvVQMMSiqsnMTLSDFslqgFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKA 428
Cdd:COG4619 79 VPQE------PALWG----GTVRDN----LPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 429 LMTQPQVVFLDEPTRGIDVGAKTDVYHLIGK-MAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-231 |
2.17e-24 |
|
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: 99.81 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRvyPGVValDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGI 94
Cdd:cd03215 2 EPVLEVRGLSV--KGAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SII----FQELnLFPNMNVMDNIFMAneffqkgkinekyqyalakSLLErleldvdpytpleelGiGHQQLVEIARALSK 170
Cdd:cd03215 78 AYVpedrKREG-LVLDLSVAENIALS-------------------SLLS---------------G-GNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 171 DTRVLIMDEPTSAL---SQSEVkvlFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRF 231
Cdd:cd03215 122 DPRVLILDEPTRGVdvgAKAEI---YRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-241 |
2.34e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.45 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 22 DLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISIIFQEL 101
Cdd:TIGR03410 5 NLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 102 NLFPNMNVMDNIFMANEFFQKG--KINEkYQYAL---AKSLLERLELDvdpytpleeLGIGHQQLVEIARALSKDTRVLI 176
Cdd:TIGR03410 85 EIFPRLTVEENLLTGLAALPRRsrKIPD-EIYELfpvLKEMLGRRGGD---------LSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 177 MDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDAS 241
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLrAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELD 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
18-232 |
2.39e-24 |
|
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: 100.73 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVyRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGisII 97
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG--YL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDniFMANEFFQKGkINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:cd03264 78 PQEFGVYPNFTVRE--FLDYIAWLKG-IPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKrRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-232 |
2.55e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 100.74 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGI------PVTLNSthqa 89
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldPADLRR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 eklGISIIFQELNLFpNMNVMDNIFMANeffqkgkinekyQYALAKSLLERLEL-DVDPYTPL-------------EELG 155
Cdd:cd03245 79 ---NIGYVPQDVTLF-YGTLRDNITLGA------------PLADDERILRAAELaGVTDFVNKhpngldlqigergRGLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 156 IGHQQLVEIARALSKDTRVLIMDEPTSALSQ-SEVKvlfnVIEQLKR--RGVTIIYISHRLeELMEIGDYITIFRDGRFI 232
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMnSEER----LKERLRQllGDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
31-230 |
3.38e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.65 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 31 VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEklgISIIFQELNLFPNMNVM 110
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 111 DNI----FMANefFQKGKINEKYQYALAKSLLERLEldvDPYtpLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQ 186
Cdd:PRK11432 97 ENVgyglKMLG--VPKEERKQRVKEALELVDLAGFE---DRY--VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059540 187 SEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:PRK11432 170 NLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
48-239 |
5.06e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.21 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnSTHQAEKlGISIIFQELNLFPNMNVMDNIFMA-------NEfF 120
Cdd:COG3840 30 ILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAER-PVSMLFQENNLFPHLTVAQNIGLGlrpglklTA-E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 121 QKGKINEkyqyALAK----SLLERLeldvdPytplEELGIGHQQLVEIARALSKDTRVLIMDEPTSALS---QSEVKVLf 193
Cdd:COG3840 106 QRAQVEQ----ALERvglaGLLDRL-----P----GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalRQEMLDL- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496059540 194 nVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:COG3840 172 -VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
283-492 |
7.66e-24 |
|
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: 99.29 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 283 YKLNDVTFSLS---KGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahFQSRlkKGLALVPEDRQGEGVV 359
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL----FDSR--KKINLPPQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 QMMSIQSNMTLSDFSLQGFRRawkwLNPHKEQASVKAMIQQLAIkvsDPQL--PITSLSGGNQQKVVLGKALMTQPQVVF 437
Cdd:cd03297 82 QQYALFPHLNVRENLAFGLKR----KRNREDRISVDELLDLLGL---DHLLnrYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 438 LDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
285-495 |
8.77e-24 |
|
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: 99.54 E-value: 8.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLALVPedrqgegvvQMMSI 364
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLP---------QEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLQGFRRAWKwlnPHKEQAS-VKAMIQQLAIKVSDPQLPItSLSGGNQQKVVLGKALMTQPQVVFLDEPTR 443
Cdd:cd03218 87 FRKLTVEENILAVLEIRGL---SKKEREEkLEELLEEFHITHLRKSKAS-SLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 444 GIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
285-493 |
9.31e-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: 98.87 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGeciDKAHFQSRLKKGlALVPED--RQgegvVQMM 362
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSI-GYVMQDvdYQ----LFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLSDfslqgfrrawkwLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFLDEPT 442
Cdd:cd03226 88 SVREELLLGL------------KELDAGNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 443 RGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRIT 493
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
285-494 |
1.10e-23 |
|
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: 99.50 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfQSRLKkglalvpEDRQGEGVVqmmsI 364
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-EAELY-------RLRRRMGML----F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSN-----MTLSD---FSLQGFRRawkwLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVV 436
Cdd:cd03261 84 QSGalfdsLTVFEnvaFPLREHTR----LSEEEIREIVLEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 437 FLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-235 |
1.94e-23 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 98.84 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV---TLNSTHQAekl 92
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 gISIIFQELNLFpNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELGI----GHQQLVEIARAL 168
Cdd:cd03251 78 -IGLVSQDVFLF-NDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYD--TVIGERGVklsgGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 169 SKDTRVLIMDEPTSAL-SQSEvKVLFNVIEQL-KRRgvTIIYISHRLEELMEIgDYITIFRDGRfISER 235
Cdd:cd03251 154 LKDPPILILDEATSALdTESE-RLVQAALERLmKNR--TTFVIAHRLSTIENA-DRIVVLEDGK-IVER 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
269-506 |
1.96e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 98.79 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI----DKAHFQSRLKK 344
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 345 G-----LALVPEDRQGEGVvqMMSIQSNMTLsdfslqgFRRAWKWLNPHKEQASVKA-----MIQQLAIKVSdpqlpitS 414
Cdd:cd03256 81 GmifqqFNLIERLSVLENV--LSGRLGRRST-------WRSLFGLFPKEEKQRALAAlervgLLDKAYQRAD-------Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRIT 493
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
250
....*....|...
gi 496059540 494 ADVPRHAVTRETL 506
Cdd:cd03256 225 FDGPPAELTDEVL 237
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
285-491 |
1.96e-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: 96.55 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsRLKKGLALVPEdrqgegvvqmmsi 364
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 qsnmtlsdfslqgfrrawkwlnphkeqasvkamiqqlaikvsdpqlpitsLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496059540 445 IDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGR 491
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-232 |
3.67e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.91 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVV--ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQAE 90
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGisIIFQEL-NLFPNMNVMDNI-F-MANEFFQKGKINEKYQYALAKSLLERLeLDVDPytplEELGIGHQQLVEIARA 167
Cdd:PRK13632 84 KIG--IIFQNPdNQFIGATVEDDIaFgLENKKVPPKKMKDIIDDLAKKVGMEDY-LDKEP----QNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 168 LSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGV-TIIYISHRLEELMeIGDYITIFRDGRFI 232
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLI 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-239 |
4.04e-23 |
|
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: 100.56 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDsVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipVTLNSTHQ-----AEKLGISIIFQELNLFPN 106
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG--EVLQDSARgiflpPHRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 107 MNVMDNIfmaneffqkgkineKYQYALAKSLLERLELD-VdpytpLEELGIGH-------------QQLVEIARALSKDT 172
Cdd:COG4148 92 LSVRGNL--------------LYGRKRAPRAERRISFDeV-----VELLGIGHlldrrpatlsggeRQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 173 RVLIMDEPTSALSQ---SEvkvLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:COG4148 153 RLLLMDEPLAALDLarkAE---ILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
40-230 |
4.10e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 97.18 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 40 VYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsTHQAEKLGISIIFQELNLFPNMNVMDNIFMANEf 119
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT---AAPPADRPVSMLFQENNLFAHLTVEQNVGLGLS- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 120 fQKGKINEKYQYALaKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQL 199
Cdd:cd03298 97 -PGLKLTAEDRQAI-EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|..
gi 496059540 200 KR-RGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03298 175 HAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-232 |
4.38e-23 |
|
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: 102.54 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 8 TPHSVESEVIIETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNS 85
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 86 THQAEKLgISIIFQELNLFpNMNVMDNIFMANEffqkGKINEKYQYALAK----SLLERLE--LDvdpyTPLEELGI--- 156
Cdd:COG4987 404 EDDLRRR-IAVVPQRPHLF-DTTLRENLRLARP----DATDEELWAALERvglgDWLAALPdgLD----TWLGEGGRrls 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 157 -GHQQLVEIARALSKDTRVLIMDEPTSAL-SQSEVKVLFNVIEQLKRRgvTIIYISHRLEELmEIGDYITIFRDGRFI 232
Cdd:COG4987 474 gGERRRLALARALLRDAPILLLDEPTEGLdAATEQALLADLLEALAGR--TVLLITHRLAGL-ERMDRILVLEDGRIV 548
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-239 |
4.43e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 98.23 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQiimdgiPVTLnsthQAEKLG- 93
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN------DVRL----FGERRGg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ---------ISIIFQELNLF--PNMNVMD--------NIFMANEFfqkgkinEKYQYALAKSLLERLELDVDPYTPLEEL 154
Cdd:COG1119 71 edvwelrkrIGLVSPALQLRfpRDETVLDvvlsgffdSIGLYREP-------TDEQRERARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 155 GIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRG-VTIIYISHRLEelmEIGDYIT---IFRDGR 230
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVE---EIPPGIThvlLLKDGR 220
|
....*....
gi 496059540 231 FISERPVND 239
Cdd:COG1119 221 VVAAGPKEE 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
278-494 |
6.79e-23 |
|
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: 99.79 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 278 HPSGGYKLnDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahFQSRlkKGLALVPEDRQgEG 357
Cdd:COG4148 9 LRRGGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL----QDSA--RGIFLPPHRRR-IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 358 VV-Q------MMSIQSNMTLsdfslqGFRRAWKwlnpHKEQASVKAMIQQLAIkvsDPQL--PITSLSGGNQQKVVLGKA 428
Cdd:COG4148 81 YVfQearlfpHLSVRGNLLY------GRKRAPR----AERRISFDEVVELLGI---GHLLdrRPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 429 LMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-215 |
7.57e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.01 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 22 DLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSthqAEKlgiSII 97
Cdd:COG4525 8 HVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG---ADR---GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIfmanEF-FQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLI 176
Cdd:COG4525 82 FQKDALLPWLNVLDNV----AFgLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059540 177 MDEPTSAL---SQSEVKVLfnVIEQLKRRGVTIIYISHRLEE 215
Cdd:COG4525 158 MDEPFGALdalTREQMQEL--LLDVWQRTGKGVFLITHSVEE 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-501 |
8.56e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.86 E-value: 8.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 9 PHS--VESEVIIETHDLSRVY----PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGI--- 79
Cdd:PRK10261 2 PHSdeLDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 80 -----PVTLNSTHQAEKLG-----ISIIFQE--LNLFPNMNVMDNIFMANEFFQKgkINEKYQYALAKSLLERLELDvDP 147
Cdd:PRK10261 82 rrsrqVIELSEQSAAQMRHvrgadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQG--ASREEAMVEAKRMLDQVRIP-EA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 148 YTPL----EELGIGHQQLVEIARALSKDTRVLIMDEPTSALS---QSEVKVLFNVIEQLKRRGVtiIYISHRLEELMEIG 220
Cdd:PRK10261 159 QTILsrypHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSMGV--IFITHDMGVVAEIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 221 DYITIFRDGRFISERPVND--------------ASIPWIIEQMVGDKKKHFDY----QPAPK-----------GETVLSV 271
Cdd:PRK10261 237 DRVLVMYQGEAVETGSVEQifhapqhpytrallAAVPQLGAMKGLDYPRRFPLisleHPAKQeppieqdtvvdGEPILQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 272 QGLTALHPSGGYKLNDVT----------FSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDkahfqsr 341
Cdd:PRK10261 317 RNLVTRFPLRSGLLNRVTrevhavekvsFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 342 LKKGLALVPEDRQGEGVVQ--MMSIQSNMTLSDfSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPITSLSGGN 419
Cdd:PRK10261 390 TLSPGKLQALRRDIQFIFQdpYASLDPRQTVGD-SIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 420 QQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITADVPR 498
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
|
...
gi 496059540 499 HAV 501
Cdd:PRK10261 549 RAV 551
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
37-230 |
8.72e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 96.47 E-value: 8.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 37 NYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEklgISIIFQELNLFPNMNVMDNIFMA 116
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP---VSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 117 NE------FFQKGKINEKYQYALAKSLLERLEldvdpytplEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVK 190
Cdd:TIGR01277 95 LHpglklnAEQQEKVVDAAQQVGIADYLDRLP---------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496059540 191 VLFNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:TIGR01277 166 EMLALVKQLcSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-230 |
1.21e-22 |
|
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: 94.59 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVA--LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPvtLNSTHQAEKLG-I 94
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD--ISQWDPNELGDhV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNmNVMDNIFMAneffqkgkinekyqyalaksllerleldvdpytpleelgiGHQQLVEIARALSKDTRV 174
Cdd:cd03246 79 GYLPQDDELFSG-SIAENILSG----------------------------------------GQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 175 LIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLeELMEIGDYITIFRDGR 230
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
285-492 |
1.34e-22 |
|
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: 95.66 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqsrlkkgLALVPEDR------QGEGV 358
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV------------TGVPPERRnigmvfQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 359 VQMMSIQSNMtlsDFSL--QGFRRAwkwlnphKEQASVKAMIQQLAIkvsDPQL--PITSLSGGNQQKVVLGKALMTQPQ 434
Cdd:cd03259 84 FPHLTVAENI---AFGLklRGVPKA-------EIRARVRELLELVGL---EGLLnrYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 435 VVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
285-442 |
1.55e-22 |
|
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: 93.87 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSrLKKGLALVPEDRQgegVVQMMSI 364
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS-LRKEIGYVFQDPQ---LFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSdFSLQGFRRAWKWlnphkeqASVKAMIQQLAIKVSDPQLP---ITSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:pfam00005 77 RENLRLG-LLLKGLSKREKD-------ARAEEALEKLGLGDLADRPVgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
.
gi 496059540 442 T 442
Cdd:pfam00005 149 T 149
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
285-495 |
2.03e-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: 93.65 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEcidKAHFQSrlkkglalvPEDRQGEGVvqmmsi 364
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK---EVSFAS---------PRDARRAGI------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 qsnmtlsdfslqgfrrawkwlnphkeqasvkAMIQQLaikvsdpqlpitslSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03216 78 -------------------------------AMVYQL--------------SVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 445 IDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-495 |
3.58e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEvigIYGLLG---AGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfqsrlKKGLALVPEDRqgegvvqm 361
Cdd:COG4152 17 VDDVSFTVPKGE---IFGLLGpngAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-----RRRIGYLPEER-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 mSIQSNMTLSDF-----SLQGfrrawkwLNPHKEQASVKAMIQQLAI------KVSDpqlpitsLSGGNQQKVVLGKALM 430
Cdd:COG4152 81 -GLYPKMKVGEQlvylaRLKG-------LSKAEAKRRADEWLERLGLgdrankKVEE-------LSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 431 TQPQVVFLDEPTRGID-VGAKTdVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:COG4152 146 HDPELLILDEPFSGLDpVNVEL-LKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-235 |
5.64e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 94.60 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVY-PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIP---VTLNSTHQAeklg 93
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDireVTLDSLRRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFpNMNVMDNIfmaneffQKGKIN----EKYQYALAKSLLERLELDVDPY-TPLEELGI----GHQQLVEI 164
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNI-------RYGRPDatdeEVIEAAKAAQIHDKIMRFPDGYdTIVGERGLklsgGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 165 ARALSKDTRVLIMDEPTSAL-SQSEVKVLFNVIEQLKRRgvTIIYISHRLEELMEiGDYITIFRDGRfISER 235
Cdd:cd03253 149 ARAILKNPPILLLDEATSALdTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGR-IVER 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-234 |
5.85e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.56 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 16 VIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGIS 95
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFPNMNVMDNIFMANEFFQKGKINEKYQ--YALAKSLLERleldvdpytPLEELGI---GHQQLVEIARALSK 170
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKwvYELFPRLHER---------RIQRAGTmsgGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
153-506 |
1.16e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 153 ELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRF 231
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 232 ISERP----VNDASIPWIieQMVGDKKKHFDYQPAPKG-ETVLSVQGLTALHP--------SGGYK--LNDVTFSLSKGE 296
Cdd:PRK15134 236 VEQNRaatlFSAPTHPYT--QKLLNSEPSGDPVPLPEPaSPLLDVEQLQVAFPirkgilkrTVDHNvvVKNISFTLRPGE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 297 VIGIYGLLGAGRTELFKGLVGLMPCQsGSVQLNGECIDkaHFQSRlkkglALVPEDRQGEGVVQ--MMSIQSNMTLSDFS 374
Cdd:PRK15134 314 TLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLH--NLNRR-----QLLPVRHRIQVVFQdpNSSLNPRLNVLQII 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 375 LQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVY 454
Cdd:PRK15134 386 EEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 455 HLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITA--------DVPRHAVTRETL 506
Cdd:PRK15134 466 ALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEqgdcervfAAPQQEYTRQLL 526
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
285-506 |
1.29e-21 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 95.15 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGL----ALVPEDRQGEGVVQ 360
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIvpqyASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSiqsnmtlsdfSLQGFRRAWKwlnphkeQASVKAMIQQLAIKVSDPQlPITSLSGGNQQKVVLGKALMTQPQVVFLDE 440
Cdd:TIGR01188 89 MMG----------RLYGLPKDEA-------EERAEELLELFELGEAADR-PVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 441 PTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA-DVP---RHAVTRETL 506
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAeGTPeelKRRLGKDTL 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
29-232 |
2.12e-21 |
|
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: 92.93 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 29 GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV-TLNSTHQAEKLGisIIFQELNLFpNM 107
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVG--VVLQENVLF-NR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 108 NVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELGI----GHQQLVEIARALSKDTRVLIMDEPTSA 183
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYD--TIVGEQGAglsgGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059540 184 LS-QSEVKVLFNVIEQLKRRgvTIIYISHRLEELMEiGDYITIFRDGRFI 232
Cdd:cd03252 169 LDyESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
285-509 |
2.19e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSrLKKGLALVPEDR------QGEGV 358
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA-ASRRVASVPQDTslsfefDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 359 VQM-----MSIQSNMTLSDfslqgfRRAwkwlnphKEQASVKAMIQQLAIKvsdpqlPITSLSGGNQQKVVLGKALMTQP 433
Cdd:PRK09536 98 VEMgrtphRSRFDTWTETD------RAA-------VERAMERTGVAQFADR------PVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 434 QVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRIT-ADVPRHAVTRETLIAA 509
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRaAGPPADVLTADTLRAA 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-232 |
3.05e-21 |
|
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: 92.40 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 25 RVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQI-IMDGIPVTLNSTHQAEklgISIIF-QELN 102
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRKKFLRR---IGVVFgQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 103 LFPNMNVMDNIFMANEFFQKGKinEKYQYALAKsLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTS 182
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPP--ARFKKRLDE-LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 183 AL---SQSEVKvlfNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:cd03267 183 GLdvvAQENIR---NFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-232 |
3.43e-21 |
|
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: 96.80 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVY----PGVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIM----DGIPVT--- 82
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 83 LNSTHQAEKLgISIIFQELNLFPNMNVMDNIFMA------NEFFQKGKI--------NEKYqyalAKSLLERLEldvdpy 148
Cdd:TIGR03269 357 PDGRGRAKRY-IGILHQEYDLYPHRTVLDNLTEAiglelpDELARMKAVitlkmvgfDEEK----AEEILDKYP------ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 149 tplEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQ-SEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFR 227
Cdd:TIGR03269 426 ---DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
....*
gi 496059540 228 DGRFI 232
Cdd:TIGR03269 503 DGKIV 507
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
47-232 |
3.61e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.38 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 47 VLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLnSTHQAEKLG------ISIIFQELNLFPNMNVMDNIFMANefF 120
Cdd:PRK11124 32 VLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDF-SKTPSDKAIrelrrnVGMVFQQYNLWPHLTVQQNLIEAP--C 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 121 QKGKINEKYQYALAKSLLERLELD--VDPYtPLEeLGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQ 198
Cdd:PRK11124 109 RVLGLSKDQALARAEKLLERLRLKpyADRF-PLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE 186
|
170 180 190
....*....|....*....|....*....|....
gi 496059540 199 LKRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:PRK11124 187 LAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
260-509 |
5.53e-21 |
|
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: 96.37 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 260 QPAPKGETV-LSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHF 338
Cdd:COG4988 327 APLPAAGPPsIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING--VDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 339 -QSRLKKGLALVPedrQGEGVVQMmSIQSNMTLS--DFSLQGFRRAwkwLnphkEQASVKAMIQQLaikvsdPQ---LPI 412
Cdd:COG4988 405 dPASWRRQIAWVP---QNPYLFAG-TIRENLRLGrpDASDEELEAA---L----EAAGLDEFVAAL------PDgldTPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 413 TS----LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAqQGLAVMFSSSELdEVMALADRILVMA 488
Cdd:COG4988 468 GEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRL-ALLAQADRILVLD 545
|
250 260
....*....|....*....|.
gi 496059540 489 DGRITAdvprhAVTRETLIAA 509
Cdd:COG4988 546 DGRIVE-----QGTHEELLAK 561
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-229 |
6.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEK 91
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 92 lGISIIFQEL-NLFPNMNVMDNIFMANEFFQKGkiNEKYQYALAKSLLERLELDVDPYTPlEELGIGHQQLVEIARALSK 170
Cdd:PRK13648 84 -HIGIVFQNPdNQFVGSIVKYDVAFGLENHAVP--YDEMHRRVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKR-RGVTIIYISHRLEELMEiGDYITIFRDG 229
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-236 |
7.21e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 7.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV-TLNSTHQA-- 89
Cdd:PRK10535 4 LLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVaTLDADALAql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 --EKLGIsiIFQELNLFPNMNVMDNIFMANEFFQKGKineKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARA 167
Cdd:PRK10535 84 rrEHFGF--IFQRYHLLSHLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 168 LSKDTRVLIMDEPTSAL-SQSEVKVLfNVIEQLKRRGVTIIYISH------RLEELMEIgdyitifRDGRFISERP 236
Cdd:PRK10535 159 LMNGGQVILADEPTGALdSHSGEEVM-AILHQLRDRGHTVIIVTHdpqvaaQAERVIEI-------RDGEIVRNPP 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-211 |
8.81e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 90.96 E-value: 8.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 11 SVESEVIIETHDLSRVYPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LN- 84
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaLDe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 85 ---STHQAEKLGisIIFQELNLFPNMNVMDNIFMANEFFqkgkiNEKYQYALAKSLLERLELD--VDPYtPlEELGIGHQ 159
Cdd:COG4181 82 darARLRARHVG--FVFQSFQLLPTLTALENVMLPLELA-----GRRDARARARALLERVGLGhrLDHY-P-AQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 160 QLVEIARALSKDTRVLIMDEPTSALSQSEVKVlfnVIEQL----KRRGVTIIYISH 211
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQ---IIDLLfelnRERGTTLVLVTH 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-236 |
9.61e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.35 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV-TLNSTHQAEKL---- 92
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 --GISIIFQELNLFPNMNVMDNIfMANEFFQKGKINEKYQyALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSK 170
Cdd:PRK11264 84 rqHVGFVFQNFNLFPHRTVLENI-IEGPVIVKGEPKEEAT-ARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERP 236
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-234 |
2.03e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.95 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlNSTHQAEKLGIS 95
Cdd:PRK13647 4 IIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELN--LFpNMNVMDNIFMA--NEFFQKGKINEKYQYALAKSLLERLElDVDPYtpleELGIGHQQLVEIARALSKD 171
Cdd:PRK13647 83 LVFQDPDdqVF-SSTVWDDVAFGpvNMGLDKDEVERRVEEALKAVRMWDFR-DKPPY----HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 172 TRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-235 |
2.05e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.70 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV---TLNSTHQAekl 92
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLASLRNQ--- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 gISIIFQELNLFpNMNVMDNI-FMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELGI----GHQQLVEIARA 167
Cdd:PRK11176 419 -VALVSQNVHLF-NDTIANNIaYARTEQYSREQIEEAARMAYAMDFINKMDNGLD--TVIGENGVllsgGQRQRIAIARA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 168 LSKDTRVLIMDEPTSAL-SQSEVKVLFNVIEQLKRRgvTIIYISHRLEELmEIGDYITIFRDGRfISER 235
Cdd:PRK11176 495 LLRDSPILILDEATSALdTESERAIQAALDELQKNR--TSLVIAHRLSTI-EKADEILVVEDGE-IVER 559
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-230 |
2.19e-20 |
|
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: 89.84 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVY---PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNStHQAEKLG 93
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNmNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELdvDPYTPLEELGI----GHQQLVEIARALS 169
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELAS--GYDTEVGEKGSqlsgGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 170 KDTRVLIMDEPTSAL-SQSEVKVLFNVIEQLKRRgvTIIYISHRLeELMEIGDYITIFRDGR 230
Cdd:cd03248 167 RNPQVLILDEATSALdAESEQQVQQALYDWPERR--TVLVIAHRL-STVERADQILVLDGGR 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-232 |
2.36e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.48 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 8 TPHSVESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKML-------AGVEspSSGQIIMDGIP 80
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 81 VTLNSTHQAE---KLGisIIFQELNLFPnMNVMDNIFMA---NEFFQKGKINEKYQYALAKSLL-----ERLEldvDPYT 149
Cdd:COG1117 80 IYDPDVDVVElrrRVG--MVFQKPNPFP-KSIYDNVAYGlrlHGIKSKSELDEIVEESLRKAALwdevkDRLK---KSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 150 pleELGIGHQQLVEIARALSKDTRVLIMDEPTSAL-SQSEVKV--LfnvIEQLKRRgVTIIYISHRLEELMEIGDYITIF 226
Cdd:COG1117 154 ---GLSGGQQQRLCIARALAVEPEVLLMDEPTSALdPISTAKIeeL---ILELKKD-YTIVIVTHNMQQAARVSDYTAFF 226
|
....*.
gi 496059540 227 RDGRFI 232
Cdd:COG1117 227 YLGELV 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
285-495 |
2.64e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 89.70 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecidkahfqsrlkkglaLVPEDRQgEGVVQMMSI 364
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----------------LVPWKRR-KKFLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 ---QSNMTLSDFS-LQGFR--RAWKWLNPHKEQASVKAMIQQLAI-KVSDpqLPITSLSGGNQQKVVLGKALMTQPQVVF 437
Cdd:cd03267 99 vfgQKTQLWWDLPvIDSFYllAAIYDLPPARFKKRLDELSELLDLeELLD--TPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 438 LDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-233 |
7.66e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 7.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISI 96
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMNVMDNIFMANEFfqKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLI 176
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQI--RDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 177 MDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFIS 233
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-234 |
7.70e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAE-KLGI 94
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELN--LFPNMNVMDNIFMA-NEFFQKGKINEKYQYALAKSLLERLEldvdpYTPLEELGIGHQQLVEIARALSKD 171
Cdd:PRK13636 85 GMVFQDPDnqLFSASVYQDVSFGAvNLKLPEDEVRKRVDNALKRTGIEHLK-----DKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 172 TRVLIMDEPTSALSQ---SEVKVLfnVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK13636 160 PKVLVLDEPTAGLDPmgvSEIMKL--LVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-239 |
8.40e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGV-----ESPSSGQIIMDGIPVTLNSTHQAEKL 92
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 gISIIFQELNLFPNMNVMDNIFMA---NEFFQ-KGKINEKYQYALAKS-LLERLELDVDpyTPLEELGIGHQQLVEIARA 167
Cdd:PRK14247 84 -VQMVFQIPNPIPNLSIFENVALGlklNRLVKsKKELQERVRWALEKAqLWDEVKDRLD--APAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 168 LSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRgVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
267-507 |
8.84e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 267 TVLSVQGLTAlhpsgGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkAHFQSR- 341
Cdd:PRK11231 1 MTLRTENLTV-----GYGtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSRq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 342 LKKGLALVPEDR---QGEGVVQMMSIQSNMTLSdfslqgfrrAWKWLNPHKEQASVKAM----IQQLAIKvsdpqlPITS 414
Cdd:PRK11231 74 LARRLALLPQHHltpEGITVRELVAYGRSPWLS---------LWGRLSAEDNARVNQAMeqtrINHLADR------RLTD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
250
....*....|...
gi 496059540 495 DVPRHAVTRETLI 507
Cdd:PRK11231 219 QGTPEEVMTPGLL 231
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-234 |
1.03e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 88.64 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 11 SVESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAE 90
Cdd:COG4674 4 DTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGISIIFQELNLFPNMNVMDNIFMA---------NEFF-----QKGKINEkyqyalaksLLERLELDVDPYTPLEELGI 156
Cdd:COG4674 84 RLGIGRKFQKPTVFEELTVFENLELAlkgdrgvfaSLFArltaeERDRIEE---------VLETIGLTDKADRLAGLLSH 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 157 GHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLkRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:COG4674 155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSL-AGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAE 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-232 |
1.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.34 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVY-PGV----VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT---LNSTHQA 89
Cdd:PRK13637 3 IKIENLTHIYmEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 EKLGISIIFQELNLFPNMNVMDNIF-MANEFFQKGKINEKyqyalAKSLLERLELDVDPY---TPLEELGiGHQQLVEIA 165
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFgPINLGLSEEEIENR-----VKRAMNIVGLDYEDYkdkSPFELSG-GQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 166 RALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
33-229 |
1.20e-19 |
|
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: 87.91 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAeklgisIIFQELNLFPNMNVMDN 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM------VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFMANEFFQKgKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEP---TSALSQSEV 189
Cdd:TIGR01184 75 IALAVDRVLP-DLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPfgaLDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 496059540 190 K-VLFNVIEQlkrRGVTIIYISHRLEELMEIGDYITIFRDG 229
Cdd:TIGR01184 154 QeELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-215 |
1.54e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.22 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 23 LSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSthqAEKlgiSIIFQELN 102
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---AER---GVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 103 LFPNMNVMDNIfmanEF-FQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPT 181
Cdd:PRK11248 81 LLPWRNVQDNV----AFgLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*
gi 496059540 182 SALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEE 215
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEE 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
285-494 |
1.67e-19 |
|
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: 87.04 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLalvpedrqgegVVQMMSI 364
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI-----------VFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMT-LSDFSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKvsdpQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTR 443
Cdd:cd03265 85 DDELTgWENLYIHARLYGVPGAERRERIDELLDFVGLLEAA----DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 444 GIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
281-492 |
1.69e-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: 87.39 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 281 GGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahfqsrlkkglaLVPEDRQGEGVVQ 360
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN------------LPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSIQSNMTLSDFSLQGFRrawKWLNPHKE-QASVKAMIQQLAIKVSDPQLPITsLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLK---KRKVDKKEiERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 440 EPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-234 |
2.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGIS 95
Cdd:PRK13644 1 MIRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNL-FPNMNVMDNIFMANE--FFQKGKINEKYQYALAKSLLERLEldvdpYTPLEELGIGHQQLVEIARALSKDT 172
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPEnlCLPPIEIRKRVDRALAEIGLEKYR-----HRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELmEIGDYITIFRDGRFISE 234
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLE 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-232 |
3.07e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.75 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 3 QQDIVTPHSVESEVIIETHDLSRVYPG-----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMD 77
Cdd:PRK13631 7 KKKLKVPNPLSDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 78 GI-------PVTLNSTHQAEKLG--------ISIIFQ--ELNLFPNMNVMDNIFMANEFFQ-KGKINEKYQYALAKSLLE 139
Cdd:PRK13631 87 DIyigdkknNHELITNPYSKKIKnfkelrrrVSMVFQfpEYQLFKDTIEKDIMFGPVALGVkKSEAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 140 RLELDVDPYtpleELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEI 219
Cdd:PRK13631 167 DSYLERSPF----GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEV 242
|
250
....*....|...
gi 496059540 220 GDYITIFRDGRFI 232
Cdd:PRK13631 243 ADEVIVMDKGKIL 255
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-232 |
4.00e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.41 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGI---PVTLNSTHQAeklg 93
Cdd:PRK13657 335 VEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirTVTRASLRRN---- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFpNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELGI----GHQQLVEIARALS 169
Cdd:PRK13657 411 IAVVFQDAGLF-NRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYD--TVVGERGRqlsgGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 170 KDTRVLIMDEPTSAL-SQSEVKVLfNVIEQLkRRGVTIIYISHRLEELMEiGDYITIFRDGRFI 232
Cdd:PRK13657 488 KDPPILILDEATSALdVETEAKVK-AALDEL-MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
48-213 |
4.60e-19 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 90.77 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMDGIP-------VTLNSthqaeklgISIIFQELNLFPNmNVMDNIFMANeff 120
Cdd:TIGR03796 510 LVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPreeipreVLANS--------VAMVDQDIFLFEG-TVRDNLTLWD--- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 121 qkGKINEKyqyALAKSLLERLELDV-----DPY-TPLEELGI----GHQQLVEIARALSKDTRVLIMDEPTSAL-SQSEV 189
Cdd:TIGR03796 578 --PTIPDA---DLVRACKDAAIHDVitsrpGGYdAELAEGGAnlsgGQRQRLEIARALVRNPSILILDEATSALdPETEK 652
|
170 180
....*....|....*....|....
gi 496059540 190 KVLFNvieqLKRRGVTIIYISHRL 213
Cdd:TIGR03796 653 IIDDN----LRRRGCTCIIVAHRL 672
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-234 |
4.74e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV-TLNSTHQAE----KLGisIIFQELNLFPNM 107
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAElrnqKLG--FIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 108 NVMDNIFMAnefFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQS 187
Cdd:PRK11629 103 TALENVAMP---LLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059540 188 EVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIfRDGRFISE 234
Cdd:PRK11629 180 NADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAE 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
30-218 |
4.78e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.95 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIM--DGIPVTLNSTHQAEKLG-----ISIIFQELN 102
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILAlrrrtIGYVSQFLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 103 LFPNMNVMDniFMANEFFQKGkINEKYQYALAKSLLERLELDvdpytplEEL---------GiGHQQLVEIARALSKDTR 173
Cdd:COG4778 104 VIPRVSALD--VVAEPLLERG-VDREEARARARELLARLNLP-------ERLwdlppatfsG-GEQQRVNIARGFIADPP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059540 174 VLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRlEELME 218
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHD-EEVRE 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-223 |
5.33e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 90.04 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGV-VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlGISI 96
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNmNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEE----LGIGHQQLVEIARALSKDT 172
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLD--TPIGEggagLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 173 RVLIMDEPTSAL-SQSEVKVLFNViEQLkRRGVTIIYISHRLeELMEIGDYI 223
Cdd:TIGR02857 478 PLLLLDEPTAHLdAETEAEVLEAL-RAL-AQGRTVLLVTHRL-ALAALADRI 526
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-235 |
5.52e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 86.05 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP---GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPV-TLNSTHQAEKLG 93
Cdd:cd03249 1 IEFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 IsiIFQELNLFpNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLEldvDPY-TPLEELGI----GHQQLVEIARAL 168
Cdd:cd03249 81 L--VSQEPVLF-DGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLP---DGYdTLVGERGSqlsgGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 169 SKDTRVLIMDEPTSAL-SQSEvKVLFNVIEQLkRRGVTIIYISHRLEELMEiGDYITIFRDGRfISER 235
Cdd:cd03249 155 LRNPKILLLDEATSALdAESE-KLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ-VVEQ 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-234 |
5.89e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.06 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAE-KLGI 94
Cdd:PRK13639 1 ILETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQelnlfpnmNVMDNIFMA-----------NEFFQKGKINEKYQYALAKSLLERLEldvdpYTPLEELGIGHQQLVE 163
Cdd:PRK13639 81 GIVFQ--------NPDDQLFAPtveedvafgplNLGLSKEEVEKRVKEALKAVGMEGFE-----NKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 164 IARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
269-492 |
5.96e-19 |
|
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: 84.19 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGG-YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfQSRLKKGLA 347
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD-PNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 LVPEDrqgegvVQMM--SIQSNMtlsdfslqgfrrawkwlnphkeqasvkamiqqlaikvsdpqlpitsLSGGNQQKVVL 425
Cdd:cd03246 80 YLPQD------DELFsgSIAENI----------------------------------------------LSGGQRQRLGL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 426 GKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELdEVMALADRILVMADGRI 492
Cdd:cd03246 108 ARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-231 |
6.34e-19 |
|
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: 90.84 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 29 GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLGISIifQELNLFPNMN 108
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCP--QHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 109 VMDNIFMANEFfqKGKINEKYQYALaKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSE 188
Cdd:TIGR01257 1020 VAEHILFYAQL--KGRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496059540 189 VKVLFNVIeqLK-RRGVTIIYISHRLEELMEIGDYITIFRDGRF 231
Cdd:TIGR01257 1097 RRSIWDLL--LKyRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
266-497 |
6.75e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.48 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqSRL 342
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI------SSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 K-KGLA---------------LVPEdrqgegvvqmMSIQSNMTLSdFSLQGFRRAwkwlnphKEQASVKAMIQQLAIKVS 406
Cdd:COG1136 76 SeRELArlrrrhigfvfqffnLLPE----------LTALENVALP-LLLAGVSRK-------ERRERARELLERVGLGDR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 407 DPQLPiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELdEVMALADRIL 485
Cdd:COG1136 138 LDHRP-SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDP-ELAARADRVI 215
|
250
....*....|..
gi 496059540 486 VMADGRITADVP 497
Cdd:COG1136 216 RLRDGRIVSDER 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-211 |
9.80e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVY-PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL--G 93
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLrrQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQELNLFPNMNVMDNIFMAneFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGiGHQQLVEIARALSKDTR 173
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIP--LIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSG-GEQQRVGIARAVVNKPA 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059540 174 VLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISH 211
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
266-494 |
1.05e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTALHP-SGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAH-FQSRLK 343
Cdd:PRK13635 3 EEIIRVEHISFRYPdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 344 KGLALVPEDRQGEGVvqmmsiqsnmTLSD---FSL--QGFrrawkwlnPHKE-QASVKAMIQQLAIKVSDPQLPiTSLSG 417
Cdd:PRK13635 83 VGMVFQNPDNQFVGA----------TVQDdvaFGLenIGV--------PREEmVERVDQALRQVGMEDFLNREP-HRLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 418 GNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVmALADRILVMADGRITA 494
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEA-AQADRVIVMNKGEILE 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
269-497 |
1.06e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 84.83 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsrlkkg 345
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 LALVPedrQGEGVVQMMSIQSNMTLSdFSLQGFRRAwkwlnphKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVL 425
Cdd:cd03293 75 RGYVF---QQDALLPWLTVLDNVALG-LELQGVPKA-------EARERAEELLELVGLSGFENAYP-HQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 426 GKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMA--DGRITADVP 497
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAEVE 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
267-497 |
1.27e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 85.63 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 267 TVLSVQGLTALHPSGGYK--------LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHF 338
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFgakqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 339 QSR--LKKGLALVPEDRQGegvvqmmSIQSNMTLSDfSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPITSLS 416
Cdd:TIGR02769 81 KQRraFRRDVQLVFQDSPS-------AVNPRMTVRQ-IIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 417 GGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
..
gi 496059540 496 VP 497
Cdd:TIGR02769 233 CD 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-240 |
1.61e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLnsthqaekLGISIIFQelnlfPNMNV 109
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL--------LELGAGFH-----PELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 110 MDNIFMANEF--FQKGKINEKYQYALAKSLLERLeLDvdpyTPLEELGIGHQqlveiAR-----ALSKDTRVLIMDEpts 182
Cdd:COG1134 106 RENIYLNGRLlgLSRKEIDEKFDEIVEFAELGDF-ID----QPVKTYSSGMR-----ARlafavATAVDPDILLVDE--- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 183 ALSqseV-------KVlFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDA 240
Cdd:COG1134 173 VLA---VgdaafqkKC-LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
269-495 |
1.84e-18 |
|
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: 83.78 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPsGGYKLNDVTFSLSKGevigIYGLLG---AGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfQSRLKKG 345
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG----MYGLLGpngAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 LALVPEDrqgegvvqmMSIQSNMTLSDFsLQGFrrAW-KWLNPHKEQASVKAMIQ--QLAIKVSDPqlpITSLSGGNQQK 422
Cdd:cd03264 74 IGYLPQE---------FGVYPNFTVREF-LDYI--AWlKGIPSKEVKARVDEVLElvNLGDRAKKK---IGSLSGGMRRR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 423 VVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAqQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
269-492 |
1.84e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 84.08 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAH-------- 337
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 338 -------FQSrlkkgLALVPEdrqgegvvqmMSIQSNMTLSDFsLQGFRRAwkwlnPHKEQAsvKAMIQQLAIKVSDPQL 410
Cdd:cd03255 81 rrhigfvFQS-----FNLLPD----------LTALENVELPLL-LAGVPKK-----ERRERA--EELLERVGLGDRLNHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 411 PiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSElDEVMALADRILVMAD 489
Cdd:cd03255 138 P-SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHD-PELAEYADRIIELRD 215
|
...
gi 496059540 490 GRI 492
Cdd:cd03255 216 GKI 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-230 |
1.89e-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: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG---VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlGI 94
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR-QV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFpNMNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELG----IGHQQLVEIARALSK 170
Cdd:TIGR00958 558 ALVGQEPVLF-SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD--TEVGEKGsqlsGGQKQRIAIARALVR 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALsqsEVKVLFNVIEQLKRRGVTIIYISHRLeELMEIGDYITIFRDGR 230
Cdd:TIGR00958 635 KPRVLILDEATSAL---DAECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGS 690
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
285-509 |
2.16e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.78 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkAHFQSR-LKKGLALVPedrqgegvvQmms 363
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL--AAWSPWeLARRRAVLP---------Q--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 iQSNMTLsDFSLQ-----GfRRAWKWLNPHKEQASVKAM----IQQLAikvsdpQLPITSLSGGNQQKVVLGKAL----- 429
Cdd:COG4559 83 -HSSLAF-PFTVEevvalG-RAPHGSSAAQDRQIVREALalvgLAHLA------GRSYQTLSGGEQQRVQLARVLaqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 430 --MTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMfssseldEVM------AL-ADRILVMADGRITADVPRHA 500
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVV-------AVLhdlnlaAQyADRILLLHQGRLVAQGTPEE 226
|
....*....
gi 496059540 501 VTRETLIAA 509
Cdd:COG4559 227 VLTDELLER 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-233 |
2.80e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMD--GIPVTLNSTHQAEKL--GISIIFQelnlFPNM 107
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyAIPANLKKIKEVKRLrkEIGLVFQ----FPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 108 NVMDNIFMANEFFQKGKINEKYQYALAK--SLLERLEL--DVDPYTPLEELGiGHQQLVEIARALSKDTRVLIMDEPTSA 183
Cdd:PRK13645 102 QLFQETIEKDIAFGPVNLGENKQEAYKKvpELLKLVQLpeDYVKRSPFELSG-GQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 184 LSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGRFIS 233
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
285-492 |
2.97e-18 |
|
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: 84.62 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI----DKAHFQSRLKKgLALVpedRQGEGVVQ 360
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRKK-ISMV---FQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSIQSNMTLSdFSLQGFRRAwkwlnpHKEQASVKAmIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFLDE 440
Cdd:cd03294 116 HRTVLENVAFG-LEVQGVPRA------EREERAAEA-LELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 441 PTRGIDVGAKTDVY-HLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03294 187 AFSALDPLIRREMQdELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-251 |
3.26e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.45 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 1 MQQQDIvtphsvESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIP 80
Cdd:PRK10575 1 MQEYTN------HSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 81 V-TLNSTHQAEKlgISIIFQELNLFPNMNVMDNIFMA--------NEFFQKGKinEKYQYALA----KSLLERLeldVDp 147
Cdd:PRK10575 75 LeSWSSKAFARK--VAYLPQQLPAAEGMTVRELVAIGrypwhgalGRFGAADR--EKVEEAISlvglKPLAHRL---VD- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 148 ytpleELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQS-EVKVLfNVIEQLKR-RGVTIIYISHRLEELMEIGDYITI 225
Cdd:PRK10575 147 -----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhQVDVL-ALVHRLSQeRGLTVIAVLHDINMAARYCDYLVA 220
|
250 260
....*....|....*....|....*.
gi 496059540 226 FRDGRFISERPVNDASIPWIIEQMVG 251
Cdd:PRK10575 221 LRGGEMIAQGTPAELMRGETLEQIYG 246
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-232 |
3.41e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.63 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 12 VESEVIIETHDLSrvypgvVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNST---HQ 88
Cdd:PRK10070 29 LSKEQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 89 AEKLGISIIFQELNLFPNMNVMDNIFMANEFfqkGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARAL 168
Cdd:PRK10070 103 VRRKKIAMVFQSFALMPHMTVLDNTAFGMEL---AGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 169 SKDTRVLIMDEPTSALS---QSEVKVLFNVIEQLKRRgvTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:PRK10070 180 AINPDILLMDEAFSALDpliRTEMQDELVKLQAKHQR--TIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
285-492 |
3.48e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.77 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLALVPEDRQgegVVQMMSI 364
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLQgfrrawkwlnphkeqasvKAMIQQLAIKVSD--PQL------PITSLSGGNQQKVVLGKALMTQPQVV 436
Cdd:PRK11614 98 EENLAMGGFFAE------------------RDQFQERIKWVYElfPRLherriqRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 437 FLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-263 |
4.66e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.50 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVY-PGV----VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQA--- 89
Cdd:PRK13641 3 IKFENVDYIYsPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 --EKLGISIIFQELNLFPNMNVMDNIFMANEF-FQKGKINEKyqyalAKSLLERLEL--DVDPYTPLEELGiGHQQLVEI 164
Cdd:PRK13641 83 lrKKVSLVFQFPEAQLFENTVLKDVEFGPKNFgFSEDEAKEK-----ALKWLKKVGLseDLISKSPFELSG-GQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 165 ARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFIS-ERPVNDASIP 243
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKhASPKEIFSDK 236
|
250 260
....*....|....*....|.
gi 496059540 244 -WIieqmvgdkKKHFDYQPAP 263
Cdd:PRK13641 237 eWL--------KKHYLDEPAT 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
33-237 |
4.95e-18 |
|
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: 82.19 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVES--PSSGQIIMDGIPVTLNSTHQAEKLGISIIFQELNLFPNMNVM 110
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 111 DNIFMANEFFQKGkinEKyqyalaksllERleldvdpytpleelgighqqlVEIARALSKDTRVLIMDEPTSALSQSEVK 190
Cdd:cd03217 96 DFLRYVNEGFSGG---EK----------KR---------------------NEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059540 191 VLFNVIEQLKRRGVTIIYISHRlEELME--IGDYITIFRDGRFISERPV 237
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITHY-QRLLDyiKPDRVHVLYDGRIVKSGDK 189
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
261-501 |
5.05e-18 |
|
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: 87.11 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 261 PAPKGEtvLSVQGLTALHP-SGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfQ 339
Cdd:COG4618 325 PRPKGR--LSVENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD-R 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 340 SRLKKGLALVPEDrqgegvVQMM--SIQSN---MTLSDfslqgfrrawkwlnPHK-----EQASVKAMIQQLaikvsdPQ 409
Cdd:COG4618 402 EELGRHIGYLPQD------VELFdgTIAENiarFGDAD--------------PEKvvaaaKLAGVHEMILRL------PD 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 410 ---LPI----TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSS---SeldeVMA 479
Cdd:COG4618 456 gydTRIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVIThrpS----LLA 531
|
250 260
....*....|....*....|..
gi 496059540 480 LADRILVMADGRITADVPRHAV 501
Cdd:COG4618 532 AVDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
284-495 |
6.00e-18 |
|
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: 82.54 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 284 KLNDVTFSL-----------SKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHfqsrlkkglaLVPED 352
Cdd:cd03298 2 RLDKIRFSYgeqpmhfdltfAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTA----------APPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 353 R------QGEGVVQMMSIQSNMTLSdfSLQGFRrawkwLNPHKEQAsVKAMIQQLAIKVSDPQLPITsLSGGNQQKVVLG 426
Cdd:cd03298 70 RpvsmlfQENNLFAHLTVEQNVGLG--LSPGLK-----LTAEDRQA-IEVALARVGLAGLEKRLPGE-LSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 427 KALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
285-494 |
6.07e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHF-QSRLKKGLALVPEDRQGEGVvqmms 363
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLkEIRKKIGIIFQNPDNQFIGA----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 iqsnmTLSD---FSLQGfrrawKWLNPHKeqasVKAMIQQLAIKVS-------DPQlpitSLSGGNQQKVVLGKALMTQP 433
Cdd:PRK13632 100 -----TVEDdiaFGLEN-----KKVPPKK----MKDIIDDLAKKVGmedyldkEPQ----NLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 434 QVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS-SSELDEVMaLADRILVMADGRITA 494
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIA 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
285-501 |
6.19e-18 |
|
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: 87.20 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHF-QSRLKKGLALVPEDrqgegvVQMM- 362
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG--IDLRQIdPASLRRQIGVVLQD------VFLFs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 -SIQSNMTLSDFSLqGFRRAWKWLnphkEQASVKAMIQQLaikvsdP---QLPI----TSLSGGNQQKVVLGKALMTQPQ 434
Cdd:COG2274 563 gTIRENITLGDPDA-TDEEIIEAA----RLAGLHDFIEAL------PmgyDTVVgeggSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 435 VVFLDEPTRGIDVGAKTDVYHLIGKMAqQGLAVMFSSSELdEVMALADRILVMADGRITADVPRHAV 501
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
285-513 |
7.08e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI-----DKAHfqsrlKKGLALVPedrQGEGVV 359
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpAKAH-----QLGIYLVP---QEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 QMMSIQSNMTlsdFSLQgfrrawkwlNPHKEQASVKAMIQQLAIKVsDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:PRK15439 99 PNLSVKENIL---FGLP---------KRQASMQKMKQLLAALGCQL-DLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 440 EPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRETLIAASTPQ 513
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPA 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
274-494 |
7.09e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 274 LTALHPSGGYK----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLALV 349
Cdd:PRK10895 4 LTAKNLAKAYKgrrvVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 350 PedrQGEGVVQMMSIQSNmtlsdfsLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKAL 429
Cdd:PRK10895 84 P---QEASIFRRLSVYDN-------LMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG-QSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 430 MTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
47-230 |
9.18e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.32 E-value: 9.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 47 VLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEklgISIIFQELNLFPNMNVMDNIFMA-------NEf 119
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP---VSMLFQENNLFSHLTVAQNIGLGlnpglklNA- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 120 FQKGKINEKYQYALAKSLLERLeldvdPytplEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQL 199
Cdd:PRK10771 105 AQREKLHAIARQMGIEDLLARL-----P----GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190
....*....|....*....|....*....|..
gi 496059540 200 -KRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:PRK10771 176 cQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-232 |
1.18e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.05 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 3 QQDIVTPHSVESE------VIIETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVeSPSSGQII 75
Cdd:PRK11174 329 ETPLAHPQQGEKElasndpVTIEAEDLEILSPdGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 76 MDGIPVT-LNSTHQAEKLgiSIIFQELNLFPNmNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEE- 153
Cdd:PRK11174 408 INGIELReLDPESWRKHL--SWVGQNPQLPHG-TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLD--TPIGDq 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 154 ---LGIGHQQLVEIARALSKDTRVLIMDEPTSAL-SQSEVKVLfNVIEQLKrRGVTIIYISHRLEELMEIgDYITIFRDG 229
Cdd:PRK11174 483 aagLSVGQAQRLALARALLQPCQLLLLDEPTASLdAHSEQLVM-QALNAAS-RRQTTLMVTHQLEDLAQW-DQIWVMQDG 559
|
...
gi 496059540 230 RFI 232
Cdd:PRK11174 560 QIV 562
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-236 |
1.19e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.71 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 22 DLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTL----------NSTHQAEK 91
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 92 LG--ISIIFQELNLFPNMNVMDNIFMANE---FFQKGKINEKYQYALAKSLLERLELDVDPYtpleELGIGHQQLVEIAR 166
Cdd:PRK10619 90 LRtrLTMVFQHFNLWSHMTVLENVMEAPIqvlGLSKQEARERAVKYLAKVGIDERAQGKYPV----HLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 167 ALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERP 236
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
266-492 |
1.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.36 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECID---KAHFQSRL 342
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 KKGLALVPEDRQ--GEGVVQMMSIQS-NMTLSDFSLQgfRRAwkwlnphkEQASVKAMIQQLAIKvsdpqlPITSLSGGN 419
Cdd:PRK13636 83 SVGMVFQDPDNQlfSASVYQDVSFGAvNLKLPEDEVR--KRV--------DNALKRTGIEHLKDK------PTHCLSFGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 420 QQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
285-509 |
1.42e-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: 82.44 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLM-PCQSGSVQLNGEcidkahfqsrlKKGLALVPEDRQGEGVV---Q 360
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGE-----------RRGGEDVWELRKRIGLVspaL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSIQSNMTLSDFSLQGF---------------RRAWKWLnphkeqasvKAM-IQQLAikvsdpQLPITSLSGGNQQKVV 424
Cdd:COG1119 88 QLRFPRDETVLDVVLSGFfdsiglyreptdeqrERARELL---------ELLgLAHLA------DRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 425 LGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQG-LAVMFSSSELDEVMALADRILVMADGRITADVPRHAV-T 502
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVlT 232
|
....*..
gi 496059540 503 RETLIAA 509
Cdd:COG1119 233 SENLSEA 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-234 |
1.47e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ-AEKL--- 92
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlARRLall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 --------GISIifQELNLF---PNMNVMdnifmaneffqkGKINEKYQyALAKSLLERLELDVDPYTPLEELGIGHQQL 161
Cdd:PRK11231 82 pqhhltpeGITV--RELVAYgrsPWLSLW------------GRLSAEDN-ARVNQAMEQTRINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 162 VEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
285-494 |
1.63e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDkahFQSR----LKKGLALVPEDRQGEgvVQ 360
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD---YSKRgllaLRQQVATVFQDPEQQ--IF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSIQSNMTlsdFSLQGFRRAWKWLNPHKEQASVKAMIQQLAikvsdpQLPITSLSGGNQQKVVLGKALMTQPQVVFLDE 440
Cdd:PRK13638 92 YTDIDSDIA---FSLRNLGVPEAEITRRVDEALTLVDAQHFR------HQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 441 PTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-234 |
1.98e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 80.05 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlgIS 95
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL--IS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFpNMNVMDNIfmaneffqkGKinekyqyalaksllerleldvdpytpleELGIGHQQLVEIARALSKDTRVL 175
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNL---------GR----------------------------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 176 IMDEPTSALS-QSEVKVLFNVIEQLKRRgvTIIYISHRLEElMEIGDYITIFRDGRFISE 234
Cdd:cd03247 121 LLDEPTVGLDpITERQLLSLIFEVLKDK--TLIWITHHLTG-IEHMDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
32-233 |
2.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQA-----EKLGISIIFQELNLFPN 106
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEikpvrKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 107 MNVMDNIFMANEFfqkgKINEKYQYALAKSLLERLELDVDPY--TPLEELGiGHQQLVEIARALSKDTRVLIMDEPTSAL 184
Cdd:PRK13643 101 TVLKDVAFGPQNF----GIPKEKAEKIAAEKLEMVGLADEFWekSPFELSG-GQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059540 185 SQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFIS 233
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-230 |
2.20e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgISII 97
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMA-----NEFFQKGKINEkyqyALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDT 172
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGrtphrSRFDTWTETDR----AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 173 RVLIMDEPTSALS-QSEVKVLfNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:PRK09536 159 PVLLLDEPTASLDiNHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGR 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-211 |
2.38e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.98 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSR-VYPG---VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQA 89
Cdd:PRK10584 3 AENIVEVHHLKKsVGQGeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 EKL---GISIIFQELNLFPNMNVMDNIFMANefFQKGKiNEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIAR 166
Cdd:PRK10584 83 AKLrakHVGFVFQSFMLIPTLNALENVELPA--LLRGE-SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496059540 167 ALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISH 211
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTH 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
285-492 |
2.49e-17 |
|
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: 80.65 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfqsrlKKGLALVpedRQGEGVV-QMMS 363
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD------KKNINEL---RQKVGMVfQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 IQSNMTLSDFSLQGFRRAWKWlnpHKEQASVKAMiqQLAIKVSDP----QLPITsLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:cd03262 87 LFPHLTVLENITLAPIKVKGM---SKAEAEERAL--ELLEKVGLAdkadAYPAQ-LSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 440 EPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-232 |
2.63e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.67 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRV-YPG----VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEK 91
Cdd:COG1101 1 MLELKNLSKTfNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 92 LgISIIFQE--LNLFPNMNVMDNIFMAnefFQKGK-------INeKYQYALAKSLLERLELDVD--PYTPLEELGIGHQQ 160
Cdd:COG1101 81 Y-IGRVFQDpmMGTAPSMTIEENLALA---YRRGKrrglrrgLT-KKRRELFRELLATLGLGLEnrLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 161 LVEIARALSKDTRVLIMDEPTSALS-QSEVKVLfNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDpKTAALVL-ELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
285-495 |
2.76e-17 |
|
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: 81.18 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLkkglalvpEDRQGEGVVqmmsI 364
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY--------ELRRRIGML----F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 Q-----SNMTLSD---FSLQGFRRawkwLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVV 436
Cdd:COG1127 89 QggalfDSLTVFEnvaFPLREHTD----LSEAEIRELVLEKLELVGLPGAADKMP-SELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 437 FLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
269-502 |
2.98e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.51 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHpSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQL---NGECIDKAHFQSRLKKG 345
Cdd:PRK11701 7 LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 LAlvpedRQGEGVVQM-------MSIQSN-------MTLSDFSLQGFRR-AWKWLnphkeqasvkamiQQLAIKVS--Dp 408
Cdd:PRK11701 86 LL-----RTEWGFVHQhprdglrMQVSAGgnigerlMAVGARHYGDIRAtAGDWL-------------ERVEIDAAriD- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 409 QLPiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLI-GKMAQQGLAVMFSSSELDEVMALADRILVM 487
Cdd:PRK11701 147 DLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260
....*....|....*....|...
gi 496059540 488 ADGRITA--------DVPRHAVT 502
Cdd:PRK11701 226 KQGRVVEsgltdqvlDDPQHPYT 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-447 |
3.19e-17 |
|
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: 84.60 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYP-GVVALDSVNYRVYRN-KVNVLiGENGAGKSTMMKMLAGVESPSSGQ-IIMDGIpvtlnsthqae 90
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPpKKEILKDISLSFFPGaKIGVL-GLNGAGKSTLLRIMAGVDKDFNGEaRPQPGI----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGisIIFQELNLFPNMNVMDNIFMA-----------NEFFQK---------------GKINEKYQYALAKSLLERLELD 144
Cdd:TIGR03719 69 KVG--YLPQEPQLDPTKTVRENVEEGvaeikdaldrfNEISAKyaepdadfdklaaeqAELQEIIDAADAWDLDSQLEIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 145 VD------PYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLfnviEQ-LKRRGVTIIYISHRLEELM 217
Cdd:TIGR03719 147 MDalrcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL----ERhLQEYPGTVVAVTHDRYFLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 218 EIGDYITIFRDGRFI-------------SERPVNDAS------------IPWI-----------------IEQMVG-DKK 254
Cdd:TIGR03719 223 NVAGWILELDRGRGIpwegnysswleqkQKRLEQEEKeesarqktlkreLEWVrqspkgrqakskarlarYEELLSqEFQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 255 KHFDYQ-----PAPK-GETVLSVQGLTAlhpSGGYKL--NDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSV 326
Cdd:TIGR03719 303 KRNETAeiyipPGPRlGDKVIEAENLTK---AFGDKLliDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 327 QLnGECIDKAHF-QSRlkkgLALVPedrqGEGVVQMMSI-QSNMTLSDFSLQGfrrawkwlnphkeqasvKAMIQQLAIK 404
Cdd:TIGR03719 380 EI-GETVKLAYVdQSR----DALDP----NKTVWEEISGgLDIIKLGKREIPS-----------------RAYVGRFNFK 433
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 496059540 405 VSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDV 447
Cdd:TIGR03719 434 GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
269-510 |
3.27e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfqsrLKKGL-A 347
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-----LQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 LVPEDRQG--------EGVVqMMSIQSNMTLsdfslqgFRRAwkwlNPHKEQASVKAMIQQLAIKVSDPQlpITSLSGGN 419
Cdd:PRK15056 82 YVPQSEEVdwsfpvlvEDVV-MMGRYGHMGW-------LRRA----KKRDRQIVTAALARVDMVEFRHRQ--IGELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 420 QQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRIlVMADGRITADVPrh 499
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGP-- 224
|
250
....*....|.
gi 496059540 500 avTRETLIAAS 510
Cdd:PRK15056 225 --TETTFTAEN 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
267-506 |
3.68e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 267 TVLSVQGLTaLHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEciDKAHFQSR-LKKG 345
Cdd:PRK13548 1 AMLEARNLS-VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR--PLADWSPAeLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 LAlvpedrqgegvvqMMSIQSNMTLSdFSLQ-----GfRRAWKWLNPHKEQASVKAM----IQQLAikvsdpQLPITSLS 416
Cdd:PRK13548 78 RA-------------VLPQHSSLSFP-FTVEevvamG-RAPHGLSRAEDDALVAAALaqvdLAHLA------GRDYPQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 417 GGNQQKVVLGKALmTQ-------PQVVFLDEPTRGIDVGAKTDVYHLIGKMA-QQGLAVMFssseldeVM------AL-A 481
Cdd:PRK13548 137 GGEQQRVQLARVL-AQlwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIV-------VLhdlnlaARyA 208
|
250 260
....*....|....*....|....*.
gi 496059540 482 DRILVMADGRITAD-VPRHAVTRETL 506
Cdd:PRK13548 209 DRIVLLHQGRLVADgTPAEVLTPETL 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-234 |
3.69e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPGV--VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKL 92
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 gISIIFQEL-NLFPNMNVMDNIFMA--NEFFQKGKINEKYQYALAKSLLERLeLDVDPYtpleELGIGHQQLVEIARALS 169
Cdd:PRK13635 83 -VGMVFQNPdNQFVGATVQDDVAFGleNIGVPREEMVERVDQALRQVGMEDF-LNREPH----RLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 170 KDTRVLIMDEPTSALS-QSEVKVLfNVIEQLKR-RGVTIIYISHRLEELMEiGDYITIFRDGRFISE 234
Cdd:PRK13635 157 LQPDIIILDEATSMLDpRGRREVL-ETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
285-495 |
3.91e-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: 80.33 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfQSRLKKGLALVPEDrqgegvVQMM-- 362
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIGYVPQD------VTLFyg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLSDfslqgfrrawkwlNPHKEQASVKAM----IQQLAIKvsDP---QLPI----TSLSGGNQQKVVLGKALMT 431
Cdd:cd03245 93 TLRDNITLGA-------------PLADDERILRAAelagVTDFVNK--HPnglDLQIgergRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 432 QPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS--SSELDevmaLADRILVMADGRITAD 495
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIThrPSLLD----LVDRIIVMDSGRIVAD 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
285-487 |
4.39e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.59 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECidkahfqsrlkkGLALVPEdrQGEG------- 357
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA------------RVAYVPQ--RSEVpdslplt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 358 VVQMMSIqsnmtlsdfSLQGFRRAWKWLNPHKEQASVKAM----IQQLAikvsdpQLPITSLSGGNQQKVVLGKALMTQP 433
Cdd:NF040873 74 VRDLVAM---------GRWARRGLWRRLTRDDRAAVDDALervgLADLA------GRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 434 QVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMAlADRILVM 487
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-234 |
4.53e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.35 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 11 SVESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDG--IPVTLNSTHQ 88
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 89 AEKLGISIIFQELNLFPNMNVMDNIfmANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARAL 168
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNV--AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 169 SKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-227 |
4.73e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVeSPSSGQIIMDGIPVTLNSTHQAEKLGI--- 94
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRVEFFNQNIYERRVNLnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 ----SIIFQELNLFPnMNVMDNIFMANEFF---QKGKINEKYQYALAKSLLERlELDVDPYTPLEELGIGHQQLVEIARA 167
Cdd:PRK14258 87 rrqvSMVHPKPNLFP-MSVYDNVAYGVKIVgwrPKLEIDDIVESALKDADLWD-EIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 168 LSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRG-VTIIYISHRLEELMEIGDYITIFR 227
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
285-492 |
4.83e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.45 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDkahfqsrlkkglALVPEDRQgegvVQMMSi 364
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT------------GLPPEKRN----VGMVF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QS-----NMTLSD---FSLqgfrRAWKwLNPHKEQASVKAMIQQLaikvsdpQLP------ITSLSGGNQQKVVLGKALM 430
Cdd:COG3842 84 QDyalfpHLTVAEnvaFGL----RMRG-VPKAEIRARVAELLELV-------GLEgladryPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 431 TQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-232 |
4.86e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.33 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ-----AEKLGISIIFQELNLFPN 106
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 107 MNVMDNIFMANEFfqkgKINEKYQYALAKsllERLEL--------DVDPYtpleELGIGHQQLVEIARALSKDTRVLIMD 178
Cdd:PRK13649 102 TVLKDVAFGPQNF----GVSQEEAEALAR---EKLALvgiseslfEKNPF----ELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 179 EPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-229 |
5.16e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.44 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVtlnSTHQAEKLGISII 97
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNI-FMANEFFQKGKINEKYQYALAKSLLERLELD--VDPYTplEELGIGHQQLVEIARALSKDTRV 174
Cdd:PRK10851 80 FQHYALFRHMTVFDNIaFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAhlADRYP--AQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 175 LIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDG 229
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
269-501 |
6.85e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 79.92 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTaLHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ-----SGSVQLNGECI-DKAHFQSRL 342
Cdd:cd03260 1 IELRDLN-VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIyDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 KKGLALVpedRQGEGVVQMmSIQSNMTLSDfSLQGFRRAwKWLNPHKEQASVKAmiqQLAIKVSDpQLPITSLSGGNQQK 422
Cdd:cd03260 80 RRRVGMV---FQKPNPFPG-SIYDNVAYGL-RLHGIKLK-EELDERVEEALRKA---ALWDEVKD-RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 423 VVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQgLAVMFSSSELDEVMALADRILVMADGRITADVPRHAV 501
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-236 |
8.44e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.53 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 22 DLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSG-----QIIMDGIPVTLNSTHQAEKLGISI 96
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPnMNVMDNIFM---ANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGiGHQQLVEIARALSKDTR 173
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAgvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSG-GQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 174 VLIMDEPTSALSQSEVKVLFNVIEQLKRRgVTIIYISHRLEELMEIGDYITIFRDGRFISERP 236
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-218 |
8.72e-17 |
|
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: 79.46 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP--GVVALDSVNYRVYRN-KVNVlIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgI 94
Cdd:cd03244 3 IEFKNVSLRYRpnLPPVLKNISFSIKPGeKVGI-VGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNmNVMDNIFMANEFfQKGKINEKYQYALAKSLLERLELDVDpyTPLEE----LGIGHQQLVEIARALSK 170
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDPFGEY-SDEELWQALERVGLKEFVESLPGGLD--TVVEEggenLSVGQRQLLCLARALLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQlKRRGVTIIYISHRLEELME 218
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
268-492 |
9.91e-17 |
|
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: 78.36 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHPSGGYK-----LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVG-LMPCQ-SGSVQLNGECIDKahfqS 340
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKsgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGvSGEVLINGRPLDK----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 341 RLKKGLALVPEDrqgegvvqmmsiqsNMTLSDFSLQgfrrawkwlnphkEQASVKAMIQqlaikvsdpqlpitSLSGGNQ 420
Cdd:cd03213 79 SFRKIIGYVPQD--------------DILHPTLTVR-------------ETLMFAAKLR--------------GLSGGER 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 421 QKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS----SSeldEVMALADRILVMADGRI 492
Cdd:cd03213 118 KRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpSS---EIFELFDKLLLLSQGRV 190
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-232 |
1.99e-16 |
|
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: 82.48 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgISI 96
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNmNVMDNIFM-ANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEE----LGIGHQQLVEIARALSKD 171
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQ--TELSEegssISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 172 TRVLIMDEPTSALSQ-SEVKVLFNVieqLKRRGVTIIYISHRLeELMEIGDYITIFRDGRFI 232
Cdd:TIGR01193 630 SKVLILDESTSNLDTiTEKKIVNNL---LNLQDKTIIFVAHRL-SVAKQSDKIIVLDHGKII 687
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
268-508 |
2.08e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.46 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsRLKKGLA 347
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR-EVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 LV---PEDRqgegvVQMMSIQSNMTLSDFSLQgfrrawkwLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVV 424
Cdd:PRK13652 82 LVfqnPDDQ-----IFSPTVEQDIAFGPINLG--------LDEETVAHRVSSALHMLGLEELRDRVP-HHLSGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 425 LGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITAD-VPRHAVT 502
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYgTVEEIFL 227
|
....*.
gi 496059540 503 RETLIA 508
Cdd:PRK13652 228 QPDLLA 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
284-497 |
2.24e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.26 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 284 KLNDVT-----------FSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqsrlkkgLALVPED 352
Cdd:COG3840 3 RLDDLTyrygdfplrfdLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL------------TALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 353 RQgegvVQM----------MSIQSNMTLsdfslqGFRRAWKwLNPhKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQK 422
Cdd:COG3840 71 RP----VSMlfqennlfphLTVAQNIGL------GLRPGLK-LTA-EQRAQVEQALERVGLAGLLDRLP-GQLSGGQRQR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 423 VVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQ-QGLAVMFSSSELDEVMALADRILVMADGRITADVP 497
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-230 |
2.92e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.62 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYP---G-------VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTL 83
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrGlfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 84 NStHQAEKL---GISIIFQelNLFPNMNVMDNIFMANEffQKGKIN------EKYQYALAksLLERLELDVDPYTPLEEL 154
Cdd:PRK11308 82 AD-PEAQKLlrqKIQIVFQ--NPYGSLNPRKKVGQILE--EPLLINtslsaaERREKALA--MMAKVGLRPEHYDRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 155 GIGHQ-QLVEIARALSKDTRVLIMDEPTSALSQS-EVKVLfNVIEQLKRR-GVTIIYISHRL-------EELM------- 217
Cdd:PRK11308 155 FSGGQrQRIAIARALMLDPDVVVADEPVSALDVSvQAQVL-NLMMDLQQElGLSYVFISHDLsvvehiaDEVMvmylgrc 233
|
250
....*....|....
gi 496059540 218 -EIGDYITIFRDGR 230
Cdd:PRK11308 234 vEKGTKEQIFNNPR 247
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-510 |
2.97e-16 |
|
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: 81.35 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 260 QPAPKGETVLSVQGLTALHPSGGYK-LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHF 338
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG--VDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 339 -QSRLKKGLALVPEDrqgeGVVQMMSIQSNMTL-----SDfslqgfRRAWKWLnphkEQASVKAMIQQLaikvsdPQ--- 409
Cdd:COG4987 403 dEDDLRRRIAVVPQR----PHLFDTTLRENLRLarpdaTD------EELWAAL----ERVGLGDWLAAL------PDgld 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 410 LPI----TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKmAQQGLAVMFSSSELDEvMALADRIL 485
Cdd:COG4987 463 TWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAG-LERMDRIL 540
|
250 260
....*....|....*....|....*
gi 496059540 486 VMADGRITAdvprhAVTRETLIAAS 510
Cdd:COG4987 541 VLEDGRIVE-----QGTHEELLAQN 560
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-230 |
3.65e-16 |
|
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: 77.57 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 27 YPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLnsthqaekLGISIIFQelnlfPN 106
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--------LGLGGGFN-----PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 107 MNVMDNIFMANEF--FQKGKINEKYQYALAKSllerlELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSAL 184
Cdd:cd03220 99 LTGRENIYLNGRLlgLSRKEIDEKIDEIIEFS-----ELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496059540 185 SQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-232 |
3.89e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 19 ETHDLSRVYPGV---VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNS---THQAEKL 92
Cdd:PRK14246 9 DVFNISRLYLYIndkAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 --GISIIFQELNLFPNMNVMDNI---FMANEFFQKGKINEKYQYALAKSLLERlELDVDPYTPLEELGIGHQQLVEIARA 167
Cdd:PRK14246 89 rkEVGMVFQQPNPFPHLSIYDNIaypLKSHGIKEKREIKKIVEECLRKVGLWK-EVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 168 LSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRgVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
285-505 |
4.03e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.94 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI-DKAHFQSRLKKGLALV---PEDRQGEGVVQ 360
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItDKKVKLSDIRKKVGLVfqyPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MmSIQ---SNMTLSDFSLQgfRRawkwlnphkeqasVKAMIQQLAIKVSD--PQLPItSLSGGNQQKVVLGKALMTQPQV 435
Cdd:PRK13637 103 K-DIAfgpINLGLSEEEIE--NR-------------VKRAMNIVGLDYEDykDKSPF-ELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 436 VFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRET 505
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEV 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
268-492 |
4.99e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.20 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECID---KAHFQSRLKK 344
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 345 GLALVPEDRQ--GEGVVQMMSIQS-NMTLsdfslqgfrrawkwlnPHKE-QASVKAMIQQLAIKVSDPQLPiTSLSGGNQ 420
Cdd:PRK13639 81 GIVFQNPDDQlfAPTVEEDVAFGPlNLGL----------------SKEEvEKRVKEALKAVGMEGFENKPP-HHLSGGQK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 421 QKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-234 |
5.41e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.30 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESP---SSGQIIMDGIPVTLNSTHQA-E 90
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIrE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGisIIFQEL-NLFPNMNVMDNIFMANEffQKGKINEKYQYALAKSLLERLELDVDPYTPlEELGIGHQQLVEIARALS 169
Cdd:PRK13640 85 KVG--IVFQNPdNQFVGATVGDDVAFGLE--NRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 170 KDTRVLIMDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEElMEIGDYITIFRDGRFISE 234
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQ 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
266-505 |
5.55e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 77.82 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTA--LHPSGGYK-LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAH----- 337
Cdd:COG1116 5 APALELRGVSKrfPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGpdrgv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 338 -FQS-------------RLkkGLAL--VPEDRQGEGVVQMmsiqsnmtLSDFSLQGFRRAWkwlnPHkeqasvkamiqql 401
Cdd:COG1116 85 vFQEpallpwltvldnvAL--GLELrgVPKAERRERAREL--------LELVGLAGFEDAY----PH------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 402 aikvsdpqlpitSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMAL 480
Cdd:COG1116 138 ------------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFL 205
|
250 260 270
....*....|....*....|....*....|...
gi 496059540 481 ADRILVMAD--GRITADV------PRHAVTRET 505
Cdd:COG1116 206 ADRVVVLSArpGRIVEEIdvdlprPRDRELRTS 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
285-492 |
5.62e-16 |
|
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: 77.38 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfqsrlkkglalvPEDRQGEGVVQMMSI 364
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------------VQERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSD---FSLQgFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:cd03296 86 FRHMTVFDnvaFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 442 TRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-234 |
5.63e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.30 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 22 DLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVtlNSTHQAEKlGISIIFQEL 101
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM--NDVPPAER-GVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 102 NLFPNMNVMDNifMAnefF-------QKGKINEKYQYALAKSLLERLeLDVDPytplEELGIGHQQLVEIARALSKDTRV 174
Cdd:PRK11000 85 ALYPHLSVAEN--MS---FglklagaKKEEINQRVNQVAEVLQLAHL-LDRKP----KALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 175 LIMDEPTSALSqSEVKVLFNV-IEQL-KRRGVTIIYISHRLEELMEIGDYITIFrDGRFISE 234
Cdd:PRK11000 155 FLLDEPLSNLD-AALRVQMRIeISRLhKRLGRTMIYVTHDQVEAMTLADKIVVL-DAGRVAQ 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-232 |
6.04e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 13 ESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGV-----ESPSSGQIIMDGIPVTLNSTH 87
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 88 QAE-KLGISIIFQELNLFPnMNVMDNIFMANEFfqKG-KINEKYQYALAKSLLERLELD-VDPYTPLEELGI--GHQQLV 162
Cdd:PRK14239 81 TVDlRKEIGMVFQQPNPFP-MSIYENVVYGLRL--KGiKDKQVLDEAVEKSLKGASIWDeVKDRLHDSALGLsgGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 163 EIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRgVTIIYISHRLEELMEIGDYITIFRDGRFI 232
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-230 |
6.13e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.50 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 9 PHSVESEVIIETHDLSRVYPG-----------VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVEsPSSGQIIMD 77
Cdd:COG4172 267 PVPPDAPPLLEARDLKVWFPIkrglfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 78 GIPVTLNSTHQAEKL--GISIIFQE----LNlfPNMNVMDNIF--MAnefFQKGKINEKYQYALAKSLLERLELDVD--- 146
Cdd:COG4172 346 GQDLDGLSRRALRPLrrRMQVVFQDpfgsLS--PRMTVGQIIAegLR---VHGPGLSAAERRARVAEALEEVGLDPAarh 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 147 --PYtpleELGIGHQQLVEIARALSKDTRVLIMDEPTSALsqsEVKVLFNVIEQL----KRRGVTIIYISHRLEELMEIG 220
Cdd:COG4172 421 ryPH----EFSGGQRQRIAIARALILEPKLLVLDEPTSAL---DVSVQAQILDLLrdlqREHGLAYLFISHDLAVVRALA 493
|
250
....*....|
gi 496059540 221 DYITIFRDGR 230
Cdd:COG4172 494 HRVMVMKDGK 503
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
285-504 |
8.15e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.31 E-value: 8.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLalVPedrqgegvvQMMSI 364
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--VP---------QFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDfSLQGFRRAWKwLNPHKEQASVKAMIQqLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:PRK13537 92 DPDFTVRE-NLLVFGRYFG-LSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 445 IDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGR-ITADVPRHAVTRE 504
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRkIAEGAPHALIESE 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
47-221 |
8.42e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.73 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 47 VLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVtlNSTHQAEKlGISIIFQELNLFPNMNVMDNifMA----NEFFQK 122
Cdd:PRK11650 34 VLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NELEPADR-DIAMVFQNYALYPHMSVREN--MAyglkIRGMPK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 123 GKINEKYQYAlAKSL-LERLeLDVDPytplEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSqSEVKVLFNV-IEQLK 200
Cdd:PRK11650 109 AEIEERVAEA-ARILeLEPL-LDRKP----RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD-AKLRVQMRLeIQRLH 181
|
170 180
....*....|....*....|..
gi 496059540 201 RR-GVTIIYISHRLEELMEIGD 221
Cdd:PRK11650 182 RRlKTTSLYVTHDQVEAMTLAD 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
285-492 |
1.02e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 75.91 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsRLKKGLALVPEDrqgeGVVQMMSI 364
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-DLRSSLTIIPQD----PTLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNmtlsdfslqgfrrawkwLNPHKEQASVKAMIqqlAIKVSDPQLpitSLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03369 99 RSN-----------------LDPFDEYSDEEIYG---ALRVSEGGL---NLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 445 IDVgaKTDvyHLIGKMAQ---QGLAVMFSSSELDEVmALADRILVMADGRI 492
Cdd:cd03369 156 IDY--ATD--ALIQKTIReefTNSTILTIAHRLRTI-IDYDKILVMDAGEV 201
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
283-492 |
1.13e-15 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 75.75 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 283 YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahfqsrlkkglaLVPEDRQGEGVVQMM 362
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD------------LPPKDRDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLSD---FSLQgFRRAwkwlnPHKE-QASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:cd03301 82 ALYPHMTVYDniaFGLK-LRKV-----PKDEiDERVREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-230 |
1.19e-15 |
|
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: 79.41 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 23 LSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSthqAEKLGISIIF-- 98
Cdd:COG4618 336 LTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELGRHIGYlp 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 99 QELNLFPNmNVMDNIFManefFQKG---KINEKYQYALAKSLLERLEldvDPY-TPLEELGI----GHQQLVEIARALSK 170
Cdd:COG4618 413 QDVELFDG-TIAENIAR----FGDAdpeKVVAAAKLAGVHEMILRLP---DGYdTRIGEGGArlsgGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLeELMEIGDYITIFRDGR 230
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGR 543
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
285-492 |
1.70e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEciDKAHFQSRlkkglalvpeDRQGEGVVQMMSI 364
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHAR----------DRKVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSD---FSLQgfrrawkwLNPHKEQASVKAMIQQLAIKVSDPQLP------ITSLSGGNQQKVVLGKALMTQPQV 435
Cdd:PRK10851 86 FRHMTVFDniaFGLT--------VLPRRERPNAAAIKAKVTQLLEMVQLAhladryPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 436 VFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
267-497 |
2.01e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 267 TVLSVQGLTALHPSGGYK--------LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahf 338
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSgkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 339 qSRLKKGlalvpEDRQGEGVVQMMSIQSnmtlsdFSLQGFRRAWKW-----------LNPHKEQASVKAMIQQLAIKVSD 407
Cdd:PRK10419 77 -AKLNRA-----QRKAFRRDIQMVFQDS------ISAVNPRKTVREiireplrhllsLDKAERLARASEMLRAVDLDDSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 408 PQ-LPiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRIL 485
Cdd:PRK10419 145 LDkRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVM 223
|
250
....*....|..
gi 496059540 486 VMADGRITADVP 497
Cdd:PRK10419 224 VMDNGQIVETQP 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
266-495 |
2.19e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.80 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTaLHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECID--KAH------ 337
Cdd:PRK11300 3 QPLLSVSGLM-MRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHqiarmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 338 ----FQS-RLKKGLALVpedrqgEG--VVQMMSIQSNMTLSDFSLQGFRRAWK--------WLnphkEQASVKAMIQQLA 402
Cdd:PRK11300 82 vvrtFQHvRLFREMTVI------ENllVAQHQQLKTGLFSGLLKTPAFRRAESealdraatWL----ERVGLLEHANRQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 403 ikvsdpqlpiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALA 481
Cdd:PRK11300 152 ----------GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGIS 221
|
250
....*....|....
gi 496059540 482 DRILVMADGRITAD 495
Cdd:PRK11300 222 DRIYVVNQGTPLAN 235
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
48-493 |
2.31e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.78 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMDgipvtlnsthQAEKLGisIIFQELNLFPNMNVMDNIFMANEFFQKGKINE 127
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD----------PNERLG--KLRQDQFAFEEFTVLDTVIMGHTELWEVKQER 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 128 KYQYALAK---------SLLERLELDVDPYTP-------LEELGIG---HQQL-----------VEIARALSKDTRVLIM 177
Cdd:PRK15064 100 DRIYALPEmseedgmkvADLEVKFAEMDGYTAearagelLLGVGIPeeqHYGLmsevapgwklrVLLAQALFSNPDILLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 178 DEPTSALSQSEVKVLFNVieqLKRRGVTIIYISHRLEEL------MEIGDY--ITIFrDGRF---------ISERPVND- 239
Cdd:PRK15064 180 DEPTNNLDINTIRWLEDV---LNERNSTMIIISHDRHFLnsvcthMADLDYgeLRVY-PGNYdeymtaatqARERLLADn 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 240 ----ASI------------------------------------------PWII-EQmvgDKKKHfdyqpapkgETVLSVQ 272
Cdd:PRK15064 256 akkkAQIaelqsfvsrfsanaskakqatsrakqidkikleevkpssrqnPFIRfEQ---DKKLH---------RNALEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 273 GLTalHPSGGYKL-NDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNgeciDKAHfqsrlkkgLALVPE 351
Cdd:PRK15064 324 NLT--KGFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----ENAN--------IGYYAQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 352 DRQGEgvvqmmsIQSNMTLSDFSLQgfrrawkWLNPHKEQASVKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMT 431
Cdd:PRK15064 390 DHAYD-------FENDLTLFDWMSQ-------WRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 432 QPQVVFLDEPTRGIDVGA------KTDVYhligkmaqQGlAVMFSSSELDEVMALADRILVMADGRIT 493
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESieslnmALEKY--------EG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
285-492 |
2.72e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.43 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDkahFQSRL--KKGLALvpedRQGEGVV-QM 361
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD---FSQKPseKAIRLL----RQKVGMVfQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTLsdfsLQGFRRA-WKWLNPHKEQASVKAM--IQQLAIKVSDPQLPItSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:COG4161 91 YNLWPHLTV----MENLIEApCKVLGLSKEQAREKAMklLARLRLTDKADRFPL-HLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
285-485 |
2.88e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLngecidkahfQSRLKKGLalvpedrqgegVVQMMSI 364
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR----------NGKLRIGY-----------VPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSdfsLQGFRRawkwLNPHKEQASVKAMIQqlaiKVSDPQL---PITSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:PRK09544 79 DTTLPLT---VNRFLR----LRPGTKKEDILPALK----RVQAGHLidaPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059540 442 TRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRIL 485
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
257-487 |
3.04e-15 |
|
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: 78.10 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 257 FDYQPAPKGET---------VLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQ 327
Cdd:TIGR02857 301 LDAAPRPLAGKapvtaapasSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 328 LNGecIDKAHF-QSRLKKGLALVPedrQGEGVVQMmSIQSNMTLSDfslqgfrrawkwlnPHKEQASVKAMIQQLAIKVS 406
Cdd:TIGR02857 381 VNG--VPLADAdADSWRDQIAWVP---QHPFLFAG-TIAENIRLAR--------------PDASDAEIREALERAGLDEF 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 407 DPQLPI----------TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAqQGLAVMFSSSELdE 476
Cdd:TIGR02857 441 VAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRL-A 518
|
250
....*....|.
gi 496059540 477 VMALADRILVM 487
Cdd:TIGR02857 519 LAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
285-492 |
3.19e-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: 74.84 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsRLKKGLALVPEDrqgegvVQMMS- 363
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-DLRSRISIIPQD------PVLFSg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 -IQSNM----TLSDFSLqgfrraWKWLnphkEQASVKAMIQQLAIKVsdpQLPITS----LSGGNQQKVVLGKALMTQPQ 434
Cdd:cd03244 93 tIRSNLdpfgEYSDEEL------WQAL----ERVGLKEFVESLPGGL---DTVVEEggenLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 435 VVFLDEPTRGIDVGakTDvyHLIGKMAQQGLA---VMFSSSELDEVMAlADRILVMADGRI 492
Cdd:cd03244 160 ILVLDEATASVDPE--TD--ALIQKTIREAFKdctVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
272-492 |
3.70e-15 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 74.37 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 272 QGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqSRLKKglALVPE 351
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV------SDLRG--RAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 352 DRQGEGVV-QMMSIQSNMTLSD---FSLQGFRRawkwlnPHKE-QASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLG 426
Cdd:cd03292 76 LRRKIGVVfQDFRLLPDRNVYEnvaFALEVTGV------PPREiRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 427 KALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
33-232 |
3.77e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVES--PSSGQIIMDGIPVTLNSTHQAEKLGISIIFQ---ElnlFPNM 107
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERARAGIFLAFQypvE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 108 NVMD----------NIFMANEFFQKgKINEK-YQYALAKSLLERlELDVDpytpleeLGIGHQQLVEIARALSKDTRVLI 176
Cdd:COG0396 93 SVSNflrtalnarrGEELSAREFLK-LLKEKmKELGLDEDFLDR-YVNEG-------FSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 177 MDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISH--RLEELMEIgDYITIFRDGRFI 232
Cdd:COG0396 164 LDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqRILDYIKP-DFVHVLVDGRIV 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
285-508 |
4.80e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.46 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLALVpedRQGEGVVQMMSI 364
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMV---HQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLQGFrrawkWLNPHKEQASVKAMIQQLAIKVsDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:PRK10982 91 MDNMWLGRYPTKGM-----FVDQDKMYRDTKAIFDELDIDI-DPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 445 IdvgAKTDVYHL---IGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRETLIA 508
Cdd:PRK10982 165 L---TEKEVNHLftiIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIA 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
287-509 |
5.03e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 287 DVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPcqSGSVQLNGECidkahfqsrLKKGLALVPEDRQGEGVVQMMsiqs 366
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP--AGVRQTAGRV---------LLDGKPVAPCALRGRKIATIM---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 367 nmtlsdfslQGFRRAWkwlNP------H-KE-------QASVKAMIQQL-AIKVSDP----QLPITSLSGGNQQKVVLGK 427
Cdd:PRK10418 86 ---------QNPRSAF---NPlhtmhtHaREtclalgkPADDATLTAALeAVGLENAarvlKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 428 ALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGK-MAQQGLAVMFSSSELDEVMALADRILVMADGRI--TADV------PR 498
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIveQGDVetlfnaPK 233
|
250
....*....|.
gi 496059540 499 HAVTReTLIAA 509
Cdd:PRK10418 234 HAVTR-SLVSA 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
285-504 |
5.93e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahfQSRL-KKGLALVPedrQGEGVVQMMS 363
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA---RARLaRARIGVVP---QFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 IQSNMTLsdfslqgFRRAWKwLNPHKEQASVKAMIQqLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTR 443
Cdd:PRK13536 131 VRENLLV-------FGRYFG-MSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 444 GIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRE 504
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
285-494 |
5.94e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.30 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLALVPedrqgegvvQMMSI 364
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYLP---------QEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDfSLQGFRRAWKwLNPHKEQASVKAMIQQLAI-KVSDpQLPItSLSGGNQQKVVLGKALMTQPQVVFLDEPTR 443
Cdd:COG1137 90 FRKLTVED-NILAVLELRK-LSKKEREERLEELLEEFGItHLRK-SKAY-SLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 444 GIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLA 216
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
29-225 |
6.81e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 6.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 29 GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlGISIIFQELNLFPNmN 108
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ-QVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 109 VMDNIFMANEFFQKgKINEKyqyALAKSlLERLELDVDPYT-PLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQS 187
Cdd:PRK10247 97 VYDNLIFPWQIRNQ-QPDPA---IFLDD-LERFALPDTILTkNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059540 188 EVKVLFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITI 225
Cdd:PRK10247 172 NKHNVNEIIHRYVReQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-221 |
8.26e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 8.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ--AEKLGISIIFQE----LNlfP 105
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDplasLN--P 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 106 NMNVMDNIFMANEFFQ----KGKINEKYQYALAK-SLLERLeldVDPYtPLEELGiGHQQLVEIARALSKDTRVLIMDEP 180
Cdd:PRK15079 114 RMTIGEIIAEPLRTYHpklsRQEVKDRVKAMMLKvGLLPNL---INRY-PHEFSG-GQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059540 181 TSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGD 221
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISD 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
285-491 |
9.51e-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: 72.03 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKgLALVPEDrqgegvVQM--M 362
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQD------PFLfsG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMtlsdfslqgfrrawkwlnphkeqasvkamiqqlaikvsdpqlpitsLSGGNQQKVVLGKALMTQPQVVFLDEPT 442
Cdd:cd03228 91 TIRENI----------------------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059540 443 RGIDVGAKTDVYHLIGKMAQQGLAVMFSSSelDEVMALADRILVMADGR 491
Cdd:cd03228 125 SALDPETEALILEALRALAKGKTVIVIAHR--LSTIRDADRIIVLDDGR 171
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
50-244 |
9.75e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 50 GENGAGKSTMMKMLAGVESPSSGQIIMDGipVTLNSTHQ-----AEKLGISIIFQELNLFPNMNVMDNI------FMANE 118
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNG--RVLFDAEKgiclpPEKRRIGYVFQDARLFPHYKVRGNLrygmakSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 119 FfqkgkinEKYQYALA-KSLLERLeldvdPYTpleeLGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIE 197
Cdd:PRK11144 109 F-------DKIVALLGiEPLLDRY-----PGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 198 QLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPV-----NDASIPW 244
Cdd:PRK11144 173 RLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLeevwaSSAMRPW 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-240 |
1.11e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 20 THDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LN-STHQAEKLGISII 97
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkLNrAQRKAFRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQelnlfpnmnvmDNIFMANEFFQKGKI-----------NEKYQYALAKSLLERLELDVDPYTPL-EELGIGHQQLVEIA 165
Cdd:PRK10419 95 FQ-----------DSISAVNPRKTVREIireplrhllslDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 166 RALSKDTRVLIMDEptsALSQSEVKVLFNVIEQLK----RRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDA 240
Cdd:PRK10419 164 RALAVEPKLLILDE---AVSNLDLVLQAGVIRLLKklqqQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
285-506 |
1.39e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGS---VQLNGECIDKAHFQSR-LKKGLALVPEDRQGEGVVQ 360
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREGRLARdIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSIQSNMTLSDFSLQGF-RRAWKWLNPHKEQASVKAMIQQLAIKVSDPQlpITSLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQR--VSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 440 EPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRETL 506
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERF 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
287-494 |
1.58e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 287 DVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfqsrlkKGLALVPEDRQGEGVVQ------ 360
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAE------KGICLPPEKRRIGYVFQdarlfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 MMSIQSNMtlsdfsLQGFRrawkwlnpHKEQASVKAMIQQLAIKVSDPQLPITsLSGGNQQKVVLGKALMTQPQVVFLDE 440
Cdd:PRK11144 90 HYKVRGNL------RYGMA--------KSMVAQFDKIVALLGIEPLLDRYPGS-LSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 441 PTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-230 |
1.73e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 22 DLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVtlnstHQAEKlGISIIFQEL 101
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEARE-DTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 102 NLFPNMNVMDNIFMAneffQKGKINEKYQYALAKSLLErlelDVDPYTPlEELGIGHQQLVEIARALSKDTRVLIMDEP- 180
Cdd:PRK11247 91 RLLPWKKVIDNVGLG----LKGQWRDAALQALAAVGLA----DRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPl 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 181 --TSALSQSEVKVLfnvIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:PRK11247 162 gaLDALTRIEMQDL---IESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-230 |
1.76e-14 |
|
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: 72.12 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 24 SRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipvtlnsthqaeklGISIIFQELNL 103
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 104 FpNMNVMDNIFMANEFfqkgkINEKYQYALAKSLLERlELDVDPY---TPLEELGI----GHQQLVEIARALSKDTRVLI 176
Cdd:cd03250 78 Q-NGTIRENILFGKPF-----DEERYEKVIKACALEP-DLEILPDgdlTEIGEKGInlsgGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 177 MDEPTSAL-SQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIgDYITIFRDGR 230
Cdd:cd03250 151 LDDPLSAVdAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
14-226 |
1.78e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 14 SEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMK----MLAGVES-PSSGQIIMDGIPVTLNSTHQ 88
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrLNDLIPGfRVEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 89 AE-KLGISIIFQELNLFPNmNVMDNI-FMANEFFQKGKINEKYQYALAKSLLERLELDvdpytPLEELGI----GHQQLV 162
Cdd:PRK14243 87 VEvRRRIGMVFQKPNPFPK-SIYDNIaYGARINGYKGDMDELVERSLRQAALWDEVKD-----KLKQSGLslsgGQQQRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 163 EIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRgVTIIYISHRLEELMEIGDYITIF 226
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFF 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-211 |
1.98e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.35 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVY------PG---------------VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQII 75
Cdd:COG4586 1 IIEVENLSKTYrvyekePGlkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 76 MDG-IPVTLNSTHQAEklgISIIF-QELNLFPNMNVMDNiFMANeffqkGKI----NEKYQYALAKsLLERLELDVDPYT 149
Cdd:COG4586 81 VLGyVPFKRRKEFARR---IGVVFgQRSQLWWDLPAIDS-FRLL-----KAIyripDAEYKKRLDE-LVELLDLGELLDT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 150 PLEELGIGHQQLVEIARALSKDTRVLIMDEPT---SALSQSEVKvlfNVIEQL-KRRGVTIIYISH 211
Cdd:COG4586 151 PVRQLSLGQRMRCELAAALLHRPKILFLDEPTiglDVVSKEAIR---EFLKEYnRERGTTILLTSH 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-229 |
2.27e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLagvespsSGQIIMDGIP---VTL--NSTHQA 89
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAgshIELlgRTVQRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 EKLGISI---------IFQELNLFPNMNVMDNIFMAN-----------EFFQKGKINEKYQyalaksLLERLELDVDPYT 149
Cdd:PRK09984 75 GRLARDIrksrantgyIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQ------ALTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 150 PLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRD 228
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQ 228
|
.
gi 496059540 229 G 229
Cdd:PRK09984 229 G 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
277-492 |
2.42e-14 |
|
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: 76.21 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 277 LHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfQSRLKKGLALVPedrQGE 356
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN--LDAVRQSLGMCP---QHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 357 GVVQMMSIQSNMTlsdFSLQGFRRAWKwlnphKEQASVKAMIQQLAIKVSDPQlPITSLSGGNQQKVVLGKALMTQPQVV 436
Cdd:TIGR01257 1013 ILFHHLTVAEHIL---FYAQLKGRSWE-----EAQLEMEAMLEDTGLHHKRNE-EAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 437 FLDEPTRGIDVGAKTDVYHLIGKMaQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
285-492 |
2.45e-14 |
|
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: 72.27 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqsrlkkgLALVPEDRQGEGVVQMMSI 364
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI------------TNLPPHKRPVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLQGFRRawKWLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03300 84 FPHLTVFENIAFGLRL--KKLPKAEIKERVAEALDLVQLEGYANRKP-SQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059540 445 IDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
250-512 |
2.60e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 250 VGDKKKHFDYQ-----PAPKGETVLSVQGltalhpsggyklndVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSG 324
Cdd:PRK15079 11 VADLKVHFDIKdgkqwFWQPPKTLKAVDG--------------VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 325 SVQLNG-ECIDKAHFQSRLKKglalvpEDrqgegvVQMM------SIQSNMTLSDF---SLQGFRrawkwlnPHKEQASV 394
Cdd:PRK15079 77 EVAWLGkDLLGMKDDEWRAVR------SD------IQMIfqdplaSLNPRMTIGEIiaePLRTYH-------PKLSRQEV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 395 KAMIQQLAIKVS-DPQL----PiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVM 468
Cdd:PRK15079 138 KDRVKAMMLKVGlLPNLinryP-HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLI 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 469 FSSSELDEVMALADRILVMADGRI----TAD----VPRHAVTRETLIAASTP 512
Cdd:PRK15079 217 FIAHDLAVVKHISDRVLVMYLGHAvelgTYDevyhNPLHPYTKALMSAVPIP 268
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
285-492 |
2.64e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGL-MPcQSGSVQLNGECIDKAHfQSRLKKGLALvpedRQGEGVV-QMM 362
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLeMP-RSGTLNIAGNHFDFSK-TPSDKAIREL----RRNVGMVfQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLsdfsLQGFRRA-WKWLNPHKEQASVKAM--IQQLAIKVSDPQLPItSLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:PRK11124 92 NLWPHLTV----QQNLIEApCRVLGLSKDQALARAEklLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 440 EPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-236 |
2.75e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.57 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGV-----ESPSSGQIIMDGIPVTLNSTHQAE-K 91
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEvR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 92 LGISIIFQELNLFPNMNVMDNIFMA---NEFFQ-KGKINEKYQYALAKSLL-ERLELDVDPYTplEELGIGHQQLVEIAR 166
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGvklNGLVKsKKELDERVEWALKKAALwDEVKDRLNDYP--SNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 167 ALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRgVTIIYISHRLEELMEIGDYITIFRDGRFISERP 236
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-239 |
2.89e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 34 DSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPS----SGQIIMDGIPVTLNSTHQAEKLgISIIFQELNLFpNMNV 109
Cdd:PTZ00265 1235 DMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTvfknSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSI 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 110 MDNIFMANEFFQKGKINEKYQYALAKSLLERL----ELDVDPYTplEELGIGHQQLVEIARALSKDTRVLIMDEPTSALS 185
Cdd:PTZ00265 1313 YENIKFGKEDATREDVKRACKFAAIDEFIESLpnkyDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 186 QSEVKVLFNVIEQLKRRG-VTIIYISHRLEELMEiGDYITIF----RDGRFISERPVND 239
Cdd:PTZ00265 1391 SNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAHGTHE 1448
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-181 |
3.61e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 16 VIIETHDLSRVYPGVVALDSVNYRVYRN-KVnVLIGENGAGKSTMMKMLAGVESPSSGQIIMdgipvtlnsthqAEKLGI 94
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVKL------------GETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQEL-NLFPNMNVMDNIfmaNEFFQKGKINEkyqyalAKSLLERL----EldvDPYTPLEELGIGHQQLVEIARALS 169
Cdd:COG0488 381 GYFDQHQeELDPDKTVLDEL---RDGAPGGTEQE------VRGYLGRFlfsgD---DAFKPVGVLSGGEKARLALAKLLL 448
|
170
....*....|..
gi 496059540 170 KDTRVLIMDEPT 181
Cdd:COG0488 449 SPPNVLLLDEPT 460
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
285-492 |
4.21e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.70 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPC---QSGSVQLNGECIDKAHFQSRLkkglALVpedRQGEGVVQM 361
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS----AYV---QQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTLS-DFSLQgfRRAWKwlnpHKEQASVKAMIQQLAI------KVSDPQLpITSLSGGNQQKVVLGKALMTQPQ 434
Cdd:TIGR00955 114 LTVREHLMFQaHLRMP--RRVTK----KEKRERVDEVLQALGLrkcantRIGVPGR-VKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 435 VVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS----SSELdevMALADRILVMADGRI 492
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSEL---FELFDKIILMAEGRV 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-211 |
4.82e-14 |
|
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: 74.44 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 11 SVESEVIIETHDLSRVYPGVVaLDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDgipvtlnsthqae 90
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 kLGISIIFQELNLFPNMNVMDNIFMANeffqKGKINEKYQYA-LAKSL-LERLeLDvdpyTPLEELGIGHQQLVEIARAL 168
Cdd:COG1245 401 -LKISYKPQYISPDYDGTVEEFLRSAN----TDDFGSSYYKTeIIKPLgLEKL-LD----KNVKDLSGGELQRVAIAACL 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496059540 169 SKDTRVLIMDEPTSAL---SQSEV-KVLFNVIEQlkrRGVTIIYISH 211
Cdd:COG1245 471 SRDADLYLLDEPSAHLdveQRLAVaKAIRRFAEN---RGKTAMVVDH 514
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
284-504 |
5.30e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 284 KLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPcQSGSVQLNGECID--KAHFQSRLKKGLAlvpedrQGEGVVQM 361
Cdd:PRK03695 11 RLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEawSAAELARHRAYLS------QQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTLSDFSLQgfrrawkwlNPHKEQASVKAMIQQLAIkvsDPQL--PITSLSGGNQQKVVL-GKALMTQP----- 433
Cdd:PRK03695 84 MPVFQYLTLHQPDKT---------RTEAVASALNEVAEALGL---DDKLgrSVNQLSGGEWQRVRLaAVVLQVWPdinpa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 434 -QVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRE 504
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-213 |
6.49e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 73.93 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 11 SVESEVIIETHDLSRVYPG-VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQA 89
Cdd:TIGR02868 328 VGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 90 EKLgISIIFQELNLFpNMNVMDNIFMANEffqkGKINEKYQYALAK----SLLERLELDVDpyTPLEELGI----GHQQL 161
Cdd:TIGR02868 408 RRR-VSVCAQDAHLF-DTTVRENLRLARP----DATDEELWAALERvglaDWLRALPDGLD--TVLGEGGArlsgGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 162 VEIARALSKDTRVLIMDEPTSALsqsEVKVLFNVIEQLKR--RGVTIIYISHRL 213
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHL---DAETADELLEDLLAalSGRTVVLITHHL 530
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
283-492 |
6.63e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.71 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 283 YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsRLKKGLALVPEDRQGEGVVQMM 362
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE-KLRKHIGIVFQNPDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLSDFSLqgfrrawkwlnPHKE-QASVKAMIQQ---LAIKVSDPQlpitSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:PRK13648 102 KYDVAFGLENHAV-----------PYDEmHRRVSEALKQvdmLERADYEPN----ALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS-SSELDEVMAlADRILVMADGRI 492
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTV 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-239 |
7.35e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ-AEKLgiSI 96
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElAKRL--AI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMNVMDNIfmanEF----FQKGKINEKYQYALAKSlLERLELD--VDPYtpLEELGIGHQQLVEIARALSK 170
Cdd:COG4604 80 LRQENHINSRLTVRELV----AFgrfpYSKGRLTAEDREIIDEA-IAYLDLEdlADRY--LDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 171 DTRVLIMDEPTSAL----SQSEVKVLFNVIEQLKRrgvTIIYISHrleelmEIG------DYITIFRDGRFISERPVND 239
Cdd:COG4604 153 DTDYVLLDEPLNNLdmkhSVQMMKLLRRLADELGK---TVVIVLH------DINfascyaDHIVAMKDGRVVAQGTPEE 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-235 |
8.88e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.36 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVY---------PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNS 85
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 86 THQAEKLgISIIFQE--LNLFPNMNV---MD-----NIFMANEFFQKGKINEKYQYALAKsllerlelDVDPYTPlEELG 155
Cdd:PRK15112 82 YSYRSQR-IRMIFQDpsTSLNPRQRIsqiLDfplrlNTDLEPEQREKQIIETLRQVGLLP--------DHASYYP-HMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 156 IGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLK-RRGVTIIYISHRLEELMEIGDYITIFRDGRFIsE 234
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV-E 230
|
.
gi 496059540 235 R 235
Cdd:PRK15112 231 R 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
268-492 |
1.06e-13 |
|
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: 70.69 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahfqsrlKK 344
Cdd:cd03258 1 MIELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTL-------LS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 345 GLALVPEDRQGEGVVQMMSIQSNMTLSD---FSLQgfrrAWKWlnPHKEQAS-VKAMIQQ--LAIKVSD-PqlpiTSLSG 417
Cdd:cd03258 74 GKELRKARRRIGMIFQHFNLLSSRTVFEnvaLPLE----IAGV--PKAEIEErVLELLELvgLEDKADAyP----AQLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 418 GNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
268-490 |
1.34e-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: 73.89 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHP-SGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfQSRLKKGL 346
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN--ISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 347 ALVPedrQGEGVVQMMSIQSNMTLSDfSLQGFrrawkwlnPHKEQASVKAM-IQQLAIKVSDPQLPITsLSGGNQQKVVL 425
Cdd:TIGR01257 2015 GYCP---QFDAIDDLLTGREHLYLYA-RLRGV--------PAEEIEKVANWsIQSLGLSLYADRLAGT-YSGGNKRKLST 2081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 426 GKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADG 490
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-230 |
1.48e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.21 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVY-PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNStHQAEKLGISI 96
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQelnlfpnmnvmDNIFMANEFF------------QKGKINEKYQYA-LAKSLLERLeldvdpYTPLEE----LGIGHQ 159
Cdd:PRK10790 420 VQQ-----------DPVVLADTFLanvtlgrdiseeQVWQALETVQLAeLARSLPDGL------YTPLGEqgnnLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 160 QLVEIARALSKDTRVLIMDEPT----SALSQSEVKVLfnvieQLKRRGVTIIYISHRLEELMEiGDYITIFRDGR 230
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATanidSGTEQAIQQAL-----AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-230 |
1.51e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.53 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ-AEKLGI-- 94
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElARRRAVlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 --SiifqELNlFPnmnvmdniFMANEFFQKGKINEKYQYALAKSLLER-LEL-DVD-----PYTpleELGIGHQQLVEIA 165
Cdd:COG4559 82 qhS----SLA-FP--------FTVEEVVALGRAPHGSSAAQDRQIVREaLALvGLAhlagrSYQ---TLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 166 RAL-------SKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:COG4559 146 RVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
279-495 |
1.65e-13 |
|
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: 70.21 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 279 PSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGE---CIDKAHFQSRLkkGLALvpedrqG 355
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaLADPAWLRRQV--GVVL------Q 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 356 EGVVQMMSIQSNMTLSDfslqgfrrawkwlnphkEQASVKAMIQqlAIKVSDP-----QLPI----------TSLSGGNQ 420
Cdd:cd03252 84 ENVLFNRSIRDNIALAD-----------------PGMSMERVIE--AAKLAGAhdfisELPEgydtivgeqgAGLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 421 QKVVLGKALMTQPQVVFLDEPTRGIDvgakTDVYHLIGKMAQQ---GLAVMFSSSELDEVMAlADRILVMADGRITAD 495
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALD----YESEHAIMRNMHDicaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
285-498 |
1.71e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.90 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahfqsrlkkglaLVPEDRQGEGVVQMMSI 364
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH------------VPAENRHVNTVFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSD---FSLQGFRRAWKWLNPHKEQASvkAMIQ--QLAikvsdpQLPITSLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:PRK09452 98 FPHMTVFEnvaFGLRMQKTPAAEITPRVMEAL--RMVQleEFA------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 440 EPTRGIDvgaktdvYHLIGKMA--------QQGLAVMFSSSELDEVMALADRILVMADGRITAD-VPR 498
Cdd:PRK09452 170 ESLSALD-------YKLRKQMQnelkalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDgTPR 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
284-500 |
1.87e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.00 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 284 KLNDVT---------FSLS--KGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEciDKAhfqsrlkkglALVPED 352
Cdd:PRK10771 3 KLTDITwlyhhlpmrFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHT----------TTPPSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 353 R------QGEGVVQMMSIQSNMTLSdfslqgfrrawkwLNP-----HKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQ 421
Cdd:PRK10771 71 RpvsmlfQENNLFSHLTVAQNIGLG-------------LNPglklnAAQREKLHAIARQMGIEDLLARLP-GQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 422 KVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHA 500
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
31-234 |
2.32e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.50 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 31 VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPvTLNSTHQAE---KLGIsiIFQElnlfPNM 107
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWDirnKAGM--VFQN----PDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 108 NVMDNIFMANEFF-------QKGKINEKYQYALAKsllerleldVDPYT----PLEELGIGHQQLVEIARALSKDTRVLI 176
Cdd:PRK13633 97 QIVATIVEEDVAFgpenlgiPPEEIRERVDESLKK---------VGMYEyrrhAPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 177 MDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEiGDYITIFRDGRFISE 234
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
283-503 |
2.42e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.53 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 283 YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAH-FQSRLKKGLALVPEDRQGEGVvqm 361
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvWDIRHKIGMVFQNPDNQFVGA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 msiqsnmTLSD---FSL--QGFrrawkwlnPHKEQAS----VKAMIQQLAIKVSDPqlpiTSLSGGNQQKVVLGKALMTQ 432
Cdd:PRK13650 98 -------TVEDdvaFGLenKGI--------PHEEMKErvneALELVGMQDFKEREP----ARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 433 PQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVmALADRILVMADGRI-TADVPRHAVTR 503
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVeSTSTPRELFSR 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
278-492 |
4.02e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.63 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 278 HPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHFQS--RLKKGLALVPEDRQG 355
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKlqGIRKLVGIVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 356 EGVVQmmSIQSNMTLSDFSLqgfrrawkWLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQV 435
Cdd:PRK13644 89 QFVGR--TVEEDLAFGPENL--------CLPPIEIRKRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 436 VFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMAlADRILVMADGRI 492
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKI 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-508 |
4.06e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDK------AHFQSRL----KKGLAlvPEdrq 354
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpeykrAKYIGRVfqdpMMGTA--PS--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 355 gegvvqmMSIQSNMTLSDfsLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDpQL--PITSLSGGNQQKVVLGKALMTQ 432
Cdd:COG1101 97 -------MTIEENLALAY--RRGKRRGLRRGLTKKRRELFRELLATLGLGLEN-RLdtKVGLLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 433 PQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITADVP---RHAVTRETLIA 508
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSgeeKKKLTVEDLLE 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
266-510 |
5.76e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQS-RLKK 344
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 345 GLALVPEDRQgegvVQMMSIQSNMTlsdFSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKvsdpqlPITSLSGGNQQKVV 424
Cdd:PRK13647 82 GLVFQDPDDQ----VFSSTVWDDVA---FGPVNMGLDKDEVERRVEEALKAVRMWDFRDK------PPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 425 LGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAVTRE 504
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
....*.
gi 496059540 505 TLIAAS 510
Cdd:PRK13647 229 DIVEQA 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
285-498 |
5.78e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 68.16 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqSRLKKglALVPEDRQGEGVV-QMMS 363
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL------SRLKR--REIPYLRRRIGVVfQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 IQSNMTLSD---FSLQ--GFrrawkwlnPHKE-QASVKAMIQQLAIKVSDPQLPITsLSGGNQQKVVLGKALMTQPQVVF 437
Cdd:COG2884 90 LLPDRTVYEnvaLPLRvtGK--------SRKEiRRRVREVLDLVGLSDKAKALPHE-LSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 438 LDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPR 498
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
415-508 |
6.01e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.81 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90
....*....|....
gi 496059540 495 DVPRHAVTRETLIA 508
Cdd:PRK10938 216 TGEREEILQQALVA 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-231 |
6.52e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.58 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVV--ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNsthqaeklgI 94
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---------I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPNMNVMDNIFMANEFFqkgkinekYQYALAKSLLERlELDVDPYTPLEELGI-------------GHQQL 161
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHL--------YLYARLRGVPAE-EIEKVANWSIQSLGLslyadrlagtysgGNKRK 2078
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 162 VEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRF 231
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
268-509 |
6.66e-13 |
|
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: 69.70 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMP---CQSGSVQLNGECI---DKAHF 338
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 339 QSRLKKGLALVPEDrqgegvvQMMSIQSNMTLSDfSLQGFRRAWKWLNPHKEQASVKAMIQQLAIkvSDPQLPITS---- 414
Cdd:COG0444 81 RKIRGREIQMIFQD-------PMTSLNPVMTVGD-QIAEPLRIHGGLSKAEARERAIELLERVGL--PDPERRLDRyphe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI- 492
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIv 230
|
250 260
....*....|....*....|....
gi 496059540 493 ----TADV---PRHAVTReTLIAA 509
Cdd:COG0444 231 eegpVEELfenPRHPYTR-ALLSS 253
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
30-225 |
7.26e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.55 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVeSPSSGQIIMD-----GIPVTLNSTHQAEKL---GISIIFQEL 101
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLSPRERRKIigrEIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 102 N--LFPNMNVMDNIF--MANEFFqKGKI----NEKYQYalAKSLLERLE-------LDVDPYtpleELGIGHQQLVEIAR 166
Cdd:COG4170 99 SscLDPSAKIGDQLIeaIPSWTF-KGKWwqrfKWRKKR--AIELLHRVGikdhkdiMNSYPH----ELTEGECQKVMIAM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 167 ALSKDTRVLIMDEPTSAL---SQSEVKVLFNVIEQLkrRGVTIIYISHRLEELMEIGDYITI 225
Cdd:COG4170 172 AIANQPRLLIADEPTNAMestTQAQIFRLLARLNQL--QGTSILLISHDLESISQWADTITV 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
414-498 |
7.39e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.55 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 414 SLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
90
....*....|
gi 496059540 493 ----TADVPR 498
Cdd:PRK11247 213 gldlTVDLPR 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
285-490 |
1.02e-12 |
|
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: 67.49 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAH------FQSrlkkgLALVPedrqgegv 358
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpdrmvvFQN-----YSLLP-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 359 vqMMSIQSNMTLSdfslqgFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:TIGR01184 68 --WLTVRENIALA------VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRP-GQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADG 490
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
287-504 |
1.20e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 287 DVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDkaHFQSR-LKKGLALVPEDRQGEGVVqmmSIQ 365
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKeVARRIGLLAQNATTPGDI---TVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 366 SNMTLSDFSLQGFRRAWKwlnPHKEQASVKAM----IQQLAIKVSDpqlpitSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:PRK10253 100 ELVARGRYPHQPLFTRWR---KEDEEAVTKAMqatgITHLADQSVD------TLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 442 TRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITAD-VPRHAVTRE 504
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQgAPKEIVTAE 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
261-467 |
1.22e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 70.08 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 261 PAPKGETVLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfQS 340
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD-QD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 341 RLKKGLALVPEDRQgegvVQMMSIQSNMTLS--DFSLQGFRRAWkwlnphkEQASVKAMIQQLAIKVSDPQLPI-TSLSG 417
Cdd:TIGR02868 406 EVRRRVSVCAQDAH----LFDTTVRENLRLArpDATDEELWAAL-------ERVGLADWLRALPDGLDTVLGEGgARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059540 418 GNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKmAQQGLAV 467
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTV 523
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
259-511 |
1.26e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 259 YQPAP-KGETVLSVQGLTALH----PSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLnGECI 333
Cdd:PRK13631 11 KVPNPlSDDIILRVKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 334 DKAHFQS----------------RLKKGLALV---PEdrqgegvVQMM--SIQSNMTLSDFSLqgfrrawkwlNPHKEQA 392
Cdd:PRK13631 90 IGDKKNNhelitnpyskkiknfkELRRRVSMVfqfPE-------YQLFkdTIEKDIMFGPVAL----------GVKKSEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 393 SVKAMIQQLAIKVSDPQLPIT--SLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS 470
Cdd:PRK13631 153 KKLAKFYLNKMGLDDSYLERSpfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 496059540 471 SSELDEVMALADRILVMADGRI-TADVPRHAVTRETLIAAST 511
Cdd:PRK13631 233 THTMEHVLEVADEVIVMDKGKIlKTGTPYEIFTDQHIINSTS 274
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
267-494 |
1.28e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.96 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 267 TVLSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI-----DKAH- 337
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgaDRGVv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 338 FQSRlkkglALVPedrqgegvvqMMSIQSNMTLSdFSLQGFRRAwkwlnphKEQASVKAMIQQLAIKVSDpQLPITSLSG 417
Cdd:COG4525 82 FQKD-----ALLP----------WLNVLDNVAFG-LRLRGVPKA-------ERRARAEELLALVGLADFA-RRRIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 418 GNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMAD--GRITA 494
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
285-492 |
1.28e-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: 67.30 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ---SGSVQLNGECIDKAHFQSRLkkglALVPEDRQgegvvqm 361
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKCV----AYVRQDDI------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 msIQSNMTLSD---FSLQgFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLpITSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:cd03234 92 --LLPGLTVREtltYTAI-LRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNL-VKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS----SSELDEvmaLADRILVMADGRI 492
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTihqpRSDLFR---LFDRILLLSSGEI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
266-513 |
1.43e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLT-ALHPSGGY--KLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQlngecIDKAHFQSRL 342
Cdd:PRK10261 10 RDVLAVENLNiAFMQEQQKiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-----CDKMLLRRRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 KKGLALVPED----RQGEGVVQMMSIQSNMT-LSDFSLQGFR-----RAWKWLNPHKEQASVKAMIQQLAIKVSDPQLP- 411
Cdd:PRK10261 85 RQVIELSEQSaaqmRHVRGADMAMIFQEPMTsLNPVFTVGEQiaesiRLHQGASREEAMVEAKRMLDQVRIPEAQTILSr 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 412 -ITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIgKMAQQGLA--VMFSSSELDEVMALADRILVMA 488
Cdd:PRK10261 165 yPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI-KVLQKEMSmgVIFITHDMGVVAEIADRVLVMY 243
|
250 260 270
....*....|....*....|....*....|...
gi 496059540 489 DGRI--TADV------PRHAVTRETLiaASTPQ 513
Cdd:PRK10261 244 QGEAveTGSVeqifhaPQHPYTRALL--AAVPQ 274
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-233 |
1.44e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPvtLNSTHQ---AEKLG 93
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP--LDYSKRgllALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQElnlfPNMNVMDNIFMANEFFQKGKINEKyQYALAKSLLERLELdVDP----YTPLEELGIGHQQLVEIARALS 169
Cdd:PRK13638 79 VATVFQD----PEQQIFYTDIDSDIAFSLRNLGVP-EAEITRRVDEALTL-VDAqhfrHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 170 KDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFIS 233
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
253-504 |
2.03e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.55 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 253 KKKHFDYQPAPkgETVLSVQGLTalhpsggyklnDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEC 332
Cdd:PRK13641 4 KFENVDYIYSP--GTPMEKKGLD-----------NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 333 I-----DKAHFQSRLKKGLAL-VPEDRQGEGVV--QMMSIQSNMTLSDfslqgfrrawkwlnphkEQASVKAM--IQQLA 402
Cdd:PRK13641 71 ItpetgNKNLKKLRKKVSLVFqFPEAQLFENTVlkDVEFGPKNFGFSE-----------------DEAKEKALkwLKKVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 403 IKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALAD 482
Cdd:PRK13641 134 LSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYAD 213
|
250 260
....*....|....*....|..
gi 496059540 483 RILVMADGRITadvpRHAVTRE 504
Cdd:PRK13641 214 DVLVLEHGKLI----KHASPKE 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
267-492 |
2.03e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.49 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 267 TVLSVQGLTALHPsggyklndVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQsGSVQLNGecidkahfqsrlkkgl 346
Cdd:PRK11174 356 EILSPDGKTLAGP--------LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKING---------------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 347 alvpedrqgegvvqmmsiqsnMTLSDFSLQGFRRAWKWL--NPHKEQASVK------------AMIQQL--AIKVSD--P 408
Cdd:PRK11174 411 ---------------------IELRELDPESWRKHLSWVgqNPQLPHGTLRdnvllgnpdasdEQLQQAleNAWVSEflP 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 409 QLPI----------TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSS--SELDE 476
Cdd:PRK11174 470 LLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHqlEDLAQ 549
|
250
....*....|....*.
gi 496059540 477 VmalaDRILVMADGRI 492
Cdd:PRK11174 550 W----DQIWVMQDGQI 561
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
285-492 |
2.48e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 68.25 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGE--CIDKaHFQSRlKKGL-----ALVPedrqgeg 357
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTNL-PPRER-RVGFvfqhyALFP------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 358 vvqmmsiqsNMTLSD---FSLQGfrrawkwLNPHKEQAsvKAMIQQLAIKVsdpQLP------ITSLSGGNQQKVVLGKA 428
Cdd:COG1118 89 ---------HMTVAEniaFGLRV-------RPPSKAEI--RARVEELLELV---QLEgladryPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 429 LMTQPQVVFLDEPTRGIDVGAKTDV------YHligkmAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELrrwlrrLH-----DELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-223 |
2.54e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 11 SVESEVIIETHDLSRVYPGVVaLDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIImdgipvtlnsthqaE 90
Cdd:PRK13409 334 ESERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--------------P 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGISIIFQELNLFPNMNVMDNIFMANEFFQkgkiNEKYQYALAKSL-LERLeLDvdpyTPLEELGIGHQQLVEIARALS 169
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVEDLLRSITDDLG----SSYYKSEIIKPLqLERL-LD----KNVKDLSGGELQRVAIAACLS 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 170 KDTRVLIMDEPTSALSQSE----VKVLFNVIEQlkrRGVTIIYISHrleELMEIgDYI 223
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEQrlavAKAIRRIAEE---REATALVVDH---DIYMI-DYI 520
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
269-492 |
2.64e-12 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 66.56 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdKAHFQSRLKKGLAL 348
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 349 VPedrQGEGVVQMMSIQSNMTLSDfSLQGfrraWKwlnPHKEQASVKAMIQQLAIkvsDPQ-----LPiTSLSGGNQQKV 423
Cdd:cd03295 80 VI---QQIGLFPHMTVEENIALVP-KLLK----WP---KEKIRERADELLALVGL---DPAefadrYP-HELSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 424 VLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
285-496 |
2.68e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahFQSRLKKGLalvpedRQGE-GVVqmms 363
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--LSSAAKAEL------RNQKlGFI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 IQSNMTLSDFS-LQGFrrAWKWL----NPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:PRK11629 93 YQFHHLLPDFTaLENV--AMPLLigkkKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDevmaLADRI---LVMADGRITADV 496
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ----LAKRMsrqLEMRDGRLTAEL 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
269-490 |
2.88e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 66.65 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPsGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQsrlkKGLAL 348
Cdd:PRK11248 2 LQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 349 vpedrQGEGVVQMMSIQSNMTLSdFSLQGFRRAwkwlnphKEQASVKAMIQQLAIKVSDpQLPITSLSGGNQQKVVLGKA 428
Cdd:PRK11248 77 -----QNEGLLPWRNVQDNVAFG-LQLAGVEKM-------QRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 429 LMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADG 490
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
31-234 |
3.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 31 VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNST-----HQAEKLGISIIFQELNLFP 105
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 106 nmnvmDNIFMANEFFQKG-KINEKYQYALAKSLLERL--ELDVDPYTPLEELGiGHQQLVEIARALSKDTRVLIMDEPTS 182
Cdd:PRK13646 101 -----DTVEREIIFGPKNfKMNLDEVKNYAHRLLMDLgfSRDVMSQSPFQMSG-GQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 183 AL---SQSEVKVLFNVIeQLKrRGVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK13646 175 GLdpqSKRQVMRLLKSL-QTD-ENKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-495 |
3.22e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecidkahfqsrlkkglaLVPEDRQGE-----GVV 359
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----------------YVPFKRRKEfarriGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 qmMSIQS----NMTLSDfSLQGFRRAWKwLNPHKEQASVKAMIQQLAIkvsDPQL--PITSLSGGNQQKVVLGKALMTQP 433
Cdd:COG4586 101 --FGQRSqlwwDLPAID-SFRLLKAIYR-IPDAEYKKRLDELVELLDL---GELLdtPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 434 QVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-233 |
3.85e-12 |
|
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: 65.51 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVY----PGVvaLDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVtlnSTHQAEKL- 92
Cdd:cd03369 7 IEVENLSVRYapdlPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 93 -GISIIFQELNLFPNmNVMDNIFMANEFfqkgkinekyqyalaksllerleLDVDPYTPL------EELGIGHQQLVEIA 165
Cdd:cd03369 82 sSLTIIPQDPTLFSG-TIRSNLDPFDEY-----------------------SDEEIYGALrvseggLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 166 RALSKDTRVLIMDEPTSAL-SQSEVKVLFNVIEQLKrrGVTIIYISHRLEELMEIgDYITIFRDGRFIS 233
Cdd:cd03369 138 RALLKRPRVLVLDEATASIdYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
266-491 |
4.59e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.53 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLT---ALHPSGGYKL---NDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLN--GECIDKAH 337
Cdd:COG4778 2 TTLLEVENLSktfTLHLQGGKRLpvlDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 338 FQSRLKkgLALvpedRQGE-GVVqmmsiqsnmtlSDF---------------SL--QGFRRawkwlnphkEQASVKA--M 397
Cdd:COG4778 82 ASPREI--LAL----RRRTiGYV-----------SQFlrviprvsaldvvaePLleRGVDR---------EEARARAreL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 398 IQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVM--FSSselD 475
Cdd:COG4778 136 LARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgiFHD---E 212
|
250
....*....|....*..
gi 496059540 476 EVM-ALADRILVMADGR 491
Cdd:COG4778 213 EVReAVADRVVDVTPFS 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
285-504 |
4.98e-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: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfqsrlKKGLALVpedRQGEGVV----- 359
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDS------KKDINKL---RRKVGMVfqqfn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 --QMMSIQSNMTLsdfslqGFRRAWKWlnpHKEQASVKAMiQQLAiKV--SD-----PqlpiTSLSGGNQQKVVLGKALM 430
Cdd:COG1126 88 lfPHLTVLENVTL------APIKVKKM---SKAEAEERAM-ELLE-RVglADkadayP----AQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 431 TQPQVVFLDEPTRGID---VGaktDVYHLIGKMAQQGLAVMFSSSELD---EVmalADRILVMADGRI-----TADV--- 496
Cdd:COG1126 153 MEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGfarEV---ADRVVFMDGGRIveegpPEEFfen 226
|
....*...
gi 496059540 497 PRHAVTRE 504
Cdd:COG1126 227 PQHERTRA 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
285-477 |
5.87e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqsrlkkgLALVPED-RQgegvvQM-M 362
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI------------STLKPEIyRQ-----QVsY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLSDFSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPT 442
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 496059540 443 RGIDVGAKTDVYHLIGKMA-QQGLAVMFSSSELDEV 477
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEI 201
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
266-500 |
5.94e-12 |
|
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: 65.53 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTALHPSGGYKLN---DVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqSRL 342
Cdd:COG4181 6 APIIELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL------FAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 -KKGLALVpeDRQGEGVVQmmsiQS-----NMT--------LSdfsLQGFRRAwkwlnphKEQAsvKAMIQQLAikVSD- 407
Cdd:COG4181 80 dEDARARL--RARHVGFVF----QSfqllpTLTalenvmlpLE---LAGRRDA-------RARA--RALLERVG--LGHr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 408 ----PQlpitSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDvgAKTdvyhligkmAQQGLAVMFsssELDE------V 477
Cdd:COG4181 140 ldhyPA----QLSGGEQQRVALARAFATEPAILFADEPTGNLD--AAT---------GEQIIDLLF---ELNRergttlV 201
|
250 260 270
....*....|....*....|....*....|.
gi 496059540 478 M-----ALA---DRILVMADGRITADVPRHA 500
Cdd:COG4181 202 LvthdpALAarcDRVLRLRAGRLVEDTAATA 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
285-495 |
6.30e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLN-------------GECIDKAHFQSRLKKGLALVPE 351
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekEKVLEKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 352 DRQGEGVV------QMM--SIQSNMTLSDFSLqgfrrawkwlNPHKEQASVKA--MIQQLAIKVSDPQLPITSLSGGNQQ 421
Cdd:PRK13651 103 IRRRVGVVfqfaeyQLFeqTIEKDIIFGPVSM----------GVSKEEAKKRAakYIELVGLDESYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 422 KVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKD 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
284-495 |
6.35e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 284 KLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAH-FQSRLKKGLALVPEDRQGEGVvqmm 362
Cdd:PRK13642 22 QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvWNLRRKIGMVFQNPDNQFVGA---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLSdFSLQGFRRAwkwlNPHKEQASVKAMIQQLAIKVSDPqlpiTSLSGGNQQKVVLGKALMTQPQVVFLDEPT 442
Cdd:PRK13642 98 TVEDDVAFG-MENQGIPRE----EMIKRVDEALLAVNMLDFKTREP----ARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 443 RGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVmALADRILVMADGRITAD 495
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKE 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
285-492 |
6.62e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.37 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDK---AHFQSRLKKGLALVpedrqgegvVQM 361
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdAELREVRRKKIAMV---------FQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTLSDFSLQGFRRAWKWLNPHKEQASvkAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMELAGINAEERREKAL--DALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 442 TRGIDVGAKTDVY-HLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK10070 192 FSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-213 |
6.68e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.56 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 16 VIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQ-AEKLGi 94
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 sIIFQELNL-FPnMNVMDNIFMANEFFQKGKINEKyqyALAKSLLERLELdvdpyTPLE-----ELGIGHQQLVEIARAL 168
Cdd:PRK13548 80 -VLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDD---ALVAAALAQVDL-----AHLAgrdypQLSGGEQQRVQLARVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 169 ------SKDTRVLIMDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRL 213
Cdd:PRK13548 150 aqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDL 201
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
285-492 |
6.73e-12 |
|
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: 65.33 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSrLKKGLALVPEDrqgegvvqmmSI 364
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQD----------TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLsdfslqGFRRAWKWLNPHKEQ---ASVKAMIQQLAIKVSDPQLPI-----TSLSGGNQQKVVLGKALMTQPQVV 436
Cdd:cd03253 86 LFNDTI------GYNIRYGRPDATDEEvieAAKAAQIHDKIMRFPDGYDTIvgergLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 437 FLDEPTRGIDVGAKTDVYHLIGKMAqQGLAVMFSSSELDEVMAlADRILVMADGRI 492
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
285-512 |
7.01e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI---DKAHFQSRLKKglalvpedrqgegvVQM 361
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQK--------------IQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MsiqsnmtlsdfslqgFRRAWKWLNPHKE--------------------QASVKAMIQQLAIKVSD----PQLpitsLSG 417
Cdd:PRK11308 97 V---------------FQNPYGSLNPRKKvgqileepllintslsaaerREKALAMMAKVGLRPEHydryPHM----FSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 418 GNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGR----- 491
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRcvekg 237
|
250 260
....*....|....*....|....*
gi 496059540 492 ----ITADvPRHAVTRETLiaASTP 512
Cdd:PRK11308 238 tkeqIFNN-PRHPYTQALL--SATP 259
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-232 |
7.65e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 2 QQQDIVTPHS---VESEVIIETHDLSRVYPG--VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIM 76
Cdd:PRK11160 320 QKPEVTFPTTstaAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 77 DGIPVTlNSTHQAEKLGISIIFQELNLFpNMNVMDNIFMANEffqkGKINEKYQYALAKSLLERLeLDVDPytPLEE-LG 155
Cdd:PRK11160 400 NGQPIA-DYSEAALRQAISVVSQRVHLF-SATLRDNLLLAAP----NASDEALIEVLQQVGLEKL-LEDDK--GLNAwLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 156 IGHQQL-------VEIARALSKDTRVLIMDEPTSAL-SQSEVKVLFNVIEQLKRRgvTIIYISHRLEElMEIGDYITIFR 227
Cdd:PRK11160 471 EGGRQLsggeqrrLGIARALLHDAPLLLLDEPTEGLdAETERQILELLAEHAQNK--TVLMITHRLTG-LEQFDRICVMD 547
|
....*
gi 496059540 228 DGRFI 232
Cdd:PRK11160 548 NGQII 552
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
48-230 |
7.95e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.81 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMdGIPVTLNSTHQAE------KLGISIIFQELNLFPNMNVMDNIFmaneffq 121
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKlkplrkKVGIVFQFPEHQLFEETVEKDICF------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 122 kGKIN----EKYQYALAKSLLERLELDVD-----PYtpleELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVL 192
Cdd:PRK13634 110 -GPMNfgvsEEDAKQKAREMIELVGLPEEllarsPF----ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059540 193 FNVIEQL-KRRGVTIIYISHRLEELMEIGDYI------TIFRDGR 230
Cdd:PRK13634 185 MEMFYKLhKEKGLTTVLVTHSMEDAARYADQIvvmhkgTVFLQGT 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-212 |
8.28e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.33 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP-GVVALDSVNYRVYRNKvNVLI-GENGAGKSTMMKMLAGVESPSSGQIIMdgiPvtlnsthqaeklgis 95
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGD-RLLItGPSGTGKSSLFRALAGLWPWGSGRIGM---P--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 iifqelnlfPNMNVMdniFMAneffQKGkinekyqYALAKSLLERLEldvdpYTPLEELGIGHQQLVEIARALSKDTRVL 175
Cdd:cd03223 62 ---------EGEDLL---FLP----QRP-------YLPLGTLREQLI-----YPWDDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059540 176 IMDEPTSALS-QSEVKVLfnviEQLKRRGVTIIYISHR 212
Cdd:cd03223 114 FLDEATSALDeESEDRLY----QLLKELGITVISVGHR 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
266-510 |
1.15e-11 |
|
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: 67.02 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLT-ALHPSGGYK--LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMP----CQSGSVQLNGECIdkahf 338
Cdd:COG4172 4 MPLLSVEDLSvAFGQGGGTVeaVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 339 qsrlkkgLALVPEDRQG-EGVVQMMSIQSNMTlsdfSL-----------------QGFRRAwkwlnphKEQASVKAMIQQ 400
Cdd:COG4172 79 -------LGLSERELRRiRGNRIAMIFQEPMT----SLnplhtigkqiaevlrlhRGLSGA-------AARARALELLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 401 LAIKvsDPQLPITS----LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELD 475
Cdd:COG4172 141 VGIP--DPERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLG 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 496059540 476 EVMALADRILVMADGRI-----TADV---PRHAVTREtLIAAS 510
Cdd:COG4172 219 VVRRFADRVAVMRQGEIveqgpTAELfaaPQHPYTRK-LLAAE 260
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
262-509 |
1.38e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.52 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 262 APKGETVLSVQGLTALHPSGG----------YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGE 331
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 332 CIDKAhfqsrlkKGLALVPEDRQgegvVQMM------SIQSNMTLSD-----FSLQGfrrawkwLNPHKE-QASVKAMIQ 399
Cdd:COG4608 81 DITGL-------SGRELRPLRRR----MQMVfqdpyaSLNPRMTVGDiiaepLRIHG-------LASKAErRERVAELLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 400 QLAIKVSD----PQlpitSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSEL 474
Cdd:COG4608 143 LVGLRPEHadryPH----EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDL 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 496059540 475 DEVMALADRILVMADGRI--TADV------PRHAVTReTLIAA 509
Cdd:COG4608 219 SVVRHISDRVAVMYLGKIveIAPRdelyarPLHPYTQ-ALLSA 260
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
33-217 |
1.70e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.36 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDgipvtlnsthqaEKLGISIIFQELNLFPNMNVMDN 112
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN------------GKLRIGYVPQKLYLDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFMA-NEFFQKGKINEKYQYALAKSLLERleldvdpytPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKV 191
Cdd:PRK09544 88 RFLRlRPGTKKEDILPALKRVQAGHLIDA---------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|....*..
gi 496059540 192 LFNVIEQLKRR-GVTIIYISHRLEELM 217
Cdd:PRK09544 159 LYDLIDQLRRElDCAVLMVSHDLHLVM 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
48-218 |
2.03e-11 |
|
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: 66.89 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAeKLGISIIFQELNLFPN---MNVmdnifmaNEFFQKGk 124
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDPVLFSGslrMNL-------DPFSQYS- 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 125 iNEKYQYALAKSLLERL------ELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSA-------LSQSEVKV 191
Cdd:TIGR00957 1388 -DEEVWWALELAHLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAvdletdnLIQSTIRT 1466
|
170 180
....*....|....*....|....*..
gi 496059540 192 LFNvieqlkrrGVTIIYISHRLEELME 218
Cdd:TIGR00957 1467 QFE--------DCTVLTIAHRLNTIMD 1485
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
285-492 |
2.07e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 63.64 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdKAHFQSRLKKGLALVPEdrqgEGVVQMMSI 364
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKYLHSKVSLVGQ----EPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMT--LSDFSLQGFRRAWKWLNPHkeqasvkAMIQQLAIKVS-DPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:cd03248 105 QDNIAygLQSCSFECVKEAAQKAHAH-------SFISELASGYDtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 442 TRGIDVGAKTDVYHLIgKMAQQGLAVMFSSSELDEVMAlADRILVMADGRI 492
Cdd:cd03248 178 TSALDAESEQQVQQAL-YDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
33-214 |
2.10e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDgipvtlnsthqaeklgisiiFQELNLFPNMNVMDN 112
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--------------------VPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFMANEFfqkgkinekyqyALAKSLLERLELdVDPYT---PLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEV 189
Cdd:COG2401 106 IGRKGDF------------KDAVELLNAVGL-SDAVLwlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|....*.
gi 496059540 190 KVL-FNVIEQLKRRGVTIIYISHRLE 214
Cdd:COG2401 173 KRVaRNLQKLARRAGITLVVATHHYD 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-236 |
2.36e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 29 GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-------LNSTHQAEKLGISiifqel 101
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqknlVAYVPQSEEVDWS------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 102 nlFPNMnvMDNIFMANEFFQKG--KINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDE 179
Cdd:PRK15056 93 --FPVL--VEDVVMMGRYGHMGwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 180 PTSALS-QSEVKVLfNVIEQLKRRGVTIIYISHRLEELMEIGDYiTIFRDGRFISERP 236
Cdd:PRK15056 169 PFTGVDvKTEARII-SLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGP 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-211 |
2.46e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNS-THQAEKLGisi 96
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEACHYLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 ifqELN-LFPNMNVMDNIfmanEFFQKGKINEKYQYALAkslLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVL 175
Cdd:PRK13539 80 ---HRNaMKPALTVAENL----EFWAAFLGGEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 496059540 176 IMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISH 211
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
33-232 |
2.53e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGveSPS----SGQIIMDGIPVTLNSTHQAEKLGISIIFQ---ELNLFP 105
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHLGIFLAFQypiEIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 106 NMNVMDNIFMANEFFQKGK----------INEKYQYA-LAKSLLERlelDVDpytplEELGIGHQQLVEIARALSKDTRV 174
Cdd:CHL00131 101 NADFLRLAYNSKRKFQGLPeldplefleiINEKLKLVgMDPSFLSR---NVN-----EGFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 175 LIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISH--RLEELMeIGDYITIFRDGRFI 232
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDYI-KPDYVHVMQNGKII 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-232 |
2.59e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 12 VESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIM---DGIPVTLNSTHQ 88
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 89 AEK-------LGisiifqelnlFPNMNVMD----------NI---FMANEFFQKGKINEKyqyalAKSLLERLELDVD-- 146
Cdd:PRK11701 81 AERrrllrteWG----------FVHQHPRDglrmqvsaggNIgerLMAVGARHYGDIRAT-----AGDWLERVEIDAAri 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 147 ---PYTpleeLGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDY 222
Cdd:PRK11701 146 ddlPTT----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHR 221
|
250
....*....|
gi 496059540 223 ITIFRDGRFI 232
Cdd:PRK11701 222 LLVMKQGRVV 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
285-492 |
2.73e-11 |
|
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: 65.92 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfQSRLKKGLALVPEdrqgEGVVQMMSI 364
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID-RHTLRQFINYLPQ----EPYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDfslqgfrrawkwlNPHKEQASVKAMIQQLAIKVSDPQLPI----------TSLSGGNQQKVVLGKALMTQPQ 434
Cdd:TIGR01193 565 LENLLLGA-------------KENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 435 VVFLDEPTRGIDVGAKTDVYHLIGKMAQQglAVMFSSSELdEVMALADRILVMADGRI 492
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-251 |
3.02e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 12 VESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQAE 90
Cdd:PRK10253 2 TESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 KLGI---------SIIFQELnlfpnmnVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDPytpLEELGIGHQQL 161
Cdd:PRK10253 82 RIGLlaqnattpgDITVQEL-------VARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQS---VDTLSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 162 VEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKR-RGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDA 240
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
250
....*....|.
gi 496059540 241 SIPWIIEQMVG 251
Cdd:PRK10253 232 VTAELIERIYG 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
285-493 |
3.41e-11 |
|
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: 66.12 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEcidkahfqsrlkkgLALVPEdrqgEGVVQMMSI 364
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ----QAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSdfslqgfrrawKWLNPHKEQASVK--AMIQQLAIKVSDPQLPI----TSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:TIGR00957 716 RENILFG-----------KALNEKYYQQVLEacALLPDLEILPSGDRTEIgekgVNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 439 DEPTRGIDVGAKTDVY-HLIGKMA----QQGLAVMFSSSELDEVmalaDRILVMADGRIT 493
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFeHVIGPEGvlknKTRILVTHGISYLPQV----DVIIVMSGGKIS 840
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
288-484 |
3.62e-11 |
|
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: 62.51 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 288 VTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfQSRLKKGLALVPedrQGEGVVQMMSIQSN 367
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ--RDSIARGLLYLG---HAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 368 MTLsdfslqgfrrawkWLNPHKEQASVKAMIQQLAIKVSDpqLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDV 447
Cdd:cd03231 94 LRF-------------WHADHSDEQVEEALARVGLNGFED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 496059540 448 -GAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRI 484
Cdd:cd03231 159 aGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
269-491 |
3.73e-11 |
|
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: 62.49 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGG----YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecidkahfqsrlkk 344
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 345 GLALVPEdrqgEGVVQMMSIQSNMTlsdFSLQgfrrawkwLNPHKEQASVKA--MIQQLAIkvsdpqLP------I---- 412
Cdd:cd03250 67 SIAYVSQ----EPWIQNGTIRENIL---FGKP--------FDEERYEKVIKAcaLEPDLEI------LPdgdlteIgekg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 413 TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGID--VGAKTdVYHLIGKMAQQGLAVMFSSSELdEVMALADRILVMADG 490
Cdd:cd03250 126 INLSGGQKQRISLARAVYSDADIYLLDDPLSAVDahVGRHI-FENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
.
gi 496059540 491 R 491
Cdd:cd03250 204 R 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
249-494 |
4.17e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 249 MVGDKKKHFDYQPAPkgetvlsvqgltalhPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQL 328
Cdd:PRK13643 1 MIKFEKVNYTYQPNS---------------PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 329 NGECIDKAHFQSRLKkglalvPEDRQGEGVVQMMSIQ--SNMTLSD--FSLQGFrrawkwlNPHKEQASVKAMIQQLAIK 404
Cdd:PRK13643 66 GDIVVSSTSKQKEIK------PVRKKVGVVFQFPESQlfEETVLKDvaFGPQNF-------GIPKEKAEKIAAEKLEMVG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 405 VSDP---QLPItSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALA 481
Cdd:PRK13643 133 LADEfweKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYA 211
|
250
....*....|...
gi 496059540 482 DRILVMADGRITA 494
Cdd:PRK13643 212 DYVYLLEKGHIIS 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-227 |
4.48e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 23 LSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKST----MMKMLAgvespSSGQIIMDGIPVTLNSTHQAEKL--GISI 96
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVrhRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELN--LFPNMNVMDNIFMANEFFQKgKINEKYQYALAKSLLErlELDVDPYT----PLEELGiGHQQLVEIARALSK 170
Cdd:PRK15134 367 VFQDPNssLNPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVME--EVGLDPETrhryPAEFSG-GQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLK-RRGVTIIYISHRLE---------------ELMEIGDYITIFR 227
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLFISHDLHvvralchqvivlrqgEVVEQGDCERVFA 515
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
285-506 |
4.68e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHfqsRLKKGLALVPEDRQGEGvvqmmsi 364
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTAR---SLSQQKGLIRQLRQHVG------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 qsnmtlsdFSLQGFRrawkwLNPH------------------KEQASVKAmiQQLAIKV-------SDPQlpitSLSGGN 419
Cdd:PRK11264 89 --------FVFQNFN-----LFPHrtvleniiegpvivkgepKEEATARA--RELLAKVglagketSYPR----RLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 420 QQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRIT------ 493
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVeqgpak 229
|
250
....*....|....*.
gi 496059540 494 ---ADvPRHAVTRETL 506
Cdd:PRK11264 230 alfAD-PQQPRTRQFL 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-230 |
5.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.21 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVY---PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLg 93
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 94 ISIIFQEL-NLFPNMNVMDNIF--MANEFFQKGKINEKYQYALAKSLLERLElDVDPytplEELGIGHQQLVEIARALSK 170
Cdd:PRK13650 83 IGMVFQNPdNQFVGATVEDDVAfgLENKGIPHEEMKERVNEALELVGMQDFK-EREP----ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELmEIGDYITIFRDGR 230
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
286-491 |
5.61e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 286 NDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ---SGSVQLNGECI----DKAHFQSRLKKgLALVPEDrqgegv 358
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpEKELNKLRAEQ-ISMIFQD------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 359 vQMMSIQSNMTLSDfSLQGFRRAWKWLNphKEQA---SVKaMIQqlAIKVSDPQLPIT----SLSGGNQQKVVLGKALMT 431
Cdd:PRK09473 106 -PMTSLNPYMRVGE-QLMEVLMLHKGMS--KAEAfeeSVR-MLD--AVKMPEARKRMKmyphEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 432 QPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGR 491
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
285-492 |
6.03e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.94 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKahfqsrlkkglaLVPEDRQgegvVQM--- 361
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD------------LPPKDRN----IAMvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 -------MSIQSNMTlsdFSL--QGFRRAwkwlnphkEQAS-VKAMIQQLAIkvsDPQL---PiTSLSGGNQQKVVLGKA 428
Cdd:COG3839 83 syalyphMTVYENIA---FPLklRKVPKA--------EIDRrVREAAELLGL---EDLLdrkP-KQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 429 LMTQPQVVFLDEPTRGIDvgaktdvYHLIGKM--------AQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:COG3839 148 LVREPKVFLLDEPLSNLD-------AKLRVEMraeikrlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-232 |
6.43e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.57 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVY----PGVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQII----------------- 75
Cdd:PRK13651 3 IKVKNIVKIFnkklPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 76 -MDGIPVTLNSTHQAEKLG-----ISIIFQ--ELNLFPNMNVMDNIFMANEFfqkgKINEKYQYALAKSLLERLELDVD- 146
Cdd:PRK13651 83 vLEKLVIQKTRFKKIKKIKeirrrVGVVFQfaEYQLFEQTIEKDIIFGPVSM----GVSKEEAKKRAAKYIELVGLDESy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 147 -PYTPLEeLGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITI 225
Cdd:PRK13651 159 lQRSPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*..
gi 496059540 226 FRDGRFI 232
Cdd:PRK13651 238 FKDGKII 244
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-211 |
6.57e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP-GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgISI 96
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-FSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IFQELNLFPNMnvmdnifMANEFFQKGKinekyqyALAKSLLERLELD-----VDPYTPLEELGIGHQQLVEIARALSKD 171
Cdd:PRK10522 402 VFTDFHLFDQL-------LGPEGKPANP-------ALVEKWLERLKMAhklelEDGRISNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496059540 172 TRVLIMDEptSALSQSEV--KVLFNV-IEQLKRRGVTIIYISH 211
Cdd:PRK10522 468 RDILLLDE--WAADQDPHfrREFYQVlLPLLQEMGKTIFAISH 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-211 |
6.73e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 61.61 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEklGISII 97
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE--NILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 98 FQELNLFPNMNVMDNIFMANEFFQKGKINekyqyalAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIM 177
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 496059540 178 DEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISH 211
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
48-235 |
7.68e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 64.46 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMDGIP---VTLNSTHQAeklgISIIFQELNLFpNMNVMDNIFMANEFFQKGK 124
Cdd:COG5265 389 IVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLRAA----IGIVPQDTVLF-NDTIAYNIAYGRPDASEEE 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 125 INEKYQYALAKSLLERLEldvDPY-TPLEELGI----GHQQLVEIARALSKDTRVLIMDEPTSAL-SQSEVKVLfnviEQ 198
Cdd:COG5265 464 VEAAARAAQIHDFIESLP---DGYdTRVGERGLklsgGEKQRVAIARTLLKNPPILIFDEATSALdSRTERAIQ----AA 536
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059540 199 LKR--RGVTIIYISHRLEELMEiGDYITIFRDGRfISER 235
Cdd:COG5265 537 LREvaRGRTTLVIAHRLSTIVD-ADEILVLEAGR-IVER 573
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-234 |
8.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.80 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKlGISIIFQEL-NLFPNMN 108
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR-KIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 109 VMDNIFMANEffQKGKINEKYQYALAKSLLERLELDVDPYTPlEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSE 188
Cdd:PRK13642 99 VEDDVAFGME--NQGIPREEMIKRVDEALLAVNMLDFKTREP-ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496059540 189 VKVLFNVIEQLKRR-GVTIIYISHRLEELMEiGDYITIFRDGRFISE 234
Cdd:PRK13642 176 RQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
48-213 |
8.76e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVeSPSSGQIIMDGIPVTLNSTH-----------QAEKLGISIIFQELNLfpnmnvmdnifma 116
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelarhraylsqQQSPPFAMPVFQYLAL------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 117 nefFQKGKINEKYQYALAKSLLERLELDvDPYT-PLEELGIGHQQLVEIARAL-------SKDTRVLIMDEPTSALSQSE 188
Cdd:COG4138 93 ---HQPAGASSEAVEQLLAQLAEALGLE-DKLSrPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|....*
gi 496059540 189 VKVLFNVIEQLKRRGVTIIYISHRL 213
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDL 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
285-501 |
1.04e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfqsRLKKGLALVPEDRQgegvVQMMSI 364
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV----RDKDGQLKVADKNQ----LRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLQGFRRAW--------KWLNPHKEQASVKAM--IQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQ 434
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLenvmeapiQVLGLSKQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 435 VVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVPRHAV 501
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
285-498 |
1.28e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.10 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI-----DKAHFQSRLKKGLAL-VPEDRQGEGV 358
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKRIGMVFqFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 359 VQMMSIqsnmtlsdFSLQGFRrawkwLNPHKEQASVKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:PRK13646 103 VEREII--------FGPKNFK-----MNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRITADV-PR 498
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTsPK 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-236 |
1.42e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 1 MQQQDIVTPHSVESEViiethdLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDG-- 78
Cdd:PRK10261 314 LQVRNLVTRFPLRSGL------LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqr 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 79 IPVTLNSTHQAEKLGISIIFQE--LNLFPNMNVMDNIFmaNEFFQKGKINEKYQYALAKSLLERLELDVD-PYTPLEELG 155
Cdd:PRK10261 388 IDTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIM--EPLRVHGLLPGKAAAARVAWLLERVGLLPEhAWRYPHEFS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 156 IGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISE 234
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
..
gi 496059540 235 RP 236
Cdd:PRK10261 546 GP 547
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-192 |
1.52e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.66 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 40 VYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHqaeklgISIIFQelnlfpnMNVMDnifmanef 119
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY------IKADYE-------GTVRD-------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 120 FQKGKINEKYQYALAKS-LLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPtSALSQSEVKVL 192
Cdd:cd03237 81 LLSSITKDFYTHPYFKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP-SAYLDVEQRLM 153
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
285-497 |
1.62e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.26 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKkglalvpedRQGEGVV-QMMS 363
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI---------RQEAGMVfQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 IQSNMTLSDFSLQGFRRAWKwlnPHKEQASVKAMiqQLAIKVSDPQ----LPiTSLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:PRK09493 88 LFPHLTALENVMFGPLRVRG---ASKEEAEKQAR--ELLAKVGLAErahhYP-SELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 440 EPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITADVP 497
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-492 |
1.72e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.60 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI--DKAHFQS---RLKKGLALVpedRQGEGVV 359
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfGKDIFQIdaiKLRKEVGMV---FQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 QMMSIQSNMTLSdfslqgfrrawkwLNPH--KEQASVKAMIQQLAIKV-------SDPQLPITSLSGGNQQKVVLGKALM 430
Cdd:PRK14246 103 PHLSIYDNIAYP-------------LKSHgiKEKREIKKIVEECLRKVglwkevyDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 431 TQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQgLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
260-491 |
2.06e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 260 QPAPKGETVLS----VQGLTALHpSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGEciDK 335
Cdd:PRK11607 7 RPQAKTRKALTplleIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 336 AH-----------FQSrlkkgLALVPEdrqgegvvqmMSIQSNMTlsdFSLQGFRRAWKWLNPHKEQASVKAMIQQLAIK 404
Cdd:PRK11607 84 SHvppyqrpinmmFQS-----YALFPH----------MTVEQNIA---FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 405 vsDPQlpitSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYH-LIGKMAQQGLAVMFSSSELDEVMALADR 483
Cdd:PRK11607 146 --KPH----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLeVVDILERVGVTCVMVTHDQEEAMTMAGR 219
|
....*...
gi 496059540 484 ILVMADGR 491
Cdd:PRK11607 220 IAIMNRGK 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
415-508 |
2.25e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRIT 493
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
90 100
....*....|....*....|...
gi 496059540 494 A--------DVPRHAVTRETLIA 508
Cdd:PRK15134 237 EqnraatlfSAPTHPYTQKLLNS 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
269-446 |
2.28e-10 |
|
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: 63.39 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYK-LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQsGSVQLNGECIDKAHFQsRLKKGLA 347
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQ-TWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 LVPEDrqgegvVQMMSIQSNMTLSDFSLQGFRRAWKWlnphKEQASVKAMIQQLAIKVsDPQLPITS--LSGGNQQKVVL 425
Cdd:TIGR01271 1296 VIPQK------VFIFSGTFRKNLDPYEQWSDEEIWKV----AEEVGLKSVIEQFPDKL-DFVLVDGGyvLSNGHKQLMCL 1364
|
170 180
....*....|....*....|.
gi 496059540 426 GKALMTQPQVVFLDEPTRGID 446
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLD 1385
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-229 |
2.60e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 60.42 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 28 PGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNS---THQAEKLGISIIFQELNLF 104
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeaTRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 105 pNMNVMDNIFMANEFfqkgkiNEKYQYALAKSLLERLELDVDPY---TPLEELGI----GHQQLVEIARALSKDTRVLIM 177
Cdd:cd03290 92 -NATVEENITFGSPF------NKQRYKAVTDACSLQPDIDLLPFgdqTEIGERGInlsgGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 178 DEPTSALS--QSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEiGDYITIFRDG 229
Cdd:cd03290 165 DDPFSALDihLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
30-239 |
2.71e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESP----SSGQIIMDGIPVTLNSTHQAEKL---GISIIFQELN 102
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLvghNVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 103 --LFPNMNVMDNIFMA-NEFFQKGKINEKYQYAL--AKSLLERLEL----DVD---PYtpleELGIGHQQLVEIARALSK 170
Cdd:PRK15093 100 scLDPSERVGRQLMQNiPGWTYKGRWWQRFGWRKrrAIELLHRVGIkdhkDAMrsfPY----ELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 171 DTRVLIMDEPTSALSQSEVKVLFNVIEQL-KRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
50-211 |
2.73e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.89 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 50 GENGAGKSTMMKMLAGVESPSSGQIIMDGIpvtlnSTHQAEKLGISIIFQELNLFPNMNVMDNIFMANEFFQKGkinEKY 129
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNC-----NINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA---ETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 130 QYALAKSLLERLeLDVDPYTpleeLGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYI 209
Cdd:PRK13541 105 YAAIHYFKLHDL-LDEKCYS----LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLS 179
|
..
gi 496059540 210 SH 211
Cdd:PRK13541 180 SH 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-211 |
4.20e-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: 59.43 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 29 GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEklGISIIFQELNLFPNMN 108
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 109 VMDNIfmanEFFQKGKINEKYQYALAKSLLERLEldvdpYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSE 188
Cdd:cd03231 90 VLENL----RFWHADHSDEQVEEALARVGLNGFE-----DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 496059540 189 VKVLFNVIEQLKRRGVTIIYISH 211
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
281-493 |
4.21e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.89 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 281 GGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecidkaHFQSRLKKglALVPEDRQGEGVV- 359
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG------HDITRLKN--REVPFLRRQIGMIf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 ----QMM--SIQSNMTL----SDFSLQGFRRawkwlnphkeqaSVKAMIQQLAIKVSDPQLPItSLSGGNQQKVVLGKAL 429
Cdd:PRK10908 86 qdhhLLMdrTVYDNVAIpliiAGASGDDIRR------------RVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 430 MTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRIT 493
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
269-514 |
4.91e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.05 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYK---LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfqsrlkKG 345
Cdd:PRK10535 5 LELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-------DA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 LALVPEDRQGEGVV-QMMSIQSNMTlsdfSLQGFR--RAWKWLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQK 422
Cdd:PRK10535 78 DALAQLRREHFGFIfQRYHLLSHLT----AAQNVEvpAVYAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 423 VVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSElDEVMALADRILVMADGRITADVPRHAVT 502
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQEKV 231
|
250
....*....|..
gi 496059540 503 RETLIAASTPQD 514
Cdd:PRK10535 232 NVAGGTEPVVNT 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-232 |
5.53e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 25 RVYPGVV-ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsthqaeKLGISIIFQELNL 103
Cdd:PLN03232 1243 RYRPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 104 FPNMNVMdniFMANEFFQKGKINEKYQYALAKSLlERLEL-DVDPYTPL----------EELGIGHQQLVEIARALSKDT 172
Cdd:PLN03232 1315 IPQSPVL---FSGTVRFNIDPFSEHNDADLWEAL-ERAHIkDVIDRNPFgldaevseggENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 173 RVLIMDEPTSALSQSEVKVLFNVIEQlKRRGVTIIYISHRLEELMEIgDYITIFRDGRFI 232
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVL 1448
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
285-494 |
5.95e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.72 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHF-QSRLKKGLALVPEDrqgegvVQM-- 361
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG--VDIRDLtLESLRRQIGVVPQD------TFLfs 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTLS--DFSLQGFRRAwkwlnphKEQASVKAMIQQLaikvsdPQ---LPI----TSLSGGNQQKVVLGKALMTQ 432
Cdd:COG1132 428 GTIRENIRYGrpDATDEEVEEA-------AKAAQAHEFIEAL------PDgydTVVgergVNLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 433 PQVVFLDEPTRGIDvgAKTDvyHLIgkmaQQGlavmfssseLDEVMA---------------LADRILVMADGRITA 494
Cdd:COG1132 495 PPILILDEATSALD--TETE--ALI----QEA---------LERLMKgrttiviahrlstirNADRILVLDDGRIVE 554
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
48-213 |
6.23e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVeSPSSGQIIMDGIPVtlnSTHQAEKLGI--SIIFQELNLFPNMNVmdniFMANEFFQKGKI 125
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPL---EAWSAAELARhrAYLSQQQTPPFAMPV----FQYLTLHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 126 NEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIA-------RALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQ 198
Cdd:PRK03695 99 RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSE 178
|
170
....*....|....*
gi 496059540 199 LKRRGVTIIYISHRL 213
Cdd:PRK03695 179 LCQQGIAVVMSSHDL 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
48-211 |
6.45e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMDG----------IPVTLNST----------HQAEKLG--------ISIIFQ 99
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdPPRNVEGTvydfvaegieEQAEYLKryhdishlVETDPS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 100 ELNLFPNMNVMDNIFMANEFFQKGKINEkyqyalaksLLERLELDVDpyTPLEELGIGHQQLVEIARALSKDTRVLIMDE 179
Cdd:PRK11147 114 EKNLNELAKLQEQLDHHNLWQLENRINE---------VLAQLGLDPD--AALSSLSGGWLRKAALGRALVSNPDVLLLDE 182
|
170 180 190
....*....|....*....|....*....|...
gi 496059540 180 PTSALSQSEVKVLfnviEQ-LKRRGVTIIYISH 211
Cdd:PRK11147 183 PTNHLDIETIEWL----EGfLKTFQGSIIFISH 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-211 |
1.10e-09 |
|
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: 60.72 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMdGIPVTLNSTHQAEKlgi 94
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 siifqelNLFPNMNVMDNIFMANEFFQKGK--INekyqyalAKSLLERLELD-VDPYTPLEELGIGHQQLVEIARALSKD 171
Cdd:TIGR03719 396 -------ALDPNKTVWEEISGGLDIIKLGKreIP-------SRAYVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059540 172 TRVLIMDEPTSALSQSEVKVLFNVIEQLKrrGVTIIyISH 211
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVV-ISH 498
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
285-509 |
1.17e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ--------SGSVQLNGE---CIDKahfqSRLKKGLALVPEdr 353
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEplaAIDA----PRLARLRAVLPQ-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 354 QGEGVVQMmSIQSNMTLSDFSLQgfRRAWKWLNPHKEQASvkamiQQLAIKVSDPQL--PITSLSGGNQQKVVLGKAL-- 429
Cdd:PRK13547 91 AAQPAFAF-SAREIVLLGRYPHA--RRAGALTHRDGEIAW-----QALALAGATALVgrDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 430 -------MTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITADVPRHAV 501
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
....*...
gi 496059540 502 TRETLIAA 509
Cdd:PRK13547 243 LTPAHIAR 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
266-446 |
2.22e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.87 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTALHPSGGYKLN---DVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRl 342
Cdd:PRK10584 4 ENIVEVHHLKKSVGQGEHELSiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 kkglALVPEDRQGEGVVQMMSIQSNMTLSDFSLQGFRRAwkwLNPHKEQASVKAMIQQLAIKVSDPQLPiTSLSGGNQQK 422
Cdd:PRK10584 83 ----AKLRAKHVGFVFQSFMLIPTLNALENVELPALLRG---ESSRQSRNGAKALLEQLGLGKRLDHLP-AQLSGGEQQR 154
|
170 180
....*....|....*....|....
gi 496059540 423 VVLGKALMTQPQVVFLDEPTRGID 446
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLD 178
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
32-239 |
2.85e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAG-VESP---SSGQIIMDGIPVTLNSTHQAEKL---GISIIFQE--LN 102
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYPgrvMAEKLEFNGQDLQRISEKERRNLvgaEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 103 LFPNMNVMDNIFMANEFFQKGkiNEKYQYALAKSLLERL-------ELDVDPYtpleELGIGHQQLVEIARALSKDTRVL 175
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVgipdpasRLDVYPH----QLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 176 IMDEPTSALsqsEVKVLFNVIEQL----KRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:PRK11022 176 IADEPTTAL---DVTIQAQIIELLlelqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
269-457 |
3.22e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.44 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLngecidkahfqsrlkkglal 348
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-------------------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 349 vPEDRQgegvVQMMSIQSNM---TL----------SDFSLQGFRRAwkwLnphkEQASVKAMIQQLAIKVSDPQLpitsL 415
Cdd:COG4178 423 -PAGAR----VLFLPQRPYLplgTLreallypataEAFSDAELREA---L----EAVGLGHLAERLDEEADWDQV----L 486
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059540 416 SGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLI 457
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL 528
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
382-487 |
3.80e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.38 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 382 WKWLNPHKEQAsvKAMIQQLAIKvsDPQLPITS----LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLI 457
Cdd:COG4170 126 WQRFKWRKKRA--IELLHRVGIK--DHKDIMNSypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLL 201
|
90 100 110
....*....|....*....|....*....|.
gi 496059540 458 GKMAQ-QGLAVMFSSSELDEVMALADRILVM 487
Cdd:COG4170 202 ARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
285-495 |
3.96e-09 |
|
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: 56.17 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqSRLKKGLalvpedRQGEGVVQmmsi 364
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV------SDLEKAL------SSLISVLN---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSnmtlsdfslqgfrrawkwlnPHKEQASVKamiQQLAIKvsdpqlpitsLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03247 82 QR--------------------PYLFDTTLR---NNLGRR----------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 445 IDvgAKTDvyhligkmaQQGLAVMFSSSELDEV---------MALADRILVMADGRITAD 495
Cdd:cd03247 129 LD--PITE---------RQLLSLIFEVLKDKTLiwithhltgIEHMDKILFLENGKIIMQ 177
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
270-506 |
3.98e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 270 SVQGLTALHPsggyklndVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKgLALV 349
Cdd:PRK10575 20 RVPGRTLLHP--------LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 350 PED-RQGEGvvqmMSIQSNMTLSDFSLQG----FRRAWKwlnPHKEQASVKAMIQQLAIKVSDpqlpitSLSGGNQQKVV 424
Cdd:PRK10575 91 PQQlPAAEG----MTVRELVAIGRYPWHGalgrFGAADR---EKVEEAISLVGLKPLAHRLVD------SLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 425 LGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITAD-VPRHAVT 502
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQgTPAELMR 237
|
....
gi 496059540 503 RETL 506
Cdd:PRK10575 238 GETL 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
285-507 |
4.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVG-LMPCQSGSVQLNGECI---DKAHFQSRLKKGLALVPEDRQGEGVvq 360
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNSKITVDGItltAKTVWDIREKVGIVFQNPDNQFVGA-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 mmsiqsnmTLSD---FSLQGfrRAWKWLNPHKEQASVKAMIQQLAIKVSDPQlpitSLSGGNQQKVVLGKALMTQPQVVF 437
Cdd:PRK13640 101 --------TVGDdvaFGLEN--RAVPRPEMIKIVRDVLADVGMLDYIDSEPA----NLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 438 LDEPTRGIDVGAKTDVYHLIGK-MAQQGLAVMFSSSELDEVmALADRILVMADGRITA-DVPRHAVTRETLI 507
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAqGSPVEIFSKVEML 237
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-230 |
4.19e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipvtlnsthqaeklGISIIFQELNLFPNMNVMD 111
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------------EVSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 112 NIfmanEF------FQKGKINekyqyALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALS 185
Cdd:PRK13546 105 NI----EFkmlcmgFKRKEIK-----AMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059540 186 QSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
416-495 |
5.15e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 416 SGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
285-492 |
5.57e-09 |
|
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: 56.46 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSrLKKGLALVPEDR---QGegvvqm 361
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS-LRSMIGVVLQDTflfSG------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 mSIQSNMTLSdfslqgfrrawkwlNPHKEQASVKAMIQQLAIKVSDPQLPI----------TSLSGGNQQKVVLGKALMT 431
Cdd:cd03254 92 -TIMENIRLG--------------RPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgengGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496059540 432 QPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS---SSELDevmalADRILVMADGRI 492
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAhrlSTIKN-----ADKILVLDDGKI 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
285-505 |
6.89e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHFQ-SRLKKGLALVPEDRQgegvvqMMS 363
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDVAKFGlTDLRRVLSIIPQSPV------LFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 IQSNMTLSDFSLQGFRRAWKWLnphkEQASVKAMIQQ----LAIKVSDPQlpiTSLSGGNQQKVVLGKALMTQPQVVFLD 439
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDADLWEAL----ERAHIKDVIDRnpfgLDAEVSEGG---ENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 440 EPTRGIDVgaKTDVyhLIGKMAQQ---GLAVMFSSSELDEVMAlADRILVMADGRITA-DVPRHAVTRET 505
Cdd:PLN03232 1397 EATASVDV--RTDS--LIQRTIREefkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEyDSPQELLSRDT 1461
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-230 |
6.99e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 44 KVNVlIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlnsthqaeKLGISIIFQELNLFPNMNVMdniFMANEFFQKG 123
Cdd:PLN03130 1267 KVGI-VGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--------KFGLMDLRKVLGIIPQAPVL---FSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 124 KINEKYQYALAKSlLERLEL-DVDPYTPL----------EELGIGHQQLVEIARALSKDTRVLIMDEPTS-------ALS 185
Cdd:PLN03130 1335 PFNEHNDADLWES-LERAHLkDVIRRNSLgldaevseagENFSVGQRQLLSLARALLRRSKILVLDEATAavdvrtdALI 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059540 186 QSEVKVLFnvieqlkrRGVTIIYISHRLEELMEIgDYITIFRDGR 230
Cdd:PLN03130 1414 QKTIREEF--------KSCTMLIIAHRLNTIIDC-DRILVLDAGR 1449
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
269-492 |
7.13e-09 |
|
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: 56.79 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYK-LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQsGSVQLNGECIDKAHFQsRLKKGLA 347
Cdd:cd03289 3 MTVKDLTAKYTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQ-KWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 348 LVPEDrqgegvVQMMSIQSNMTLSDFSLQGFRRAWKWlnphKEQASVKAMIQQLAIKVsDPQLPITS--LSGGNQQKVVL 425
Cdd:cd03289 81 VIPQK------VFIFSGTFRKNLDPYGKWSDEEIWKV----AEEVGLKSVIEQFPGQL-DFVLVDGGcvLSHGHKQLMCL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 426 GKALMTQPQVVFLDEPTRGIDvgakTDVYHLIGKMAQQGLA---VMFSSSELdEVMALADRILVMADGRI 492
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLD----PITYQVIRKTLKQAFAdctVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-447 |
8.76e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 15 EVIIETHDLSRVYPG-VVALDSVNYRVYRN-KVNVLiGENGAGKSTMMKMLAGVESPSSGQ-IIMDGIpvtlnsthqaeK 91
Cdd:PRK11819 4 QYIYTMNRVSKVVPPkKQILKDISLSFFPGaKIGVL-GLNGAGKSTLLRIMAGVDKEFEGEaRPAPGI-----------K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 92 LGIsiIFQELNLFPNMNVMDNIFMA--------NEF-------------FQK-----GKINEKYQYALAKSLLERLELDV 145
Cdd:PRK11819 72 VGY--LPQEPQLDPEKTVRENVEEGvaevkaalDRFneiyaayaepdadFDAlaaeqGELQEIIDAADAWDLDSQLEIAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 146 D------PYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLfnviEQ-LKRRGVTIIYISH-Rleelm 217
Cdd:PRK11819 150 DalrcppWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL----EQfLHDYPGTVVAVTHdR----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 218 eigdYitiFRD-----------GRFI-------------SERPVNDAS------------IPWI---------------- 245
Cdd:PRK11819 221 ----Y---FLDnvagwileldrGRGIpwegnysswleqkAKRLAQEEKqeaarqkalkreLEWVrqspkarqakskarla 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 246 -IEQMVG-DKKKHFDYQ-----PAPK-GETVLSVQGLTAlhpSGGYKL--NDVTFSLSKGEVIGIYGLLGAGRTELFKGL 315
Cdd:PRK11819 294 rYEELLSeEYQKRNETNeifipPGPRlGDKVIEAENLSK---SFGDRLliDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 316 VGLMPCQSGSVQLnGECIDKAHF-QSRlkkgLALVPEDRqgegVVQMMSI-QSNMTLSDFslqgfrrawkwlnphkEQAS 393
Cdd:PRK11819 371 TGQEQPDSGTIKI-GETVKLAYVdQSR----DALDPNKT----VWEEISGgLDIIKVGNR----------------EIPS 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 394 vKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDV 447
Cdd:PRK11819 426 -RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
285-492 |
9.54e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSR----LKKGLALVPEdrqgegvvq 360
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdicmVFQSYALFPH--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 mMSIQSNMtlsdfslqGFrrAWKWLNPHKEQasVKAMIQQlAIKVSD----PQLPITSLSGGNQQKVVLGKALMTQPQVV 436
Cdd:PRK11432 93 -MSLGENV--------GY--GLKMLGVPKEE--RKQRVKE-ALELVDlagfEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 437 FLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-212 |
1.07e-08 |
|
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: 55.25 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAG-VESPS-SGQIIMDGIPVTLNSthqaekLGISIIF--QELNLFPNMN 108
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGvSGEVLINGRPLDKRS------FRKIIGYvpQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 109 VMDNIFMAneffqkgkinekyqyalAKsllerleldvdpytpLEELGIGHQQLVEIARALSKDTRVLIMDEPTSAL-SQS 187
Cdd:cd03213 99 VRETLMFA-----------------AK---------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLdSSS 146
|
170 180
....*....|....*....|....*
gi 496059540 188 EVKVLFnVIEQLKRRGVTIIYISHR 212
Cdd:cd03213 147 ALQVMS-LLRRLADTGRTIICSIHQ 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
47-212 |
1.49e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 47 VLI-GENGAGKSTMMKMLAGVESPSSGQIIMdgiPVtlnsthqaeklGISIIF--Q----------ELNLFPNmnvmdni 113
Cdd:COG4178 392 LLItGPSGSGKSTLLRAIAGLWPYGSGRIAR---PA-----------GARVLFlpQrpylplgtlrEALLYPA------- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 114 fmANEFFQkgkiNEKYQYALAK----SLLERLElDVDPYTplEELGIGHQQLVEIARALSKDTRVLIMDEPTSALS-QSE 188
Cdd:COG4178 451 --TAEAFS----DAELREALEAvglgHLAERLD-EEADWD--QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDeENE 521
|
170 180
....*....|....*....|....*.
gi 496059540 189 VKVLfnviEQLKRR--GVTIIYISHR 212
Cdd:COG4178 522 AALY----QLLREElpGTTVISVGHR 543
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
31-251 |
1.59e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 31 VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGvESPSS---------GQIIMDGIPVTLNSTHQAEKLGISIIFQEL 101
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 102 NLFPnmnvmdniFMANEFFQKGKinekYQYA------------LAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALS 169
Cdd:PRK13547 94 PAFA--------FSAREIVLLGR----YPHArragalthrdgeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 170 K---------DTRVLIMDEPTSALSQSEVKVLFNVIEQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250
....*....|..
gi 496059540 240 ASIPWIIEQMVG 251
Cdd:PRK13547 242 VLTPAHIARCYG 253
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
287-471 |
2.12e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 287 DVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfqsrlkkglalvpeDRQGEGVVQMM---- 362
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI------------------RRQRDEYHQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 ---SIQSNMTlsdfslqgfrrAW---KWLNPHKEQASVKAMIQQLAiKVS-----DpqLPITSLSGGNQQKVVLGKALMT 431
Cdd:PRK13538 81 hqpGIKTELT-----------ALenlRFYQRLHGPGDDEALWEALA-QVGlagfeD--VPVRQLSAGQQRRVALARLWLT 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059540 432 QPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSS 471
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTT 186
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
280-497 |
2.67e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.10 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 280 SGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPC-----QSGSVQLNGECIdkahFQSRLkkglalVPEDRQ 354
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSI----FNYRD------VLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 355 GEGVVQMMSIQSNMTLSDFSLQGFRrAWKwLNPHKE-QASVKAMIQQLAI------KVSDPQLpitSLSGGNQQKVVLGK 427
Cdd:PRK14271 102 RVGMLFQRPNPFPMSIMDNVLAGVR-AHK-LVPRKEfRGVAQARLTEVGLwdavkdRLSDSPF---RLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 428 ALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQgLAVMFSSSELDEVMALADRILVMADGRITADVP 497
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
285-492 |
3.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.01 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI----DKAHFQSRLKKGLALV---PEdrqgeg 357
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKKIKEVKRLRKEIGLVfqfPE------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 358 vVQMM--SIQSNMTLSDFSLqgfrrawkwlNPHKEQASVKamIQQLAIKVSDPQLPIT----SLSGGNQQKVVLGKALMT 431
Cdd:PRK13645 101 -YQLFqeTIEKDIAFGPVNL----------GENKQEAYKK--VPELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 432 QPQVVFLDEPTRGIDVGAKTDVYHLIGKM-AQQGLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
279-493 |
3.21e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.14 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 279 PSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECI-----DKAHFQSRLKKGLAL-VPED 352
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIKQIRKKVGLVFqFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 353 RQGEGVVqmmsiqsnmtLSD--FSLQGFrrawkwlNPHKEQASVKAMIQQLAIKVSDP---QLPItSLSGGNQQKVVLGK 427
Cdd:PRK13649 97 QLFEETV----------LKDvaFGPQNF-------GVSQEEAEALAREKLALVGISESlfeKNPF-ELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 428 ALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRIT 493
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
285-447 |
3.51e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdkahfQSRLKKGlalVPEDRQG-------EG 357
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI-----VARLQQD---PPRNVEGtvydfvaEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 358 V--------------VQMMSIQSNMTLSDFS-LQG---FRRAWKWlnphkeQASVKAMIQQLAIkvsDPQLPITSLSGGN 419
Cdd:PRK11147 91 IeeqaeylkryhdisHLVETDPSEKNLNELAkLQEqldHHNLWQL------ENRINEVLAQLGL---DPDAALSSLSGGW 161
|
170 180
....*....|....*....|....*...
gi 496059540 420 QQKVVLGKALMTQPQVVFLDEPTRGIDV 447
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
30-230 |
3.77e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 30 VVALDSVNYRVYRNKVNVLIGENGAGKS----TMMKMLAGvESPSSGQIIMDGIPVtLN-STHQAEKL---GISIIFQE- 100
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREI-LNlPEKELNKLraeQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 101 -LNLFPNMNVMDNIfMANEFFQKGkINEKYQYALAKSLLE-------RLELDVDPYtpleELGIGHQQLVEIARALSKDT 172
Cdd:PRK09473 107 mTSLNPYMRVGEQL-MEVLMLHKG-MSKAEAFEESVRMLDavkmpeaRKRMKMYPH----EFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 173 RVLIMDEPTSALS---QSEVKVLFNvieQLKRR-GVTIIYISHRLEELMEIGDYITIFRDGR 230
Cdd:PRK09473 181 KLLIADEPTTALDvtvQAQIMTLLN---ELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
280-490 |
3.91e-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: 53.87 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 280 SGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKGLALVPEDRQGEGVV 359
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 QMmSIQSNMTL-SDFSLQGFrrawkwlnphkeqasvKAMIQQLAIKVSDPQLPI----------TSLSGGNQQKVVLGKA 428
Cdd:cd03290 92 NA-TVEENITFgSPFNKQRY----------------KAVTDACSLQPDIDLLPFgdqteigergINLSGGQRQRICVARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 429 LMTQPQVVFLDEPTRGIDVgaktdvyHLIGKMAQQGLAVMFSSSELDEVMAL--------ADRILVMADG 490
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDI-------HLSDHLMQEGILKFLQDDKRTLVLVThklqylphADWIIAMKDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
285-473 |
4.28e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAhfQSRLKKGLALVPEdRQGegvvqmmsI 364
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD--LCTYQKQLCFVGH-RSG--------I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLqgfrrawkwLNPHKEQASVKamIQQLAIKVSDPQL---PITSLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:PRK13540 86 NPYLTLRENCL---------YDIHFSPGAVG--ITELCRLFSLEHLidyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 496059540 442 TRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSE 473
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-212 |
4.71e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLN-STHQAEklgISIIFQELNLFPNMNVMD 111
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlCTYQKQ---LCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 112 NIFMANEFFQKG-KINEKYQyalakslLERLELDVDpyTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVK 190
Cdd:PRK13540 94 NCLYDIHFSPGAvGITELCR-------LFSLEHLID--YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 496059540 191 VLFNVIEQLKRRGVTIIYISHR 212
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
285-499 |
4.85e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.64 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLnGECIDKAHFQSRLKKGLalvpedRQGEGVV-QMMS 363
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLKPL------RKKVGIVfQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 IQ--SNMTLSD--FSLQGFrrawkwlNPHKEQASVKA--MIQQLAIkvsDPQLPITS---LSGGNQQKVVLGKALMTQPQ 434
Cdd:PRK13634 96 HQlfEETVEKDicFGPMNF-------GVSEEDAKQKAreMIELVGL---PEELLARSpfeLSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 435 VVFLDEPTRGIDVGAKTDVYHLIGKMAQ-QGLAVMFSSSELDEVMALADRILVMADGRITAD-VPRH 499
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQgTPRE 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
283-513 |
9.66e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.55 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 283 YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNG--ECIDKAHFQSRLKKGLALVPEDRQgegvvq 360
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLWDIRNKAGMVFQNPDNQ------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 361 mmsIQSNMTLSDFslqgfrrAWKWLNPHKEQASVKAMIQQLAIKVS-------DPQLpitsLSGGNQQKVVLGKALMTQP 433
Cdd:PRK13633 98 ---IVATIVEEDV-------AFGPENLGIPPEEIRERVDESLKKVGmyeyrrhAPHL----LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 434 QVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVmALADRILVMADGRITAD-VPRHA---VTRETLIA 508
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEgTPKEIfkeVEMMKKIG 242
|
....*
gi 496059540 509 ASTPQ 513
Cdd:PRK13633 243 LDVPQ 247
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-486 |
1.07e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 42 RNKVNVLIGENGAGKSTMMKMLAG--------VESPSSGQIIMDGIPVTLNSTH----QAEKLGISIIFQELNLFPNM-- 107
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKRFRGTELQNYfkklYNGEIKVVHKPQYVDLIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 108 -NVMDNIFMANEffqKGKINEkyqyalaksLLERLELD--VDpyTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSAL 184
Cdd:PRK13409 178 gKVRELLKKVDE---RGKLDE---------VVERLGLEniLD--RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 185 sqsEVKVLFNVIEQLKR--RGVTIIYISHRLEELMEIGDYITI-----------------------FRDGrFISErpvnd 239
Cdd:PRK13409 244 ---DIRQRLNVARLIRElaEGKYVLVVEHDLAVLDYLADNVHIaygepgaygvvskpkgvrvgineYLKG-YLPE----- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 240 asipwiiEQM-VGDKKKHFDYQP---APKGETVLSVQGLTalhpsggYKLNDvtFSLS-------KGEVIGIYGLLGAGR 308
Cdd:PRK13409 315 -------ENMrIRPEPIEFEERPprdESERETLVEYPDLT-------KKLGD--FSLEveggeiyEGEVIGIVGPNGIGK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 309 TELFKGLVGLMPCQSGSVQLNgecidkahfqsrLKkgLALVPedrqgegvvQMMSIQSNMTLSDFsLQGFRRAW--KWLN 386
Cdd:PRK13409 379 TTFAKLLAGVLKPDEGEVDPE------------LK--ISYKP---------QYIKPDYDGTVEDL-LRSITDDLgsSYYK 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 387 PHkeqasvkaMIQQLAIkvsDPQL--PITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQG 464
Cdd:PRK13409 435 SE--------IIKPLQL---ERLLdkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
490 500
....*....|....*....|....
gi 496059540 465 LAVMFsSSELDEVMA--LADRILV 486
Cdd:PRK13409 504 EATAL-VVDHDIYMIdyISDRLMV 526
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-73 |
1.08e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 1.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 9 PHSVESEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQ 73
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE 322
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
285-493 |
1.22e-07 |
|
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: 52.26 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ---SGSVQLNGecIDKAHFQSRLKKGLALVPEDRqgegvVQM 361
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKYPGEIIYVSEED-----VHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTLsDFSLQgfrrawkwLNPHkeqASVKAmiqqlaikvsdpqlpitsLSGGNQQKVVLGKALMTQPQVVFLDEP 441
Cdd:cd03233 96 PTLTVRETL-DFALR--------CKGN---EFVRG------------------ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 442 TRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSEL-DEVMALADRILVMADGRIT 493
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVlKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQI 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-75 |
1.73e-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: 50.52 E-value: 1.73e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 18 IETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQII 75
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT 58
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-508 |
1.75e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.35 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQS-----GSVQLNGECIDKAHFQ-SRLKKGLALV-PE------ 351
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlNRLRRQVSMVhPKpnlfpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 352 ---DRQGEGVvQMMSIQSNMTLSDFSLQGFRRAWKWlnphkeqASVKAMIQQLAIKvsdpqlpitsLSGGNQQKVVLGKA 428
Cdd:PRK14258 103 svyDNVAYGV-KIVGWRPKLEIDDIVESALKDADLW-------DEIKHKIHKSALD----------LSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 429 LMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMA-QQGLAVMFSSSELDEVMALAD----------RILVMADGRITADV- 496
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDftaffkgnenRIGQLVEFGLTKKIf 244
|
250
....*....|....
gi 496059540 497 --PRHAVTRETLIA 508
Cdd:PRK14258 245 nsPHDSRTREYVLS 258
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-229 |
1.85e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 52.22 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYPGVV--ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgIS 95
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR-LS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQE---------LNLFPNMNVMDNifmaneffqkgKINEKYQYALAKSLLERLE--LDVDPYTPLEELGIGHQQLVEI 164
Cdd:cd03288 99 IILQDpilfsgsirFNLDPECKCTDD-----------RLWEALEIAQLKNMVKSLPggLDAVVTEGGENFSVGQRQLFCL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 165 ARALSKDTRVLIMDEPTSALSQSEVKVLFNVI-EQLKRRgvTIIYISHRLEELMEiGDYITIFRDG 229
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-504 |
2.01e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 17 IIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTlNSTHQaEKLGISI 96
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-DARHR-RAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 97 IF--QEL--NLFPNMNVMDNI-FMANEFFQKG-----KINEkyqyalaksLLERLELDVDPYTPLEELGIGHQQLVEIAR 166
Cdd:NF033858 79 AYmpQGLgkNLYPTLSVFENLdFFGRLFGQDAaerrrRIDE---------LLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 167 ALSKDTRVLIMDEPTSA---LSQSEvkvlF-NVIEQLKRR--GVTII----YI--------------------------- 209
Cdd:NF033858 150 ALIHDPDLLILDEPTTGvdpLSRRQ----FwELIDRIRAErpGMSVLvataYMeeaerfdwlvamdagrvlatgtpaell 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 210 ----SHRLEELmeigdYITIFRDGRFISERPVNdasIPWiieqmvgdkkkhfdYQPAPKGETVLSVQGLT-------Alh 278
Cdd:NF033858 226 artgADTLEAA-----FIALLPEEKRRGHQPVV---IPP--------------RPADDDDEPAIEARGLTmrfgdftA-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 279 psggykLNDVTFSLSKGEvigIYGLLGA---GRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKkglalvpedrqg 355
Cdd:NF033858 282 ------VDHVSFRIRRGE---IFGFLGSngcGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRR------------ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 356 egvVQMMSiQSnmtlsdFSLQG--------------FRrawkwLNPHKEQASVKAMIQQLAIK-VSDpQLPiTSLSGGNQ 420
Cdd:NF033858 341 ---VGYMS-QA------FSLYGeltvrqnlelharlFH-----LPAAEIAARVAEMLERFDLAdVAD-ALP-DSLPLGIR 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 421 QKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMA-QQGLAVMFSSSELDEVmALADRILVMADGRITA-DVP- 497
Cdd:NF033858 404 QRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLAsDTPa 482
|
570
....*....|..
gi 496059540 498 -----RHAVTRE 504
Cdd:NF033858 483 alvaaRGAATLE 494
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
414-492 |
2.27e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.11 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 414 SLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI 492
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
47-446 |
2.55e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 47 VLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVTLNSTHQAEKLgISIIFQELN---LFPNMNvmDNIFMANEFFQKG 123
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL-VSDEWQRNNtdmLSPGED--DTGRTTAEIIQDE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 124 KINEKYQYALAK-----SLLERleldvdpytPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQ 198
Cdd:PRK10938 110 VKDPARCEQLAQqfgitALLDR---------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 199 LKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVNDasipwIIEQMVGDKKKH---FDYQPAPKGETVLSVQGLT 275
Cdd:PRK10938 181 LHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREE-----ILQQALVAQLAHseqLEGVQLPEPDEPSARHALP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 276 ALHP---------SGGYK--LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPcQSGSVQL--------NGECI-D- 334
Cdd:PRK10938 256 ANEPrivlnngvvSYNDRpiLHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGYSNDLtlfgrrrgSGETIwDi 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 335 KAHF---QSRLKkglalvpedrqgegvvqmMSIQSNMTLSDFSLQGFRRAWKWLNPHKEQASVKAMiQQLAIKVSDPQL- 410
Cdd:PRK10938 335 KKHIgyvSSSLH------------------LDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQ-QWLDILGIDKRTa 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 496059540 411 --PITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGID 446
Cdd:PRK10938 396 daPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
280-492 |
2.80e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.18 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 280 SGGYKLNDVTFSLSKGEV--------------IGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSrLKKG 345
Cdd:PRK10790 338 SGRIDIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV-LRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 LALVPEDRqgegVVQMMSIQSNMTLS-DFSLQgfrRAWKWLNPHKEQASVKAMIQQLAIKVSDPQlpiTSLSGGNQQKVV 424
Cdd:PRK10790 417 VAMVQQDP----VVLADTFLANVTLGrDISEE---QVWQALETVQLAELARSLPDGLYTPLGEQG---NNLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 425 LGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS---SSELDevmalADRILVMADGRI 492
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAhrlSTIVE-----ADTILVLHRGQA 552
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-213 |
3.05e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 36 VNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIImdgipvtLNSTHQAEKLG-------ISIIFQELNLFPNmN 108
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-------INDSHNLKDINlkwwrskIGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 109 VMDNI-----------FMANEFFQ-------------------KGKINEKYQYALAKSLLE-RLELDV------------ 145
Cdd:PTZ00265 476 IKNNIkyslyslkdleALSNYYNEdgndsqenknkrnscrakcAGDLNDMSNTTDSNELIEmRKNYQTikdsevvdvskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 146 -----------DPYTPL-----EELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLK--RRGVTII 207
Cdd:PTZ00265 556 vlihdfvsalpDKYETLvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII 635
|
....*.
gi 496059540 208 yISHRL 213
Cdd:PTZ00265 636 -IAHRL 640
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
48-230 |
4.10e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.74 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPS---SGQIIMDGIPVTLNSTHQaeklgISIIFQELNLF-PNMNVMDN-IFMAnEFFQK 122
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRA-----ISAYVQQDDLFiPTLTVREHlMFQA-HLRMP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 123 GKINEKYQYALAKSLLERLELDVDPYT------PLEELGIGHQQLVEIARALSKDTRVLIMDEPTSAL----SQSEVKVL 192
Cdd:TIGR00955 130 RRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLdsfmAYSVVQVL 209
|
170 180 190
....*....|....*....|....*....|....*....
gi 496059540 193 FNvieqLKRRGVTIIYISHR-LEELMEIGDYITIFRDGR 230
Cdd:TIGR00955 210 KG----LAQKGKTIICTIHQpSSELFELFDKIILMAEGR 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
415-514 |
4.51e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.73 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI- 492
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLv 220
|
90 100
....*....|....*....|....*....
gi 496059540 493 ----TADV---PRHAVTREtLIAASTPQD 514
Cdd:PRK11153 221 eqgtVSEVfshPKHPLTRE-FIQSTLHLD 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
257-493 |
5.74e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 257 FDYQPAPKGETVLSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKA 336
Cdd:PRK10522 311 FPRPQAFPDWQTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 337 HFQSRLKKGLALvpedrqgegvvqmmsiqsnmtLSDFSLqgFRRAwkwLNPHKEQASVKAMIQQLA-------IKVSDPQ 409
Cdd:PRK10522 391 QPEDYRKLFSAV---------------------FTDFHL--FDQL---LGPEGKPANPALVEKWLErlkmahkLELEDGR 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 410 LPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYH-LIGKMAQQGLAVmFSSSELDEVMALADRILVMA 488
Cdd:PRK10522 445 ISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTI-FAISHDDHYFIHADRLLEMR 523
|
....*
gi 496059540 489 DGRIT 493
Cdd:PRK10522 524 NGQLS 528
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-207 |
6.91e-07 |
|
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: 50.35 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAG-VESPS--SGQIIMDGIPvtlNSTHQAEKLgISIIFQELNLFPNMNV 109
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGttSGQILFNGQP---RKPDQFQKC-VAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 110 MDNI-FMANEFFQKGKINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSE 188
Cdd:cd03234 99 RETLtYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170
....*....|....*....
gi 496059540 189 VKVLFNVIEQLKRRGVTII 207
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVI 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
48-225 |
6.96e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESpSSGQIIMDGipVTLNS-THQAEKLGISIIFQELNLFPNMNVMDniFMANEFFQKGKIN 126
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSvTLQTWRKAFGVIPQKVFIFSGTFRKN--LDPYEQWSDEEIW 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 127 EKYQYALAKSLLERLELDVDpyTPLEELGI----GHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQlKRR 202
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLD--FVLVDGGYvlsnGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFS 1401
|
170 180
....*....|....*....|...
gi 496059540 203 GVTIIYISHRLEELMEIGDYITI 225
Cdd:TIGR01271 1402 NCTVILSEHRVEALLECQQFLVI 1424
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-207 |
9.15e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.55 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPS--SGQIIMDGIPVTLN---STHQAEKLGIsiifqelnLFPNM 107
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNfqrSTGYVEQQDV--------HSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 108 NVMDNI-FMANeffqkgkinekyqyalaksllerleldvdpytpLEELGIGHQQLVEIARALSKDTRVLIMDEPTSAL-S 185
Cdd:cd03232 95 TVREALrFSAL---------------------------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLdS 141
|
170 180
....*....|....*....|..
gi 496059540 186 QSEVKVLfNVIEQLKRRGVTII 207
Cdd:cd03232 142 QAAYNIV-RFLKKLADSGQAIL 162
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
285-452 |
1.00e-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: 51.87 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSrLKKGLALVPEDRQgegvvqMMSI 364
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPV------LFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLQGFRRAWKWLNPHKEQASVKAMIQQLAIKVSDPQlpiTSLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:TIGR00957 1375 SLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGG---ENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
....*...
gi 496059540 445 IDVgaKTD 452
Cdd:TIGR00957 1452 VDL--ETD 1457
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
269-460 |
1.03e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 48.69 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTALHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLngecidkahfqsrlkkglal 348
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 349 vPEDRQgegvVQMMSIQSNMTLSdfSLQgfrrawkwlnphkeqasvkamiQQLAIKVSDpqlpitSLSGGNQQKVVLGKA 428
Cdd:cd03223 61 -PEGED----LLFLPQRPYLPLG--TLR----------------------EQLIYPWDD------VLSGGEQQRLAFARL 105
|
170 180 190
....*....|....*....|....*....|..
gi 496059540 429 LMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKM 460
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
285-491 |
1.04e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMP--CQSGSVQLNGECIDKahfqsRLKKGLALVPEDrqgEGVVQMM 362
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTK-----QILKRTGFVTQD---DILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSnmTLSDFSLQgfrRAWKWLNPHKEQASVKAMIQQLAIKVSDPQLP----ITSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:PLN03211 156 TVRE--TLVFCSLL---RLPKSLTKQEKILVAESVISELGLTKCENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSE-LDEVMALADRILVMADGR 491
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
288-508 |
1.24e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 288 VTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPcQSGSVQLNGECIDKAHFQSRLKKglalvpEDRQGEGVVQMMSIQSN 367
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRISEK------ERRNLVGAEVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 368 MT-LSDFSLQGFRrAWKWLNPHkeQASVKAMIQQLAIK------VSDPQLPIT----SLSGGNQQKVVLGKALMTQPQVV 436
Cdd:PRK11022 99 MTsLNPCYTVGFQ-IMEAIKVH--QGGNKKTRRQRAIDllnqvgIPDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 437 FLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITAD--------VPRHAVTRETLI 507
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETgkahdifrAPRHPYTQALLR 255
|
.
gi 496059540 508 A 508
Cdd:PRK11022 256 A 256
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-215 |
1.41e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGvESPS--------------SGQIIMD---GIPVTLNSTHQAEKLGIS 95
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgSGETIWDikkHIGYVSSSLHLDYRVSTS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQELNLFpnmnvMDNIFManefFQKgkINEKyQYALAKSLLERLELDVD-PYTPLEELGIGHQQLVEIARALSKDTRV 174
Cdd:PRK10938 355 VRNVILSGF-----FDSIGI----YQA--VSDR-QQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 496059540 175 LIMDEPTSALSQSEVKVLFNVIEQLKRRGVT-IIYISHRLEE 215
Cdd:PRK10938 423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAED 464
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-218 |
1.41e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 27 YPGVV--ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-LNSTHQAEKLgiSIIFQELNL 103
Cdd:PRK10789 323 YPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTkLQLDSWRSRL--AVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 104 FPNmNVMDNIFMANEFFQKGKINEKYQYALAKSLLERLELDVDpyTPLEELGI----GHQQLVEIARALSKDTRVLIMDE 179
Cdd:PRK10789 401 FSD-TVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYD--TEVGERGVmlsgGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059540 180 PTSALS-QSEVKVLFNVIEQlkRRGVTIIYISHRLEELME 218
Cdd:PRK10789 478 ALSAVDgRTEHQILHNLRQW--GEGRTVIISAHRLSALTE 515
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
285-446 |
1.58e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTEL---FKGLVGLMPCQ--SGSVQLNGECIDKAHFqSRLKKGLALVpedRQGEGVV 359
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLlrvFNRLIELYPEArvSGEVYLDGQDIFKMDV-IELRRRVQMV---FQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 QMMSIQSNMTLSdFSLQGFRRAWKWLNPHKEQASVKAmiqQLAIKVSDP-QLPITSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:PRK14247 95 PNLSIFENVALG-LKLNRLVKSKKELQERVRWALEKA---QLWDEVKDRlDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
....*...
gi 496059540 439 DEPTRGID 446
Cdd:PRK14247 171 DEPTANLD 178
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
285-492 |
1.89e-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: 48.68 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQ--SGSVQLNGECIdkahfqsrlkkgLALVPEDRQGEGVvqMM 362
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDI------------TDLPPEERARLGI--FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMTLSDFSLQGFRRAwkwLNphkeqasvkamiqqlaikvsdpqlpiTSLSGGNQQKVVLGKALMTQPQVVFLDEPT 442
Cdd:cd03217 82 AFQYPPEIPGVKNADFLRY---VN--------------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 443 RGIDVGAKTDVYHLIGKMAQQGLAVMFSSSE---LDEVMalADRILVMADGRI 492
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRI 183
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-229 |
1.95e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMK-MLAGVESPSSGQIIMDGipvTLNSTHQaeklgISIIFqelnlfpNMNVMD 111
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG---TVAYVPQ-----VSWIF-------NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 112 NIFMANEFFQkgkinEKYQYALAKSLLERlELDVDPYTPLEELGI-------GHQQLVEIARALSKDTRVLIMDEPTSAL 184
Cdd:PLN03130 698 NILFGSPFDP-----ERYERAIDVTALQH-DLDLLPGGDLTEIGErgvnisgGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 496059540 185 SQSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIgDYITIFRDG 229
Cdd:PLN03130 772 DAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEG 815
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
50-211 |
2.57e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.26 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 50 GENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT-----LNST-----HQAeklGISiifQELNLFPNMNvmdnifmaneF 119
Cdd:PRK13538 34 GPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeYHQDllylgHQP---GIK---TELTALENLR----------F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 120 FQK--GKIN-EKYQYALAKSLLERLElDVdpytPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVI 196
Cdd:PRK13538 98 YQRlhGPGDdEALWEALAQVGLAGFE-DV----PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
170
....*....|....*
gi 496059540 197 EQLKRRGVTIIYISH 211
Cdd:PRK13538 173 AQHAEQGGMVILTTH 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-223 |
2.86e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 2.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 150 PLEELGIGHQQLVEIARALSKDTR--VLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRlEELMEIGDYI 223
Cdd:cd03238 84 KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWI 158
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-223 |
3.10e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.01 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFMANEFFQK-GKINEKYQyALAKSLLERLELDVDPYTpleeLGIGHQQLVEIARALSK-DT-RVL-IMDEPTSALSQSE 188
Cdd:TIGR00630 793 VEEAYEFFEAvPSISRKLQ-TLCDVGLGYIRLGQPATT----LSGGEAQRIKLAKELSKrSTgRTLyILDEPTTGLHFDD 867
|
90 100 110
....*....|....*....|....*....|....*
gi 496059540 189 VKVLFNVIEQLKRRGVTIIYISHRLeELMEIGDYI 223
Cdd:TIGR00630 868 IKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTADYI 901
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
287-494 |
3.17e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 287 DVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdKAHFQSRLKkglalvpEDRQgegvvQM-MSIQ 365
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-PAMSRSRLY-------TVRK-----RMsMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 366 SNMTLSDFSLqgFRR-AWKwLNPHKE------QASVKAMIQQLAIKVSDPQLPiTSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:PRK11831 92 SGALFTDMNV--FDNvAYP-LREHTQlpapllHSTVMMKLEAVGLRGAAKLMP-SELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 439 DEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRITA 494
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
415-514 |
3.83e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.92 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADRILVMADGRI- 492
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIv 220
|
90 100
....*....|....*....|....*....
gi 496059540 493 ----TADV---PRHAVTREtLIAASTPQD 514
Cdd:COG1135 221 eqgpVLDVfanPQSELTRR-FLPTVLNDE 248
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-239 |
4.07e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLsRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESP----SSGQIIMDGIPV---TLNSTHqae 90
Cdd:PRK10418 5 IELRNI-ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapcALRGRK--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 91 klgISIIFQE----LNLFPNMNVMdnifmANE-FFQKGKINEKyqyALAKSLLERLELDvDPYTPLE----ELGIGHQQL 161
Cdd:PRK10418 81 ---IATIMQNprsaFNPLHTMHTH-----AREtCLALGKPADD---ATLTAALEAVGLE-NAARVLKlypfEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 162 VEIARALSKDTRVLIMDEPTS---ALSQSEVKVLFNVIEQlkRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVN 238
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTdldVVAQARILDLLESIVQ--KRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE 226
|
.
gi 496059540 239 D 239
Cdd:PRK10418 227 T 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
285-495 |
6.53e-06 |
|
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: 47.14 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecidkahfqsRLKKGLALvpedrqGEGVVQMMSI 364
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGL------GGGFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSdFSLQGFRRawkwlnphKEQASVKAMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRG 444
Cdd:cd03220 102 RENIYLN-GRLLGLSR--------KEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 445 IDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVMADGRITAD 495
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
285-492 |
6.67e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.67 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIdKAHFQSRLKKGLALVPEdRqgegvVQMMS- 363
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEAALRQAISVVSQ-R-----VHLFSa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 364 -IQSNMTLSdfslqgfrrawkwlNPHKEQASVKAMIQQ--LAIKVSDPQlPITS--------LSGGNQQKVVLGKALMTQ 432
Cdd:PRK11160 429 tLRDNLLLA--------------APNASDEALIEVLQQvgLEKLLEDDK-GLNAwlgeggrqLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 433 PQVVFLDEPTRGIDvgAKTD--VYHLIGKMAqQGLAVMFSSSELDEvMALADRILVMADGRI 492
Cdd:PRK11160 494 APLLLLDEPTEGLD--AETErqILELLAEHA-QNKTVLMITHRLTG-LEQFDRICVMDNGQI 551
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-216 |
7.00e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 32 ALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIP--VTLNSTHQAEKLGISIIfqELNlfpnmnv 109
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLNGQLTGIENI--ELK------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 110 mdNIFMAnefFQKGKINEkyqyaLAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEV 189
Cdd:PRK13545 110 --GLMMG---LTKEKIKE-----IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180
....*....|....*....|....*..
gi 496059540 190 KVLFNVIEQLKRRGVTIIYISHRLEEL 216
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
261-492 |
7.57e-06 |
|
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: 48.56 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 261 PAPKGETVLSVQGLTALHPSGGYK-LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGecIDKAHFQ 339
Cdd:TIGR02203 323 AIERARGDVEFRNVTFRYPGRDRPaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG--HDLADYT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 340 SR-LKKGLALVPEDrqgegvVQMM--SIQSNMTLSDfsLQGFRRAwkwlnpHKEQASVKAMIQQLAIKVSDP-QLPITS- 414
Cdd:TIGR02203 401 LAsLRRQVALVSQD------VVLFndTIANNIAYGR--TEQADRA------EIERALAAAYAQDFVDKLPLGlDTPIGEn 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 ---LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVyhligkmaQQGL-AVMFSSSELdeVMAL-------ADR 483
Cdd:TIGR02203 467 gvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLV--------QAALeRLMQGRTTL--VIAHrlstiekADR 536
|
....*....
gi 496059540 484 ILVMADGRI 492
Cdd:TIGR02203 537 IVVMDDGRI 545
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
269-489 |
8.42e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 46.71 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTaLHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMP---CQSGSVQLNGECIDkahfqsrlkkg 345
Cdd:COG4136 2 LSLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLT----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 346 lALVPEDRQGEGVVQM------MSIQSNMTlsdFSL-QGFRRAWKwlnphkeQASVKAMIQQLAIK---VSDPqlpiTSL 415
Cdd:COG4136 70 -ALPAEQRRIGILFQDdllfphLSVGENLA---FALpPTIGRAQR-------RARVEQALEEAGLAgfaDRDP----ATL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496059540 416 SGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMA-QQGLAVMFSSSELDEVMAlADRILVMAD 489
Cdd:COG4136 135 SGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIrQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
285-492 |
1.04e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 46.76 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSRLKKgLALVPEdrqgEGVVQMMSI 364
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQ----EPVLFDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 365 QSNMTLSDFSLQgfrrawkwlNPHKEQASVKAMIQQLAIKvsdpqLPI----------TSLSGGNQQKVVLGKALMTQPQ 434
Cdd:cd03249 94 AENIRYGKPDAT---------DEEVEEAAKKANIHDFIMS-----LPDgydtlvgergSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 435 VVFLDEPTRGIDVGAKTDVYHLIGKmAQQGLAVMFSSSELDEVMAlADRILVMADGRI 492
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDR-AMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQV 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
268-499 |
1.47e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTA--LHPSGGYKLND-VTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMP--CQSGSVQLNGECIDKAHFQSRL 342
Cdd:PRK15093 3 LLDIRNLTIefKTSDGWVKAVDrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 343 KKGL--------------ALVPEDRQGEGVVQmmsiqsnmTLSDFSLQGfrRAWKWLNPHKEQASvkAMIQQLAIKvsDP 408
Cdd:PRK15093 83 RRKLvghnvsmifqepqsCLDPSERVGRQLMQ--------NIPGWTYKG--RWWQRFGWRKRRAI--ELLHRVGIK--DH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 409 QLPITS----LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ-GLAVMFSSSELDEVMALADR 483
Cdd:PRK15093 149 KDAMRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADK 228
|
250
....*....|....*.
gi 496059540 484 ILVMADGRITADVPRH 499
Cdd:PRK15093 229 INVLYCGQTVETAPSK 244
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
150-223 |
1.86e-05 |
|
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: 46.45 E-value: 1.86e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 150 PLEELGIGHQQLVEIARALSKDTR---VLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLeELMEIGDYI 223
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWI 241
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
33-229 |
2.46e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.00 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipvtlnsthqaeklGISIIFQELNLFPNmNVMDN 112
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------------RISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFManeffqkGKINEKYQYalaKSLLERLELDVD-------PYTPLEELGI----GHQQLVEIARALSKDTRVLIMDEPT 181
Cdd:cd03291 118 IIF-------GVSYDEYRY---KSVVKACQLEEDitkfpekDNTVLGEGGItlsgGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496059540 182 SALSQSEVKVLFN--VIEQLKRRgvTIIYISHRLEELmEIGDYITIFRDG 229
Cdd:cd03291 188 GYLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHL-KKADKILILHEG 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
269-491 |
2.64e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 43.98 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 269 LSVQGLTaLHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLnGECIDKAHFqsrlkkglal 348
Cdd:cd03221 1 IELENLS-KTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVKIGYF---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 349 vpedrqgegvvqmmsiqsnmtlsdfslqgfrrawkwlnphkeqasvkamiqqlaikvsdPQLpitslSGGNQQKVVLGKA 428
Cdd:cd03221 69 -----------------------------------------------------------EQL-----SGGEKMRLALAKL 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 429 LMTQPQVVFLDEPTRGIDVGAKTdvyHLIGKMAQQGLAVMFSSSE---LDEVmalADRILVMADGR 491
Cdd:cd03221 85 LLENPNLLLLDEPTNHLDLESIE---ALEEALKEYPGTVILVSHDryfLDQV---ATKIIELEDGK 144
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-225 |
2.67e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 18 IETHDLSRVYP--GVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESpSSGQIIMDGipVTLNS-THQAEKLGI 94
Cdd:cd03289 3 MTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG--VSWNSvPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 95 SIIFQELNLFPN---MNVMDNifmaneffqkGKINEKYQYALA-----KSLLERL--ELDVDPYTPLEELGIGHQQLVEI 164
Cdd:cd03289 80 GVIPQKVFIFSGtfrKNLDPY----------GKWSDEEIWKVAeevglKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496059540 165 ARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQlKRRGVTIIYISHRLEELMEIGDYITI 225
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLECQRFLVI 209
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-82 |
2.81e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 2.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496059540 36 VNYR---VYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT 82
Cdd:cd03222 15 LLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV 64
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
103-223 |
3.36e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 103 LFPNMNVMDNIFM----ANEFF-QKGKINEKYQyALAKSLLERLELDvdpyTPLEELGIGHQQLVEIARAL---SKDTRV 174
Cdd:PRK00635 759 RYKGKNIADILEMtayeAEKFFlDEPSIHEKIH-ALCSLGLDYLPLG----RPLSSLSGGEIQRLKLAYELlapSKKPTL 833
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 496059540 175 LIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRLeELMEIGDYI 223
Cdd:PRK00635 834 YVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYV 881
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
31-230 |
3.39e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 31 VALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIImdgipvtlnsthqAEKlGISIIFQELNLFpNMNVM 110
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AER-SIAYVPQQAWIM-NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 111 DNIFmaneFFqkgkiNEKYQYALAKSL-LERLELDVDPY-----TPLEELGI----GHQQLVEIARALSKDTRVLIMDEP 180
Cdd:PTZ00243 739 GNIL----FF-----DEEDAARLADAVrVSQLEADLAQLgggleTEIGEKGVnlsgGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 496059540 181 TSALsqsEVKVLFNVIEQLKR---RGVTIIYISHRLeELMEIGDYITIFRDGR 230
Cdd:PTZ00243 810 LSAL---DAHVGERVVEECFLgalAGKTRVLATHQV-HVVPRADYVVALGDGR 858
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-234 |
3.74e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPssgqiiMDGIPVTLNSThQAEKLGISIIFqelnlfpNMNVMDN 112
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH------AETSSVVIRGS-VAYVPQVSWIF-------NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFMANEFFqkgkiNEKYQYALAKSLLERlELDVDPYTPLEELGI-------GHQQLVEIARALSKDTRVLIMDEPTSALS 185
Cdd:PLN03232 699 ILFGSDFE-----SERYWRAIDVTALQH-DLDLLPGRDLTEIGErgvnisgGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496059540 186 QSEVKVLFNVIEQLKRRGVTIIYISHRLEELMEIgDYITIFRDGRFISE 234
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEE 820
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
285-492 |
4.31e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 46.25 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDK--AHFqsrLKKGLALVpedrQGEGVVQMM 362
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydHHY---LHRQVALV----GQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 SIQSNMT--LSDFSLQGFRRAWKWLNPHKeqaSVKAMIQQLAIKVSDPQlpiTSLSGGNQQKVVLGKALMTQPQVVFLDE 440
Cdd:TIGR00958 570 SVRENIAygLTDTPDEEIMAAAKAANAHD---FIMEFPNGYDTEVGEKG---SQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496059540 441 PTRGIDVGAKTDVYHLigkMAQQGLAVMFSSSELDEVMAlADRILVMADGRI 492
Cdd:TIGR00958 644 ATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
415-490 |
4.34e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.54 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 415 LSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFS----SSELdevMALADRILVMADG 490
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTihqpSASI---FEKFDRLLLLKRG 185
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
111-239 |
4.72e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 111 DNIFMANEFFQkgkINEKYQYALAKSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVK 190
Cdd:NF000106 105 ENLYMIGR*LD---LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 496059540 191 VLFNVIEQLKRRGVTIIYISHRLEELMEIGDYITIFRDGRFISERPVND 239
Cdd:NF000106 182 EVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
266-446 |
5.40e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.77 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 266 ETVLSVQGLTaLHPSGGYKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLV---GLMP--CQSGSVQLNGECIDKAHFQS 340
Cdd:PRK14239 3 EPILQVSDLS-VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 341 -RLKKGLALVPEdrqgegvvqmmsiQSN---MTLSDFSLQGFRrawkwLNPHKEQA----SVKAMIQQLAI------KVS 406
Cdd:PRK14239 82 vDLRKEIGMVFQ-------------QPNpfpMSIYENVVYGLR-----LKGIKDKQvldeAVEKSLKGASIwdevkdRLH 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 496059540 407 DPQLpitSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGID 446
Cdd:PRK14239 144 DSAL---GLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
285-330 |
5.77e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 5.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNG 330
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
268-468 |
7.37e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.09 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 268 VLSVQGLTALHpsGG-YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSR---LK 343
Cdd:PRK13539 2 MLEGEDLACVR--GGrVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchyLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 344 KGLALVPEdrqgegvvqmMSIQSNMTlsdfslqgFRRAWKWLNPHKEQASVKAM-IQQLAikvsdpQLPITSLSGGNQQK 422
Cdd:PRK13539 80 HRNAMKPA----------LTVAENLE--------FWAAFLGGEELDIAAALEAVgLAPLA------HLPFGYLSAGQKRR 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 496059540 423 VVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLI-GKMAQQGLAVM 468
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVALFAELIrAHLAQGGIVIA 182
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
48-92 |
8.21e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 8.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQI-IMDGIPVTLNSTHQAEKL 92
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFL 388
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-234 |
8.41e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.71 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipvtlnsthqaeklGISIIFQELnLFPNMNVMDN 112
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------SVAYVPQQA-WIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFMANEffqkgkINEKYQYAL--AKSLLERLE-LDVDPYTPLEELGI----GHQQLVEIARALSKDTRVLIMDEPTSALS 185
Cdd:TIGR00957 719 ILFGKA------LNEKYYQQVleACALLPDLEiLPSGDRTEIGEKGVnlsgGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496059540 186 QSEVKVLF-NVIEQLKR-RGVTIIYISHRLEELMEIgDYITIFRDGRfISE 234
Cdd:TIGR00957 793 AHVGKHIFeHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGK-ISE 841
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-380 |
8.89e-05 |
|
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: 45.29 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 33 LDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGipvtlnsthqaeklGISIIFQELNLFPNmNVMDN 112
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFManeffqkGKINEKYQYalaKSLLE--RLELDVDPY-----TPLEELGI----GHQQLVEIARALSKDTRVLIMDEPT 181
Cdd:TIGR01271 507 IIF-------GLSYDEYRY---TSVIKacQLEEDIALFpekdkTVLGEGGItlsgGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 182 SALSQSEVKVLFN--VIEQLKRRgvTIIYISHRLEELMEiGDYITIFRDGR--FISERPVNDASIPWIIEQMVGdkKKHF 257
Cdd:TIGR01271 577 THLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGVcyFYGTFSELQAKRPDFSSLLLG--LEAF 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 258 DYQPAPKGETVL-------SVQGLTAL-------HPSggYKLNDVTFSLSKGEVIGIYGLLGAGRTELFkglvglmpcQS 323
Cdd:TIGR01271 652 DNFSAERRNSILtetlrrvSIDGDSTVfsgpetiKQS--FKQPPPEFAEKRKQSIILNPIASARKFSFV---------QM 720
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 496059540 324 GSVQLNGECIDKAhFQSRLKKGLALVPEDRQGEGVVQmmsiQSNMTLSDFSLQGFRR 380
Cdd:TIGR01271 721 GPQKAQATTIEDA-VREPSERKFSLVPEDEQGEESLP----RGNQYHHGLQHQAQRR 772
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
362-446 |
9.29e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 362 MSIQSNMTL--SDFSLQGFRRAWKWlnphkeqASVKAMIQQLAIKVSDPQLPI-TSLSGGNQQKVVLGKALMTQPQVVFL 438
Cdd:PTZ00265 1310 MSIYENIKFgkEDATREDVKRACKF-------AAIDEFIESLPNKYDTNVGPYgKSLSGGQKQRIAIARALLREPKILLL 1382
|
....*...
gi 496059540 439 DEPTRGID 446
Cdd:PTZ00265 1383 DEATSSLD 1390
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
412-487 |
1.23e-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: 43.89 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496059540 412 ITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVMFSSSELDEVMALADRILVM 487
Cdd:cd03236 137 IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
414-463 |
1.25e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 1.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496059540 414 SLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ 463
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-184 |
1.48e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 16 VIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIimdgipvtlnstHQAEKLGIS 95
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HCGTKLEVA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 IIFQ-ELNLFPNMNVMDNIfmaNEFFQKGKINEKYQYALAkSLLERLELDVDPYTPLEELGIGHQQLVEIARALSKDTRV 174
Cdd:PRK11147 386 YFDQhRAELDPEKTVMDNL---AEGKQEVMVNGRPRHVLG-YLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNL 461
|
170
....*....|
gi 496059540 175 LIMDEPTSAL 184
Cdd:PRK11147 462 LILDEPTNDL 471
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-223 |
1.85e-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: 44.23 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 IFMANEFFQKGKINEKYQYA---LAKSLLERLELDVD---PYTPLEE----LGIGHQQLVEIARAL-SKDTRVL-IMDEP 180
Cdd:TIGR00630 438 IREAHEFFNQLTLTPEEKKIaeeVLKEIRERLGFLIDvglDYLSLSRaagtLSGGEAQRIRLATQIgSGLTGVLyVLDEP 517
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496059540 181 TSALSQSEVKVLFNVIEQLKRRGVTIIYISHRlEELMEIGDYI 223
Cdd:TIGR00630 518 SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYV 559
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-82 |
2.40e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 2.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 5 DIVTPHSveSEVIIETHDLSRVYPGVVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDGIPVT 82
Cdd:PRK13543 1 MIEPLHT--APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT 76
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
413-446 |
2.51e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.72 E-value: 2.51e-04
10 20 30
....*....|....*....|....*....|....
gi 496059540 413 TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGID 446
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
48-236 |
2.55e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAGVESPSSGQIIMdgipvtlnsthqaeklgisiifqelnlfpnmnVMDNIFMANEFFQKGKINE 127
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------IDGEDILEEVLDQLLLIIV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 128 KYQYAlaksllerleldvdpytpleELGIGHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIE------QLKR 201
Cdd:smart00382 55 GGKKA--------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKSE 114
|
170 180 190
....*....|....*....|....*....|....*
gi 496059540 202 RGVTIIYISHRLEELmeIGDYITIFRDGRFISERP 236
Cdd:smart00382 115 KNLTVILTTNDEKDL--GPALLRRRFDRRIVLLLI 147
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
285-492 |
3.34e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 43.41 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGECIDKAHFQSrLKKGLALVPED-----Rqgegvv 359
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS-LRRNIAVVFQDaglfnR------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 360 qmmSIQSNMTL--SDFSLQGFRRAWKwlnphKEQAS--VKAMIQQLAIKVSDPQLpitSLSGGNQQKVVLGKALMTQPQV 435
Cdd:PRK13657 424 ---SIEDNIRVgrPDATDEEMRAAAE-----RAQAHdfIERKPDGYDTVVGERGR---QLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496059540 436 VFLDEPTRGIDVGAKTDVyhligKMAqqglavmfssseLDEVM---------------ALADRILVMADGRI 492
Cdd:PRK13657 493 LILDEATSALDVETEAKV-----KAA------------LDELMkgrttfiiahrlstvRNADRILVFDNGRV 547
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-450 |
5.63e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 5.63e-04
10 20 30
....*....|....*....|....*....|....*....
gi 496059540 413 TSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGID-VGAK 450
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpVGTA 186
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
411-493 |
6.29e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 411 PITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAktdVYHLI-GKMAQQGLAVMFSSSElDEVMALADRILVMAD 489
Cdd:PLN03073 624 PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIqGLVLFQGGVLMVSHDE-HLISGSVDELWVVSE 699
|
....
gi 496059540 490 GRIT 493
Cdd:PLN03073 700 GKVT 703
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
137-223 |
1.57e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 137 LLERLELDVD---PYTPLEE----LGIGHQQLVEIARAL-SKDTRVL-IMDEPTSALSQSEVKVLFNVIEQLKRRGVTII 207
Cdd:cd03270 114 IRERLGFLVDvglGYLTLSRsaptLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
|
90
....*....|....*.
gi 496059540 208 YISHRlEELMEIGDYI 223
Cdd:cd03270 194 VVEHD-EDTIRAADHV 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
48-230 |
1.84e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.02 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 48 LIGENGAGKSTMMKMLAG-VESPS-SGQIIMDGIPVTLNSTHQaeklgISIIFQELNLFPNMNVMDNIFMANEFFQKGKI 125
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPTKQILKR-----TGFVTQDDILYPHLTVRETLVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 126 NEKYQYALAKSLLERLELDVDPYTPLEELGI-----GHQQLVEIARALSKDTRVLIMDEPTSALSQSEVKVLFNVIEQLK 200
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENTIIGNSFIrgisgGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170 180 190
....*....|....*....|....*....|.
gi 496059540 201 RRGVTIIYISHR-LEELMEIGDYITIFRDGR 230
Cdd:PLN03211 254 QKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
283-331 |
1.92e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 496059540 283 YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNGE 331
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
285-514 |
2.36e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 285 LNDVTFSLSKGEVIGIYGLLGAGRTELFkGLV-GLMPCQSGSVQ-LNGECIDKAHfQSRLKKGLALVPedrQGEGvvqmm 362
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLIaGARKIQQGRVEvLGGDMADARH-RRAVCPRIAYMP---QGLG----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 363 siqSN--MTLS-----DF--SLQGFRRAWKwlnphkeqasvKAMIQQL-------------AIKvsdpqlpitsLSGGNQ 420
Cdd:NF033858 87 ---KNlyPTLSvfenlDFfgRLFGQDAAER-----------RRRIDELlratglapfadrpAGK----------LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 421 QKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQ--GLAVMFSSSELDEvmalADR---ILVMADGRItad 495
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEE----AERfdwLVAMDAGRV--- 215
|
250
....*....|....*....
gi 496059540 496 vprhavtretlIAASTPQD 514
Cdd:NF033858 216 -----------LATGTPAE 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
411-468 |
2.40e-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: 40.54 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 496059540 411 PITSLSGGNQQKVVLGKALMTQPQVVFLDEPTRGIDVGAKTDVYHLIGKMAQQGLAVM 468
Cdd:COG1245 209 DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-95 |
3.12e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 8 TPHSVESEVIIETHDLSRVYPG-VVALDSVNYRVYRNKVNVLIGENGAGKSTMMKMLAGVESPSSGQIIMDG-IPVTLNS 85
Cdd:PLN03073 499 TPDDRPGPPIISFSDASFGYPGgPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkVRMAVFS 578
|
90
....*....|
gi 496059540 86 THQAEKLGIS 95
Cdd:PLN03073 579 QHHVDGLDLS 588
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
283-330 |
3.18e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 3.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 496059540 283 YKLNDVTFSLSKGEVIGIYGLLGAGRTELFKGLVGLMPCQSGSVQLNG 330
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-221 |
3.57e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 3.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496059540 157 GHQQLVEIARALS----KDTRVLIMDEPTSALSQSEVKVLFNVIEQLKRRGVTIIYISHRlEELMEIGD 221
Cdd:cd03227 81 GEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL-PELAELAD 148
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
29-212 |
5.57e-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: 39.35 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 29 GVVALDSVNYRVyRNKVNVLI-GENGAGKSTMMKMLAGV--------ESPSSGQIIMdgIP----VTLNSthqaeklgis 95
Cdd:TIGR00954 464 GDVLIESLSFEV-PSGNNLLIcGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY--VPqrpyMTLGT---------- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 96 iiFQELNLFPnmnvmDNIFmanEFFQKGkinekYQYALAKSLLERLELD-----------VDPYtpLEELGIGHQQLVEI 164
Cdd:TIGR00954 531 --LRDQIIYP-----DSSE---DMKRRG-----LSDKDLEQILDNVQLThilereggwsaVQDW--MDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496059540 165 ARALSKDTRVLIMDEPTSALSqseVKVLFNVIEQLKRRGVTIIYISHR 212
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVS---VDVEGYMYRLCREFGITLFSVSHR 638
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
396-485 |
5.67e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 396 AMIQQLAIKVSDPQLPITSLSGGNQQKVVLGKALMTQPQVV--FLDEPTRGIDvgaKTDVYHLIG---KMAQQGLAVMFs 470
Cdd:PRK00635 458 SILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLH---PQDTHKLINvikKLRDQGNTVLL- 533
|
90
....*....|....*.
gi 496059540 471 sSELDEVM-ALADRIL 485
Cdd:PRK00635 534 -VEHDEQMiSLADRII 548
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
44-211 |
8.36e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 38.41 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 44 KVNVLIGENGAGKSTMMKMLAGVespSSGQIIM-----DGIPVTLNST-HQAEKLGISIIF--QELNLFPNMNVMDN--- 112
Cdd:COG4938 21 PLTLLIGPNGSGKSTLIQALLLL---LQSNFIYlpaerSGPARLYPSLvRELSDLGSRGEYtaDFLAELENLEILDDksk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496059540 113 --IFMANEFFQK---GKINEKyqyalAKSLLERLELDVDP---YTPLEELGIGHQQLVEI---ARALSKDTRVLIMDEPT 181
Cdd:COG4938 98 elLEQVEEWLEKifpGKVEVD-----ASSDLVRLVFRPSGngkRIPLSNVGSGVSELLPIllaLLSAAKPGSLLIIEEPE 172
|
170 180 190
....*....|....*....|....*....|...
gi 496059540 182 SAL---SQSEvkvLFNVIEQLKRRGVTIIYISH 211
Cdd:COG4938 173 AHLhpkAQSA---LAELLAELANSGVQVIIETH 202
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
37-58 |
8.71e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.37 E-value: 8.71e-03
10 20
....*....|....*....|....*...
gi 496059540 37 NYRVYRN------KVNVLIGENGAGKST 58
Cdd:COG4637 9 NFKSLRDlelplgPLTVLIGANGSGKSN 36
|
|
| |
