|
Name |
Accession |
Description |
Interval |
E-value |
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-533 |
0e+00 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 637.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 1 MRLLRELLHNARWRILLSILSSALSAATSIGLIGYINRSLEHGLDDLGPALLLFGGLLLLLFISGVISQWLLVQIGHRLV 80
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 81 YQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISLYNGLLLLTGLAYMAWLSVPFFVLTLGVIALG 160
Cdd:COG4615 81 ARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 161 VGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDGRCELGLSRERRHLLYRHRLEPVASASLAASVRADTLWAVNLNWTT 240
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDEDLQPTAERYRDLRIRADTIFALANNWGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 241 LLVFVLIGTLFFLGQGLGLLDQQVVVGYVLAIMFLRTPISVILDAVPAVIRGHVALQAIDALAL-----GESVTFTEPEQ 315
Cdd:COG4615 241 LLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELalaaaEPAAADAAAPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 316 AAAPFRELRLSNVHYRYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRT 395
Cdd:COG4615 321 APADFQTLELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 396 SEWHREHFAAIFADFYLFADVLGEGGQHDglEARVEHYLERLGLAHKVQFVDGRLSTTALSQGQRKRLALLLLMMEDREV 475
Cdd:COG4615 401 REAYRQLFSAVFSDFHLFDRLLGLDGEAD--PARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPI 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 476 FLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:COG4615 479 LVFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-532 |
1.14e-157 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 460.98 E-value: 1.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 1 MRLLRELLHNARWRILLSILSSALSAATSIGLIGYINRSLEHGLDDLGPALLLFGGLLLLLFISGVISQWLLVQIGHRLV 80
Cdd:PRK10522 1 MELLRLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 81 YQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISLYNGLLLLTGLAYMAWLSVPFFVLTLGVIALG 160
Cdd:PRK10522 81 YRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFVRLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWMAVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 161 VGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDGRCELGLSRERRHLLYRHRLEPVASASLAASVRADTLWAVNLNWTT 240
Cdd:PRK10522 161 IWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 241 LLVFVLIGTLFFLGQGLGLLDQQVVVGYVLAIMFLRTPISVILDAVPAVIRGHVALQAIDALALGE-SVTFTEPeQAAAP 319
Cdd:PRK10522 241 IMMLGAIGLVFYMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKLALAPyKAEFPRP-QAFPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 320 FRELRLSNVHYRYPGQSddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH 399
Cdd:PRK10522 320 WQTLELRNVTFAYQDNG----FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REHFAAIFADFYLFADVLGEGGQhDGLEARVEHYLERLGLAHKVQFVDGRLSTTALSQGQRKRLALLLLMMEDREVFLLD 479
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLLGPEGK-PANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLD 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 480 EWAADQDPVFRHVFYHELLPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQL 532
Cdd:PRK10522 475 EWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
75-533 |
2.85e-110 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 339.63 E-value: 2.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 75 IGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISLYNGLLLLTGLAYMAWLSVPFFVLTL 154
Cdd:TIGR01194 80 AGMHIIANLRIALCEKILGAPIEEIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIFFFCIAYLAYLSVPMFAITI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 155 GVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDGRCELGLSRERRHLLYRHRLEPVASASLAASVRADTLWAV 234
Cdd:TIGR01194 160 SAIIIGTAAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGIRRLSFAHGAIQESANNIADLHIIEILIFIA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 235 NLNWTTLLVFVLIGTLFFLGQGLGLLDQQVVVGYVLAIMFLRTPISVILDAVPAVIRGHVALQAIdaLALGESVTFTEPE 314
Cdd:TIGR01194 240 AENFGQLLFFLLIGCALFAAAMFASIDAAAISAFVLALLYIKGPLEMLVSALPILAQAQIACQRL--ADFGERFNEPEPE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 315 ---------QAAAPFR---ELRLSNVHYRYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAG 382
Cdd:TIGR01194 318 lelsdadnvLLLAHDKsvdSIELKDVHMNPKAPEGSEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 383 TVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLG-EGGQHDGLEaRVEHYLERLGLAHKVQFVDGRLS-TTALSQGQR 460
Cdd:TIGR01194 398 EILLDGAAVSADSRDDYRDLFSAIFADFHLFDDLIGpDEGEHASLD-NAQQYLQRLEIADKVKIEDGGFStTTALSTGQQ 476
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 461 KRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:TIGR01194 477 KRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCIV 549
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
63-533 |
2.46e-51 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 184.60 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAF-KQLPISLYNGLLLLTGLAY 141
Cdd:COG1132 76 LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDGRCEL-GLSRERRHllyRHRLEPVASA 220
Cdd:COG1132 156 LFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVkAFGREERE---LERFREANEE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 221 SLAASVRADTLWAVNLNWTTLLVFVLIGTLFFLGqGLGLLDQQVVVG----YVLAIMFLRTPISVILDAVPAVIRGHVAL 296
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLGLALVLLVG-GLLVLSGSLTVGdlvaFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 297 QAIDALaLGESVTFTEPEQAAA--PFR-ELRLSNVHYRYPGQS---DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLA 370
Cdd:COG1132 312 ERIFEL-LDEPPEIPDPPGAVPlpPVRgEIEFENVSFSYPGDRpvlKD-------ISLTIPPGETVALVGPSGSGKSTLV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 371 KLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGE---GGQHDGLEARVEHYLERLGLAHKV-QFV 446
Cdd:COG1132 384 NLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIREnirYGRPDATDEEVEEAAKAAQAHEFIeALP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 447 DGrLST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQDP-----VFRHVfyHELLpelkaAGKTVIAITH-- 513
Cdd:COG1132 464 DG-YDTvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTetealIQEAL--ERLM-----KGRTTIVIAHrl 535
|
490 500
....*....|....*....|....
gi 2733243359 514 ----DdryfdvADRIYRLDYGQLV 533
Cdd:COG1132 536 stirN------ADRILVLDDGRIV 553
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
78-533 |
5.05e-42 |
|
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: 158.78 E-value: 5.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 78 RLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQL---PISLynGLLLLTGLAYMAWLSVPF-FVLT 153
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVllpLLVA--LLVILAAVAFLAFFSPALaLVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 154 LGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDGRCELGLS-RERRhllYRHRLEPVASASLAASVRADTLW 232
Cdd:COG4987 163 LGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYgALDR---ALARLDAAEARLAAAQRRLARLS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 233 AVNLNWTTLLV-FVLIGTLFFLGQGL--GLLDQQVVVGYVLAIMFLRTPISVILDAVPAVIRGHVALQAIDALA-LGESV 308
Cdd:COG4987 240 ALAQALLQLAAgLAVVAVLWLAAPLVaaGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLdAPPAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 309 TFTEPEQAAAPFRELRLSNVHYRYPGQSDDfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG 388
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSFRYPGAGRP---VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 389 VPLDGRTSEWHREHFAAIFADFYLFADVLGEG---GQHDGLEARVEHYLERLGLAHKVQFVDGRLST------TALSQGQ 459
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENlrlARPDATDEELWAALERVGLGDWLAALPDGLDTwlgeggRRLSGGE 476
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 460 RKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELKaaGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
63-533 |
5.44e-41 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 157.30 E-value: 5.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALtKDVTTVATAF-KQLPISLYNGLLLLTGLAY 141
Cdd:COG2274 211 LLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLtGSLLTALLDLLFVLIFLIV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDGRCEL-GLSRERRhllYRHRLEPVASA 220
Cdd:COG2274 290 LFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIkALGAESR---FRRRWENLLAK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 221 SLAASVRADTLWAVNLNWTTLLVFVLIGTLFFLGqGLGLLDQQVVVGYVLAIMFLR----TPISVILDAVPAVIRGHVAL 296
Cdd:COG2274 367 YLNARFKLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQLIAFNILSgrflAPVAQLIGLLQRFQDAKIAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 297 QAIDalalgeSVTFTEPEQAAAPFR--------ELRLSNVHYRYPGQSDDfafQLGPIDLSIRRGELIFVVGGNGSGKST 368
Cdd:COG2274 446 ERLD------DILDLPPEREEGRSKlslprlkgDIELENVSFRYPGDSPP---VLDNISLTIKPGERVAIVGRSGSGKST 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 369 LAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGE---GGQHDGLEARVEHYLERLGLAHKVQF 445
Cdd:COG2274 517 LLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIREnitLGDPDATDEEIIEAARLAGLHDFIEA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 446 VDGRLST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFyHELLPELkAAGKTVIAITHDDRYFD 519
Cdd:COG2274 597 LPMGYDTvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII-LENLRRL-LKGRTVIIIAHRLSTIR 674
|
490
....*....|....
gi 2733243359 520 VADRIYRLDYGQLV 533
Cdd:COG2274 675 LADRIIVLDKGRIV 688
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
324-531 |
8.31e-40 |
|
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: 143.76 E-value: 8.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 324 RLSNVHYRYPGQSddfAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHF 403
Cdd:cd03225 1 ELKNLSFSYPDGA---RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 404 AAIF--ADFYLFADVLGE----GGQHDGL-----EARVEHYLERLGLAHKVQfvdgrLSTTALSQGQRKRLALLLLMMED 472
Cdd:cd03225 78 GLVFqnPDDQFFGPTVEEevafGLENLGLpeeeiEERVEEALELVGLEGLRD-----RSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFyHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQ 531
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
323-540 |
6.50e-39 |
|
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: 142.09 E-value: 6.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDdfAFQlgPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:COG1122 1 IELENLSFSYPGGTP--ALD--DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIF--ADFYLFADVLGE----GGQHDGL-----EARVEHYLERLGLAHKVQFvdgrlSTTALSQGQRKRLALL-LLMM 470
Cdd:COG1122 77 VGLVFqnPDDQLFAPTVEEdvafGPENLGLpreeiRERVEEALELVGLEHLADR-----PPHELSGGQKQRVAIAgVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 471 EDrEVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHYDHATE 540
Cdd:COG1122 152 EP-EVLVLDEPTAGLDPRGRRELL-ELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
323-531 |
3.92e-38 |
|
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: 137.90 E-value: 3.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:cd03228 1 IEFKNVSFSYPGRP---KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGEGGqhdglearvehylerlglahkvqfvdgrlsttaLSQGQRKRLALLLLMMEDREVFLLDEWA 482
Cdd:cd03228 78 IAYVPQDPFLFSGTIRENI---------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2733243359 483 ADQDPVFRHVFYHELLPELKaaGKTVIAITHDDRYFDVADRIYRLDYGQ 531
Cdd:cd03228 125 SALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
323-532 |
3.48e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.70 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDdfafqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:COG4619 1 LELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGE-------GGQHDGLEARVEHYLERLGLAHKVqfvdgrLSTTA--LSQGQRKRLALLLLMMEDR 473
Cdd:COG4619 76 VAYVPQEPALWGGTVRDnlpfpfqLRERKFDRERALELLERLGLPPDI------LDKPVerLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 474 EVFLLDEWAADQDPV-FRHVfyHELLPEL-KAAGKTVIAITHDDRYFD-VADRIYRLDYGQL 532
Cdd:COG4619 150 DVLLLDEPTSALDPEnTRRV--EELLREYlAEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
343-483 |
8.50e-32 |
|
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: 119.67 E-value: 8.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLF-----ADVL 417
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFprltvRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 418 GEGGQHDGL-----EARVEHYLERLGLAHKV-QFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAA 483
Cdd:pfam00005 81 RLGLLLKGLskrekDARAEEALEKLGLGDLAdRPVGERPGT--LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
323-532 |
2.76e-30 |
|
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: 116.34 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQS--DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdGRTSEWHR 400
Cdd:cd03230 1 IEVRNLSKRYGKKTalDD-------ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAIFADFYLFADVlgeggqhdgleaRVEHYLErlglahkvqfvdgrlsttaLSQGQRKRLALLLLMMEDREVFLLDE 480
Cdd:cd03230 73 RRIGYLPEEPSLYENL------------TVRENLK-------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 481 WAADQDPVFRHVFyHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQL 532
Cdd:cd03230 122 PTSGLDPESRREF-WELLRELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
323-533 |
1.96e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.93 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQsddFAfqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWhREH 402
Cdd:COG1131 1 IEVRGLTKRYGDK---TA--LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGE----------GGQHDGLEARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKRLALLLLMMED 472
Cdd:COG1131 75 IGYVPQEPALYPDLTVRenlrffarlyGLPRKEARERIDELLELFGLTD---AADRKVGT--LSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHddrYFD----VADRIYRLDYGQLV 533
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELW-ELLRELAAEGKTVLLSTH---YLEeaerLCDRVAIIDKGRIV 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
323-532 |
3.29e-29 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 114.89 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL----DGRTSEW 398
Cdd:cd03255 1 IELKNLSKTYGGGGEKV-QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 HREHFAAIFADFYLFAD----------VLGEGGQHDGLEARVEHYLERLGLAHKV-QFVDgrlsttALSQGQRKRLALLL 467
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDltalenvelpLLLAGVPKKERRERAEELLERVGLGDRLnHYPS------ELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 468 LMMEDREVFLLDEWAADQDPVFRHVFyHELLPEL-KAAGKTVIAITHDDRYFDVADRIYRLDYGQL 532
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEV-MELLRELnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
293-533 |
3.87e-28 |
|
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: 118.32 E-value: 3.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 293 HVALQAIDALA-----LGESVTFTEPEQAAAPFR---ELRLSNVHYRYPGqsDDFAfqLGPIDLSIRRGELIFVVGGNGS 364
Cdd:COG4988 299 HARANGIAAAEkifalLDAPEPAAPAGTAPLPAAgppSIELEDVSFSYPG--GRPA--LDGLSLTIPPGERVALVGPSGA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 365 GKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGE---GGQHDGLEARVEHYLERLGLAH 441
Cdd:COG4988 375 GKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREnlrLGRPDASDEELEAALEAAGLDE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 442 KVQFVDGRLST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLpELkAAGKTVIAITHDD 515
Cdd:COG4988 455 FVAALPDGLDTplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALR-RL-AKGRTVILITHRL 532
|
250
....*....|....*...
gi 2733243359 516 RYFDVADRIYRLDYGQLV 533
Cdd:COG4988 533 ALLAQADRILVLDDGRIV 550
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
323-533 |
4.44e-28 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 112.21 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQS--DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHR 400
Cdd:cd03261 1 IELRGLTKSFGGRTvlKG-------VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EH---------FAAIFADFYLFADV---LGEGGQ--HDGLEARVEHYLERLGLAHKVQfvdgrLSTTALSQGQRKRLALL 466
Cdd:cd03261 74 RLrrrmgmlfqSGALFDSLTVFENVafpLREHTRlsEEEIREIVLEKLEAVGLRGAED-----LYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2733243359 467 LLMMEDREVFLLDEWAADQDPVFRHVFyHELLPELKAA-GKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVI-DDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
324-531 |
6.22e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 109.26 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 324 RLSNVHYRYPGQsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHF 403
Cdd:cd00267 1 EIENLSFRYGGR-----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 404 AAIFadfylfadvlgeggQhdglearvehylerlglahkvqfvdgrlsttaLSQGQRKRLALLLLMMEDREVFLLDEWAA 483
Cdd:cd00267 76 GYVP--------------Q--------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2733243359 484 DQDPVFRHvFYHELLPELKAAGKTVIAITHDDRYFD-VADRIYRLDYGQ 531
Cdd:cd00267 110 GLDPASRE-RLLELLRELAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
323-525 |
1.87e-27 |
|
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: 109.87 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGqsDDFAFQ-LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGrtsewHRE 401
Cdd:cd03293 1 LEVRNVSKTYGG--GGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 HFAAIFADFYLFA--DVLG--------EGGQHDGLEARVEHYLERLGLAHkvqFVDGRlsTTALSQGQRKRLALLLLMME 471
Cdd:cd03293 74 DRGYVFQQDALLPwlTVLDnvalglelQGVPKAEARERAEELLELVGLSG---FENAY--PHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 472 DREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIY 525
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDiDEAVFLADRVV 203
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
63-533 |
2.40e-27 |
|
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: 115.97 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISLYNGLLLLTGL-AY 141
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLfIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 142 MAWLSvpfFVLTLGVIALGVGLDILL---GRKIKALMRAVRQRDDQLTEQFEAAIDGRCEL----GLSRERRhllyrhRL 214
Cdd:TIGR02203 149 LLYYS---WQLTLIVVVMLPVLSILMrrvSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVklfgGQAYETR------RF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 215 EPVASASLAASVRADTLWAVNLNWTTLLVFVLIGTLFFLGQGLGLLDQQVV---VGYVLAIMFLRTPISVILDAVPAVIR 291
Cdd:TIGR02203 220 DAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAgdfTAFITAMIALIRPLKSLTNVNAPMQR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 292 GHVALQAIDALalgesvTFTEPEQAA---APFR---ELRLSNVHYRYPGQSDDfafQLGPIDLSIRRGELIFVVGGNGSG 365
Cdd:TIGR02203 300 GLAAAESLFTL------LDSPPEKDTgtrAIERargDVEFRNVTFRYPGRDRP---ALDSISLVIEPGETVALVGRSGSG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 366 KSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVL------GEGGQHDglEARVEHYLErlgL 439
Cdd:TIGR02203 371 KSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIanniayGRTEQAD--RAEIERALA---A 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 440 AHKVQFVDGR---LST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQD-PVFRHVfyHELLPELKaAGKTVI 509
Cdd:TIGR02203 446 AYAQDFVDKLplgLDTpigengVLLSGGQRQRLAIARALLKDAPILILDEATSALDnESERLV--QAALERLM-QGRTTL 522
|
490 500
....*....|....*....|....
gi 2733243359 510 AITHDDRYFDVADRIYRLDYGQLV 533
Cdd:TIGR02203 523 VIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-540 |
2.45e-27 |
|
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: 110.33 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWhREH 402
Cdd:COG4555 2 IEVENLSKKYGKV-----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFA--------DVLGE--GGQHDGLEARVEHYLERLGLahkVQFVDGRLSTtaLSQGQRKRLALLLLMMED 472
Cdd:COG4555 76 IGVLPDERGLYDrltvreniRYFAElyGLFDEELKKRIEELIELLGL---EEFLDRRVGE--LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFyHELLPELKAAGKTVIAITHDdrYFDVA---DRIYRLDYGQLVHYDHATE 540
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLL-REILRALKKEGKTVLFSSHI--MQEVEalcDRVVILHKGKVVAQGSLDE 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
323-534 |
5.04e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.98 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYP-GQSDDFAfqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL----DGRTSE 397
Cdd:COG1136 5 LELRNLTKSYGtGEGEVTA--LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 398 WHREHFAAIFADFYLFAD----------VLGEGGQHDGLEARVEHYLERLGLAHKVQFvdgrlSTTALSQGQRKRLALLL 467
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPEltalenvalpLLLAGVSRKERRERARELLERVGLGDRLDH-----RPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 468 LMMEDREVFLLDEWAADQDPVFRHVFyHELLPEL-KAAGKTVIAITHDDRYFDVADRIYRLDYGQLVH 534
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEV-LELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
343-528 |
1.67e-26 |
|
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: 106.79 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE-----HFAAIFADF------Y 411
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRlaylgHADGLKPELtvrenlR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 412 LFADVLGEGGQhdglEARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRH 491
Cdd:COG4133 98 FWAALYGLRAD----REAIDEALEAVGLAG---LADLPVRQ--LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2733243359 492 VFyHELLPELKAAGKTVIAITHDDRYFDvADRIYRLD 528
Cdd:COG4133 169 LL-AELIAAHLARGGAVLLTTHQPLELA-AARVLDLG 203
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-534 |
2.08e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.87 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRtseWHR-- 400
Cdd:COG1121 7 IELENLTVSYGGRP-----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 --EHFAAIFADFYLFA-DVLGEG-----------GQHDglEARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKRLALL 466
Cdd:COG1121 79 yvPQRAEVDWDFPITVrDVVLMGrygrrglfrrpSRAD--REAVDEALERVGLED---LADRPIGE--LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 467 LLMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD----DRYFdvaDRIYRLDYGQLVH 534
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALY-ELLRELRREGKTILVVTHDlgavREYF---DRVLLLNRGLVAH 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
346-533 |
4.32e-26 |
|
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: 106.75 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRtsewhREH----------F--AAIFADFYLF 413
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-----PPHeiarlgigrtFqiPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 414 ADVL--------------GEGGQHDGLEARVEHYLERLGLAHkvqfvdgRLSTTA--LSQGQRKRLALLLLMMEDREVFL 477
Cdd:cd03219 94 ENVMvaaqartgsglllaRARREEREARERAEELLERVGLAD-------LADRPAgeLSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 478 LDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:cd03219 167 LDEPAAGLNPEETEELA-ELIRELRERGITVLLVEHDmDVVMSLADRVTVLDQGRVI 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
83-514 |
2.57e-25 |
|
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: 109.76 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 83 LRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQ--LPIslynGLLLLTGLAY---MAWLSVPFfVLTLGVI 157
Cdd:TIGR02868 88 LRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRviVPA----GVALVVGAAAvaaIAVLSVPA-ALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 158 AL--GVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDGRCEL---GLSRErrhllYRHRLEPVASASLAASVRADTLW 232
Cdd:TIGR02868 163 LLlaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELvasGALPA-----ALAQVEEADRELTRAERRAAAAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 233 AVNLNWTTLLV-FVLIGTLFFLGQGL--GLLDQQVVVGYVLAIMFLRTPISVILDAVPAVIRGHVALQAIDAL--ALGES 307
Cdd:TIGR02868 238 ALGAALTLLAAgLAVLGALWAGGPAVadGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVldAAGPV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 308 VTFTEPEQAAAPFRE--LRLSNVHYRYPGQSDdfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVS 385
Cdd:TIGR02868 318 AEGSAPAAGAVGLGKptLELRDLSAGYPGAPP----VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 386 LNGVPLDGRTSEWHREHFAAIFADFYLFADVLGEG---GQHDGLEARVEHYLERLGLAHKVQFVDGRLST------TALS 456
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlrlARPDATDEELWAALERVGLADWLRALPDGLDTvlgeggARLS 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 457 QGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRhvfyHELLPELKAA--GKTVIAITHD 514
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETA----DELLEDLLAAlsGRTVVLITHH 529
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
323-533 |
4.36e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 104.43 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDdfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGvpLDGRTSE--WH- 399
Cdd:TIGR04520 1 IEVENVSFSYPESEK---PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEEnlWEi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REH----F--------AAIFADfylfaDV------LGEggQHDGLEARVEHYLERLGLAHKVQFvdgrlSTTALSQGQRK 461
Cdd:TIGR04520 76 RKKvgmvFqnpdnqfvGATVED-----DVafglenLGV--PREEMRKRVDEALKLVGMEDFRDR-----EPHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2733243359 462 RLAL--LLLMMEDreVFLLDEWAADQDPVFRH-VFyhELLPELKA-AGKTVIAITHD-DryfDV--ADRIYRLDYGQLV 533
Cdd:TIGR04520 144 RVAIagVLAMRPD--IIILDEATSMLDPKGRKeVL--ETIRKLNKeEGITVISITHDmE---EAvlADRVIVMNKGKIV 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
264-533 |
6.10e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.45 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 264 VVVGYVLAIMFLRTPISVILDAVPAVIRGHVALQAIDALALGESVTfTEPEQAAAPFreLRLSNVHYRYPGQSDDFAFQL 343
Cdd:COG1123 205 VVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRA-APAAAAAEPL--LEVRNLSKRYPVRGKGGVRAV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 344 GPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSE---WHREHFAAIFADFY--LF----- 413
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDPYssLNprmtv 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 414 ADVLGEGGQHDGL------EARVEHYLERLGLAHKVqfvdGRLSTTALSQGQRKRLAL---LLLmmeDREVFLLDEWAAD 484
Cdd:COG1123 362 GDIIAEPLRLHGLlsraerRERVAELLERVGLPPDL----ADRYPHELSGGQRQRVAIaraLAL---EPKLLILDEPTSA 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 485 QDP-VFRHVFyhELLPELKAA-GKTVIAITHD---DRYfdVADRIYRLDYGQLV 533
Cdd:COG1123 435 LDVsVQAQIL--NLLRDLQRElGLTYLFISHDlavVRY--IADRVAVMYDGRIV 484
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-525 |
8.99e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.55 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDF-AfqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEwhre 401
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtA--LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 hFAAIFADFYLF--ADVLG--------EGGQHDGLEARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKRLALLLLMME 471
Cdd:COG1116 82 -RGVVFQEPALLpwLTVLDnvalglelRGVPKAERRERARELLELVGLAG---FEDAYPHQ--LSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 472 DREVFLLDE-WAAdQDPVFRHVFYHELLPELKAAGKTVIAITHddryfDV------ADRIY 525
Cdd:COG1116 156 DPEVLLMDEpFGA-LDALTRERLQDELLRLWQETGKTVLFVTH-----DVdeavflADRVV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
346-533 |
2.64e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 98.90 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVP---LDGRTSEWHREHF------AAIFAD------- 409
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRRIgmlfqgGALFDSltvfenv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 410 -FYLFadvlgeggQHDGL-----EARVEHYLERLGLAHkvqfvDGRLSTTALSQGQRKRLAL---LLLmmeDREVFLLDE 480
Cdd:COG1127 104 aFPLR--------EHTDLseaeiRELVLEKLELVGLPG-----AADKMPSELSGGMRKRVALaraLAL---DPEILLYDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 481 WAADQDPVFRHVFyHELLPELKAA-GKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:COG1127 168 PTAGLDPITSAVI-DELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKII 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
292-527 |
3.21e-23 |
|
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: 103.14 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 292 GHVALQAIDA-LALGESVTFTEPEQAAAPFRELRLSNVHYRYPGQSDdfafQLGPIDLSIRRGELIFVVGGNGSGKSTLA 370
Cdd:TIGR02857 290 GVAAAEALFAvLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP----ALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 371 KLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGEG---GQHDGLEARVEHYLERLGLAHKVQFVD 447
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENirlARPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 448 GRLST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPelKAAGKTVIAITHDDRYFDVA 521
Cdd:TIGR02857 446 QGLDTpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA--LAQGRTVLLVTHRLALAALA 523
|
....*.
gi 2733243359 522 DRIYRL 527
Cdd:TIGR02857 524 DRIVVL 529
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
324-519 |
4.64e-23 |
|
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: 97.22 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 324 RLSNVHYRYPGQ---SDdfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdgrTSEWHR 400
Cdd:cd03235 1 EVEDLTVSYGGHpvlED--------VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL---EKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 ----EHFAAIFADFYLFA-DVLGEGG-QHDGL--------EARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKRLALL 466
Cdd:cd03235 70 igyvPQRRSIDRDFPISVrDVVLMGLyGHKGLfrrlskadKAKVDEALERVGLSE---LADRQIGE--LSGGQQQRVLLA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 467 LLMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD----DRYFD 519
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIY-ELLRELRREGMTILVVTHDlglvLEYFD 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
327-519 |
5.21e-23 |
|
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: 97.09 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 327 NVHYRYPGQSddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVP---LDGRTSEWHREHF 403
Cdd:cd03292 5 NVTKTYPNGT----AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 404 AAIFADFYLFAD------------VLGEGGQHdgLEARVEHYLERLGLAHKVqfvdgRLSTTALSQGQRKRLALLLLMME 471
Cdd:cd03292 81 GVVFQDFRLLPDrnvyenvafaleVTGVPPRE--IRKRVPAALELVGLSHKH-----RALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2733243359 472 DREVFLLDEWAADQDPVF-RHVFyhELLPELKAAGKTVIAITHDDRYFD 519
Cdd:cd03292 154 SPTILIADEPTGNLDPDTtWEIM--NLLKKINKAGTTVVVATHAKELVD 200
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
346-532 |
1.33e-22 |
|
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: 96.06 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH--REHFAAIFADFYLFA--DVLG--- 418
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelRQKVGMVFQQFNLFPhlTVLEnit 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 ------EGGQHDGLEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLLMMEDREVFLLDEWAADQDP-VFRH 491
Cdd:cd03262 99 lapikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSG-----GQQQRVAIARALAMNPKVMLFDEPTSALDPeLVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2733243359 492 VFyhELLPELKAAGKTVIAITHDDRY-FDVADRIYRLDYGQL 532
Cdd:cd03262 174 VL--DVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-540 |
1.87e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.89 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDdfAFQlgPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdGRTSEW---- 398
Cdd:COG2884 2 IRFENVSKRYPGGRE--ALS--DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL-SRLKRReipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 HREHFAAIFADFYLFAD------------VLGEGgqHDGLEARVEHYLERLGLAHKvqfvdGRLSTTALSQGQRKRLALL 466
Cdd:COG2884 77 LRRRIGVVFQDFRLLPDrtvyenvalplrVTGKS--RKEIRRRVREVLDLVGLSDK-----AKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 467 LLMMEDREVFLLDEWAADQDP-----VFRhvfyheLLPELKAAGKTVIAITHDDRYFD-VADRIYRLDYGQLVHYDHATE 540
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPetsweIME------LLEEINRRGTTVLIATHDLELVDrMPKRVLELEDGRLVRDEARGV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-540 |
3.37e-22 |
|
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: 95.88 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdgrtSEWHREH 402
Cdd:COG1120 2 LEAENLSVGYGGR-----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL----ASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFAdfYLF-----------ADV-----------LGEGGQHDglEARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQR 460
Cdd:COG1120 73 LARRIA--YVPqeppapfgltvRELvalgryphlglFGRPSAED--REAVEEALERTGLEH---LADRPVDE--LSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 461 KRLALLLLMMEDREVFLLDEWAADQDPVFRH-VFyhELLPEL-KAAGKTVIAITHD----DRYfdvADRIYRLDYGQLVH 534
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLeVL--ELLRRLaRERGRTVVMVLHDlnlaARY---ADRLVLLKDGRIVA 218
|
....*.
gi 2733243359 535 YDHATE 540
Cdd:COG1120 219 QGPPEE 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
325-536 |
4.47e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 325 LSNVHYRYPGQS--DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG----------VPLD 392
Cdd:COG0488 1 LENLSKSFGGRPllDD-------VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqePPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 393 GRTS-----------------EWHR--EHFAAIFADFYLFADVLGEGGQHDG--LEARVEHYLERLGLAHkvqfVDGRLS 451
Cdd:COG0488 74 DDLTvldtvldgdaelraleaELEEleAKLAEPDEDLERLAELQEEFEALGGweAEARAEEILSGLGFPE----EDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 452 TTALSQGQRKRLALLLLMMEDREVFLLDE-----------WAADqdpvfrhvfyhellpELKAAGKTVIAITHDdRYF-- 518
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEptnhldlesieWLEE---------------FLKNYPGTVLVVSHD-RYFld 213
|
250
....*....|....*...
gi 2733243359 519 DVADRIYRLDYGQLVHYD 536
Cdd:COG0488 214 RVATRILELDRGKLTLYP 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
78-533 |
6.62e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.51 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 78 RLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISLYNGLLLLTGLAY-MAWLSVPFfVLTLGV 156
Cdd:PRK11160 90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIgLSFFDLTL-ALTLGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 157 IALGVGLDI-----LLGRKI-KALMRAVRQRDDQLTEqfeaAIDGRCELGL-SRERRhllYRHRLEPVASASLAASVRAD 229
Cdd:PRK11160 169 ILLLLLLLLpllfyRLGKKPgQDLTHLRAQYRVQLTE----WLQGQAELTLfGAEDR---YRQQLEQTEQQWLAAQRRQA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 230 TLWAVNlnwTTLLVFV----LIGTLFFLGQGLGlldQQVVVGYVLAIMFLRTPISV-ILDAVPAVIR--GHVALQA--ID 300
Cdd:PRK11160 242 NLTGLS---QALMILAngltVVLMLWLAAGGVG---GNAQPGALIALFVFAALAAFeALMPVAGAFQhlGQVIASArrIN 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 301 ALALGE-SVTFTEPEQAAAPFRELRLSNVHYRYPGQSDDFafqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQP 379
Cdd:PRK11160 316 EITEQKpEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPV---LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 380 SAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGEG---GQHDGLEARVEHYLERLGLAHKVQFVDGrLST---- 452
Cdd:PRK11160 393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNlllAAPNASDEALIEVLQQVGLEKLLEDDKG-LNAwlge 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 453 --TALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVF-RHVFyhELLPELkAAGKTVIAITHDDRYFDVADRIYRLDY 529
Cdd:PRK11160 472 ggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQIL--ELLAEH-AQNKTVLMITHRLTGLEQFDRICVMDN 548
|
....
gi 2733243359 530 GQLV 533
Cdd:PRK11160 549 GQII 552
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
324-535 |
6.89e-22 |
|
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: 92.88 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 324 RLSNVHYRYPGQsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdgrtSEWHREHF 403
Cdd:cd03214 1 EVENLSVGYGGR-----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----ASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 404 AAIFAdfYlfadvlgeggqhdglearVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAA 483
Cdd:cd03214 72 ARKIA--Y------------------VPQALELLGLAH---LADRPFNE--LSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 484 DQDpvFRHVfyHELLPELKA----AGKTVIAITHD-DRYFDVADRIYRLDYGQLVHY 535
Cdd:cd03214 127 HLD--IAHQ--IELLELLRRlareRGKTVVMVLHDlNLAARYADRVILLKDGRIVAQ 179
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
322-533 |
7.13e-22 |
|
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: 94.19 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYPGQSDDfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdgrtSEWH-- 399
Cdd:cd03245 2 RIEFRNVSFSYPNQEIP---ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI----RQLDpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 --REHFAAIFADFYLFADVLGEG---GQHDGLEARVEHYLERLGLAhkvQFVD-------------GRlsttALSQGQRK 461
Cdd:cd03245 75 dlRRNIGYVPQDVTLFYGTLRDNitlGAPLADDERILRAAELAGVT---DFVNkhpngldlqigerGR----GLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 462 RLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELkaAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
323-532 |
7.17e-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: 92.66 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdgrtSEWHREH 402
Cdd:cd03246 1 LEVENVSFRYPGAE---PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI----SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FaaifadfylfadvlgegGQHDGLearvehylerlgLAHKVQFVDGRLSTTALSQGQRKRLALLLLMMEDREVFLLDEWA 482
Cdd:cd03246 74 L-----------------GDHVGY------------LPQDDELFSGSIAENILSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2733243359 483 ADQDPVFRHVFYhELLPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQL 532
Cdd:cd03246 125 SHLDVEGERALN-QAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
322-533 |
8.82e-22 |
|
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: 94.21 E-value: 8.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRY----PGQSDdfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSE 397
Cdd:cd03254 2 EIEFENVNFSYdekkPVLKD--------INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 398 WHREHFAAIFADFYLFADVLGEGGQHDGLEARVEHYLERLGLAHKVQFVDGR---LSTTA------LSQGQRKRLALLLL 468
Cdd:cd03254 74 SLRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpngYDTVLgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 469 MMEDREVFLLDEWAADQDPVFRHVFYHELLPELKaaGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-533 |
9.68e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 94.48 E-value: 9.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPV-LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYL-------FADVLGEGGQHDGL---EARVEHYLERLGLAHKVQFvdgRLStTALSQGQRKRLALLLLMMED 472
Cdd:COG1124 81 VQMVFQDPYAslhprhtVDRILAEPLRIHGLpdrEERIAELLEQVGLPPSFLD---RYP-HQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 473 REVFLLDEWAADQDPVFR-HVFyhELLPELKAA-GKTVIAITHDDRYFD-VADRIYRLDYGQLV 533
Cdd:COG1124 157 PELLLLDEPTSALDVSVQaEIL--NLLKDLREErGLTYLFVSHDLAVVAhLCDRVAVMQNGRIV 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
323-531 |
1.05e-21 |
|
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: 92.25 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGqsddfAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLD--GRTSEWHR 400
Cdd:cd03229 1 LELKNVSKRYGQ-----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAIFADFYLFadvlgeggQHdgLEARvehylERLGLahkvqfvdgrlsttALSQGQRKRLALLLLMMEDREVFLLDE 480
Cdd:cd03229 76 RRIGMVFQDFALF--------PH--LTVL-----ENIAL--------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 481 WAADQDPVFRHVFyHELLPELKA-AGKTVIAITHD-DRYFDVADRIYRLDYGQ 531
Cdd:cd03229 127 PTSALDPITRREV-RALLKSLQAqLGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
323-533 |
1.50e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 92.97 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSewHREH 402
Cdd:cd03259 1 LELKGLSKTYGSV-----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP--ERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLF-----ADVLGEGGQHDGL-----EARVEHYLERLGLAHkvqfvDGRLSTTALSQGQRKRLALLLLMMED 472
Cdd:cd03259 74 IGMVFQDYALFphltvAENIAFGLKLRGVpkaeiRARVRELLELVGLEG-----LLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGRIV 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
323-533 |
1.88e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPgqsdDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH--R 400
Cdd:PRK13636 6 LKVEELNYNYS----DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMklR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAIF--ADFYLFA---------DVLGEGGQHDGLEARVEHYLERLGLAHKVQfvdgrLSTTALSQGQRKRLALLLLM 469
Cdd:PRK13636 82 ESVGMVFqdPDNQLFSasvyqdvsfGAVNLKLPEDEVRKRVDNALKRTGIEHLKD-----KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 470 MEDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVI 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
323-534 |
2.29e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 92.26 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfafQLGPIDLSIRRGeLIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHR-- 400
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRri 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 ----------EHFAAIfaDFYLFADVLGeGGQHDGLEARVEHYLERLGLAhkvQFVDGRLSttALSQGQRKRLALLLLMM 470
Cdd:cd03264 75 gylpqefgvyPNFTVR--EFLDYIAWLK-GIPSKEVKARVDEVLELVNLG---DRAKKKIG--SLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 471 EDREVFLLDEWAADQDPVFRHVFyHELLPELkAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVH 534
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRF-RNLLSEL-GEDRIVILSTHIvEDVESLCNQVAVLNKGKLVF 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-533 |
4.33e-21 |
|
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: 90.18 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfAfqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSewhreh 402
Cdd:cd03216 1 LELRGITKRFGGVK---A--LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 faaifadfylfadvlgeggqhdgLEARvehyleRLGLAHKVQfvdgrlsttaLSQGQRKRLALLLLMMEDREVFLLDEWA 482
Cdd:cd03216 70 -----------------------RDAR------RAGIAMVYQ----------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 483 A--DQDPVfRHVFyhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:cd03216 111 AalTPAEV-ERLF--KVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
323-533 |
4.71e-21 |
|
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: 90.45 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFafqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWhREH 402
Cdd:cd03247 1 LSINNVSFSYPEQEQQV---LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-SSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLgeggqhdglearvehyLERLGlahkvqfvdgrlstTALSQGQRKRLALLLLMMEDREVFLLDEWA 482
Cdd:cd03247 77 ISVLNQRPYLFDTTL----------------RNNLG--------------RRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 483 ADQDPVFRHVFYHELLPELKaaGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-533 |
5.90e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDdfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSeWH-RE 401
Cdd:PRK13635 6 IRVEHISFRYPDAAT---YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETV-WDvRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 HFAAIF------------ADFYLFAdVLGEGGQHDGLEARVEHYLERLGLAhkvQFVDGRLSTtaLSQGQRKRLALLLLM 469
Cdd:PRK13635 82 QVGMVFqnpdnqfvgatvQDDVAFG-LENIGVPREEMVERVDQALRQVGME---DFLNREPHR--LSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 470 MEDREVFLLDEWAADQDPVFRhvfyHELLP---ELKAAGK-TVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGR----REVLEtvrQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-533 |
1.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.59 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 325 LSNVHYRYPgqsDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFA 404
Cdd:PRK13632 10 VENVSFSYP---NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 405 AIFAD----FylfadvLGEGGQHD---GLEAR----------VEHYLERLG----LAHKVQFvdgrlsttaLSQGQRKRL 463
Cdd:PRK13632 87 IIFQNpdnqF------IGATVEDDiafGLENKkvppkkmkdiIDDLAKKVGmedyLDKEPQN---------LSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 464 ALLLLMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKAAG-KTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIK-KIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
323-533 |
1.94e-20 |
|
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: 90.37 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGqsdDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:cd03251 1 VEFKNVTFRYPG---DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGEG---GQHDGLEARVEHYLErlgLAHKVQFVDGR---LST------TALSQGQRKRLALLLLMM 470
Cdd:cd03251 78 IGLVSQDVFLFNDTVAENiayGRPGATREEVEEAAR---AANAHEFIMELpegYDTvigergVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 471 EDREVFLLDEWAADQDPVFRHVFyHELLPELkAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:cd03251 155 KDPPILILDEATSALDTESERLV-QAALERL-MKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
346-535 |
2.66e-20 |
|
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: 89.26 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDgrtsEWHREHFAAIFADFYLF-----ADVLGEG 420
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEERGLYpkmkvIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 GQHDGL---EAR--VEHYLERLGLAHKvqfVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYH 495
Cdd:cd03269 95 AQLKGLkkeEARrrIDEWLERLELSEY---ANKRVEE--LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2733243359 496 ELLpELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHY 535
Cdd:cd03269 170 VIR-ELARAGKTVILSTHQmELVEELCDRVLLLNKGRAVLY 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-533 |
3.54e-20 |
|
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: 93.81 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSA---GTVSLNGVPLDGRTSEWH 399
Cdd:COG1123 5 LEVRDLSVRYPGGDVP---AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REHFAAIFADFYL----------FADVLGEGGQ-HDGLEARVEHYLERLGLAHKVqfvdgRLSTTALSQGQRKRLALLLL 468
Cdd:COG1123 82 GRRIGMVFQDPMTqlnpvtvgdqIAEALENLGLsRAEARARVLELLEAVGLERRL-----DRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 469 MMEDREVFLLDEWAADQDPVFRHVFYhELLPEL-KAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEIL-DLLRELqRERGTTVLLITHDlGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
346-540 |
1.11e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 88.85 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGElIFVVGG-NGSGKSTLAKLMTGLYQPSAGTVSLNGVPL----DGRTSEWHREHFAAIFADFYLFA------ 414
Cdd:cd03294 43 VSLDVREGE-IFVIMGlSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRKKISMVFQSFALLPhrtvle 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 415 ------DVLGEGGQHDglEARVEHYLERLGL-AHKVQFVDgrlsttALSQGQRKRLALLLLMMEDREVFLLDEWAADQDP 487
Cdd:cd03294 122 nvafglEVQGVPRAER--EERAAEALELVGLeGWEHKYPD------ELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 488 VFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHYDHATE 540
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-540 |
1.52e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.89 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPgqsdDFAFQlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSewHREH 402
Cdd:COG3840 2 LRLDDLTYRYG----DFPLR---FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFA--DV-----LgegGQHDGL------EARVEHYLERLGLAHKVQfvdgRLStTALSQGQRKRLALLLLM 469
Cdd:COG3840 73 VSMLFQENNLFPhlTVaqnigL---GLRPGLkltaeqRAQVEQALERVGLAGLLD----RLP-GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 470 MEDREVFLLDEWAADQDPVFRHVFYHeLLPEL-KAAGKTVIAITHD-DRYFDVADRIYRLDYGQlVHYDHATE 540
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLD-LVDELcRERGLTVLMVTHDpEDAARIADRVLLVADGR-IAADGPTA 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
323-533 |
2.57e-19 |
|
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: 86.39 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFafqlgpiDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVplDGRTSEWHREH 402
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF-------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV--DVTAAPPADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGEggQHDGL------------EARVEHYLERLGLAHKvqfvDGRLSTTaLSQGQRKRLALLLLMM 470
Cdd:cd03298 72 VSMLFQENNLFAHLTVE--QNVGLglspglkltaedRQAIEVALARVGLAGL----EKRLPGE-LSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 471 EDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-533 |
9.44e-19 |
|
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: 85.25 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG---VPLDGRTSEWH 399
Cdd:cd03257 2 LEVKNLSVSFPTGGGSV-KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REHFAAIFADFY-----------LFADVLGEGGQHDGLEAR---VEHYLERLGLAHKVQfvdGRLStTALSQGQRKRLAL 465
Cdd:cd03257 81 RKEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARkeaVLLLLVGVGLPEEVL---NRYP-HELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 466 LLLMMEDREVFLLDEWAADQDPVFRhVFYHELLPELKAA-GKTVIAITHDdryFDV----ADRIYRLDYGQLV 533
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQ-AQILDLLKKLQEElGLTLLFITHD---LGVvakiADRVAVMYAGKIV 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
323-536 |
1.18e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQS--DDFafqlgpiDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLngvpldGRTSEW-- 398
Cdd:COG0488 316 LELEGLSKSYGDKTllDDL-------SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIgy 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 ---HREHFAA---IFadfylfaDVLGEGGQhDGLEARVEHYLERLGLAHKVQFVdgrlSTTALSQGQRKRLALLLLMMED 472
Cdd:COG0488 383 fdqHQEELDPdktVL-------DELRDGAP-GGTEQEVRGYLGRFLFSGDDAFK----PVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 473 REVFLLDEWAADQDPVFRhvfyhELLPE-LKAAGKTVIAITHdDRYF--DVADRIYRLDYGQLVHYD 536
Cdd:COG0488 451 PNVLLLDEPTNHLDIETL-----EALEEaLDDFPGTVLLVSH-DRYFldRVATRILEFEDGGVREYP 511
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
323-536 |
1.68e-18 |
|
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: 85.04 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPldgrTSEWH--- 399
Cdd:cd03295 1 IEFENVTKRYGGGK----KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED----IREQDpve 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 -REHFAAIFADFYLF---------ADVLG-EGGQHDGLEARVEHYLERLGLAHKvQFVDgRLSTTaLSQGQRKRLALLLL 468
Cdd:cd03295 73 lRRKIGYVIQQIGLFphmtveeniALVPKlLKWPKEKIRERADELLALVGLDPA-EFAD-RYPHE-LSGGQQQRVGVARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2733243359 469 MMEDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHYD 536
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQVG 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
240-533 |
2.90e-18 |
|
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: 88.26 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 240 TLLVFVL-IGTLFflgqglgLLDQQVVVGYVLA----IMFLRTPISVILDAVPAVIRGHVALQAIDALALGESvTFTEPE 314
Cdd:TIGR01193 391 ILNVVILwTGAYL-------VMRGKLTLGQLITfnalLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDS-EFINKK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 315 QAAA---PFRELRLSNVHYRYpGQSDDFafqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL 391
Cdd:TIGR01193 463 KRTElnnLNGDIVINDVSYSY-GYGSNI---LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 392 DGRTSEWHREHFAAIFADFYLFAD------VLG--EGGQHDGLEARVEHYLERLGLAHKVQFVDGRLST--TALSQGQRK 461
Cdd:TIGR01193 539 KDIDRHTLRQFINYLPQEPYIFSGsilenlLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEegSSISGGQKQ 618
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 462 RLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPelkAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN---LQDKTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
346-519 |
6.61e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGE------ 419
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRqvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 420 --------GGQHDGLEARVEHYLERLGLAhkvQFVDgrLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDpVFRH 491
Cdd:PRK09536 102 rtphrsrfDTWTETDRAAVERAMERTGVA---QFAD--RPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-INHQ 175
|
170 180 190
....*....|....*....|....*....|..
gi 2733243359 492 VFYHELLPELKAAGKTVIAITHD----DRYFD 519
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIHDldlaARYCD 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
346-536 |
7.47e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.58 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG--VPLDGRTSEWH-----REhfaaifaDFYLFADVLG 418
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGGGFNpeltgRE-------NIYLNGRLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 -EGGQHDGLEARVEHYLErLGlahkvQFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYhEL 497
Cdd:cd03220 114 lSRKEIDEKIDEIIEFSE-LG-----DFIDLPVKT--YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ-RR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2733243359 498 LPELKAAGKTVIAITHDDRYF-DVADRIYRLDYGQLVHYD 536
Cdd:cd03220 185 LRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
323-536 |
7.67e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.11 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRY-PGQSddfaFQ---LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEW 398
Cdd:PRK13641 3 IKFENVDYIYsPGTP----MEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 H----REHFAAIF--ADFYLFADVLGE---------GGQHDGLEARVEHYLERLGLAHKVQfvdgRLSTTALSQGQRKRL 463
Cdd:PRK13641 79 NlkklRKKVSLVFqfPEAQLFENTVLKdvefgpknfGFSEDEAKEKALKWLKKVGLSEDLI----SKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 464 ALLLLMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHYD 536
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMM-QLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLIKHA 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-539 |
1.03e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.89 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 312 EPEQAAAPFRELRlsNVHYRYPGQS--DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGV 389
Cdd:PRK11607 11 KTRKALTPLLEIR--NLTKSFDGQHavDD-------VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 390 PLdGRTSEWHREhFAAIFADFYLFADVLGE-----GGQHDGL-----EARVEhylERLGLAHKVQFvdGRLSTTALSQGQ 459
Cdd:PRK11607 82 DL-SHVPPYQRP-INMMFQSYALFPHMTVEqniafGLKQDKLpkaeiASRVN---EMLGLVHMQEF--AKRKPHQLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 460 RKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVH---- 534
Cdd:PRK11607 155 RQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQigep 234
|
....*...
gi 2733243359 535 ---YDHAT 539
Cdd:PRK11607 235 eeiYEHPT 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
327-535 |
1.56e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.86 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 327 NVHYRYPgqsdDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAI 406
Cdd:PRK13647 9 DLHFRYK----DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 407 FAD-------FYLFADV----LGEGGQHDGLEARVEHYLERLG---LAHKVQFvdgrlsttALSQGQRKRLALLLLMMED 472
Cdd:PRK13647 85 FQDpddqvfsSTVWDDVafgpVNMGLDKDEVERRVEEALKAVRmwdFRDKPPY--------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHY 535
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGRVLAE 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
323-534 |
1.59e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG---VPLDGRT-SEW 398
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEV-LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvATLDADAlAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 HREHFAAIFADFYLFADVLGE----------GGQHDGLEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLL 468
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAqnvevpavyaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSG-----GQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 469 MMEDREVFLLDEWAADQDpvfRH--VFYHELLPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLVH 534
Cdd:PRK10535 159 LMNGGQVILADEPTGALD---SHsgEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-535 |
2.13e-17 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 81.47 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAfQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGV---PLDGRTSEWH 399
Cdd:cd03258 2 IELKNVSKVFGDTGGKVT-ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REHFAAIFADFYLFA--DVLG--------EGGQHDGLEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLLM 469
Cdd:cd03258 81 RRRIGMIFQHFNLLSsrTVFEnvalpleiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSG-----GQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 470 MEDREVFLLDEWAADQDPVFRHVFYhELLPEL-KAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHY 535
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSIL-ALLRDInRELGLTIVLITHEmEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-540 |
2.84e-17 |
|
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: 81.46 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDdfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVP---LDGRTSEWH 399
Cdd:cd03256 1 IEVENLSKTYPNGKK----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REHFAAIFADFYL------FADVL-GEGGQH-------------DGLEARveHYLERLGLAHKV-QFVDgrlsttALSQG 458
Cdd:cd03256 77 RRQIGMIFQQFNLierlsvLENVLsGRLGRRstwrslfglfpkeEKQRAL--AALERVGLLDKAyQRAD------QLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 459 QRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHDDRYF-DVADRIYRLDYGQLVhYDH 537
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRIV-FDG 227
|
...
gi 2733243359 538 ATE 540
Cdd:cd03256 228 PPA 230
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
318-535 |
2.94e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 84.71 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 318 APFRELRLSNVHYRYPGQSDDfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDgrtsE 397
Cdd:TIGR01842 312 EPEGHLSVENVTIVPPGGKKP---TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----Q 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 398 WHREHFAAIFA----DFYLFADVLGEGGQHDGLEARVEHYLE--RLGLAHKV--QFVDGRLST-----TALSQGQRKRLA 464
Cdd:TIGR01842 385 WDRETFGKHIGylpqDVELFPGTVAENIARFGENADPEKIIEaaKLAGVHELilRLPDGYDTVigpggATLSGGQRQRIA 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 465 LLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLpELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLVHY 535
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIK-ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
323-514 |
4.45e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.34 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYpgQSDDfAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:PRK13648 8 IVFKNVSFQY--QSDA-SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFAD--------FYLFADVLGEGGQ---HDGLEARVEHYLERLGLAHKVQFvdgrlSTTALSQGQRKRLALLLLMME 471
Cdd:PRK13648 85 IGIVFQNpdnqfvgsIVKYDVAFGLENHavpYDEMHRRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2733243359 472 DREVFLLDEWAADQDPVFRHVFYhELLPELKAAGK-TVIAITHD 514
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLL-DLVRKVKSEHNiTIISITHD 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
323-535 |
5.84e-17 |
|
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: 79.86 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQS----DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEW 398
Cdd:cd03263 1 LQIRNLTKTYKKGTkpavDD-------LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 HRE-----HFAAIFADF------YLFADVlgEGGQHDGLEARVEHYLERLGLAHKVQfvdgRLSTTaLSQGQRKRLALLL 467
Cdd:cd03263 74 RQSlgycpQFDALFDELtvrehlRFYARL--KGLPKSEIKEEVELLLRVLGLTDKAN----KRART-LSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 468 LMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKaAGKTVIAITHD----DRyfdVADRIYRLDYGQLVHY 535
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIW-DLILEVR-KGRSIILTTHSmdeaEA---LCDRIAIMSDGKLRCI 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
325-533 |
6.63e-17 |
|
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: 80.22 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 325 LSNVHYRYPGqsdDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFA 404
Cdd:cd03252 3 FEHVRFRYKP---DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 405 AIFADFYLFADVLGE--GGQHDGLEARVEHYLERLGLAHKV---------QFVDGRlsTTALSQGQRKRLALLLLMMEDR 473
Cdd:cd03252 80 VVLQENVLFNRSIRDniALADPGMSMERVIEAAKLAGAHDFiselpegydTIVGEQ--GAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 474 EVFLLDEWAADQDPVFRHVF---YHELLpelkaAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:cd03252 158 RILIFDEATSALDYESEHAImrnMHDIC-----AGRTVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
327-533 |
7.23e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.90 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 327 NVHYRY-PGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH-REHFA 404
Cdd:PRK13633 9 NVSYKYeSNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDiRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 405 AIF--ADFYLFADVLGE---------GGQHDGLEARVEHYLERLGLahkvqFVDGRLSTTALSQGQRKRLAL--LLLMME 471
Cdd:PRK13633 89 MVFqnPDNQIVATIVEEdvafgpenlGIPPEEIRERVDESLKKVGM-----YEYRRHAPHLLSGGQKQRVAIagILAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 472 DREVFllDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHddrYFDV---ADRIYRLDYGQLV 533
Cdd:PRK13633 164 ECIIF--DEPTAMLDPSGRREVVNTIKELNKKYGITIILITH---YMEEaveADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-533 |
9.56e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPgqsdDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL--DGRTSEWHR 400
Cdd:PRK13639 2 LETRDLKYSYP----DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAIF--ADFYLFA-----DV----LGEGGQHDGLEARVEHYLERLGLahkvqfvDGRLSTTA--LSQGQRKRLALLL 467
Cdd:PRK13639 78 KTVGIVFqnPDDQLFAptveeDVafgpLNLGLSKEEVEKRVKEALKAVGM-------EGFENKPPhhLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 468 LMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIM-KLLYDLNKEGITIIISTHDvDLVPVYADKVYVMSDGKII 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
323-533 |
1.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH--- 399
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 -REHFAAI--FADFYLFADVLGE----GGQHDGL-----EARVEHYLERLGLAHKVQfvdgRLSTTALSQGQRKRLALLL 467
Cdd:PRK13643 82 vRKKVGVVfqFPESQLFEETVLKdvafGPQNFGIpkekaEKIAAEKLEMVGLADEFW----EKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 468 LMMEDREVFLLDEWAADQDPVFRhVFYHELLPELKAAGKTVIAITH-DDRYFDVADRIYRLDYGQLV 533
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKAR-IEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHII 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
346-534 |
1.76e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.29 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAaifadfyLFADVL-------- 417
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA-------LLPQHHltpegitv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 418 ---------------GEGGQHDglEARVEHYLERLGLAHkvqFVDGRLstTALSQGQRKRLALLLLMMEDREVFLLDEWA 482
Cdd:PRK11231 94 relvaygrspwlslwGRLSAED--NARVNQAMEQTRINH---LADRRL--TDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 483 ADQDpVFRHVFYHELLPELKAAGKTVIAITHD----DRYfdvADRIYRLDYGQLVH 534
Cdd:PRK11231 167 TYLD-INHQVELMRLMRELNTQGKTVVTVLHDlnqaSRY---CDHLVVLANGHVMA 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-533 |
2.88e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPgqsdDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL-DGRTSEWHRE 401
Cdd:PRK13644 2 IRLENVSYSYP----DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 HFAAIFADFYlfADVLGEGGQHD-------------GLEARVEHYLERLGLA---HKvqfvdgrlSTTALSQGQRKRLAL 465
Cdd:PRK13644 78 LVGIVFQNPE--TQFVGRTVEEDlafgpenlclppiEIRKRVDRALAEIGLEkyrHR--------SPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 466 LLLMMEDREVFLLDEWAADQDP-----VFRHVfyhellPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPdsgiaVLERI------KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
346-540 |
3.11e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.20 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG---VPLDgrtsewhrehFAAIF-ADF------YLFAD 415
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsALLE----------LGAGFhPELtgreniYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 416 VLG-EGGQHDGLEARVEHYLErLGlahkvQFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFY 494
Cdd:COG1134 115 LLGlSRKEIDEKFDEIVEFAE-LG-----DFIDQPVKT--YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2733243359 495 HELLpELKAAGKTVIAITHDDRYF-DVADRIYRLDYGQLVHYDHATE 540
Cdd:COG1134 187 ARIR-ELRESGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
346-515 |
3.19e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE-----HFAAIFAD--------FYL 412
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylgHQPGIKTEltalenlrFYQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 413 fadvlgeGGQHDGLEARVEHYLERLGLAhkvqfvdGR--LSTTALSQGQRKRLALLLLMMEDREVFLLDE--WAADQDPV 488
Cdd:PRK13538 100 -------RLHGPGDDEALWEALAQVGLA-------GFedVPVRQLSAGQQRRVALARLWLTRAPLWILDEpfTAIDKQGV 165
|
170 180
....*....|....*....|....*..
gi 2733243359 489 FRhvfYHELLPELKAAGKTVIAITHDD 515
Cdd:PRK13538 166 AR---LEALLAQHAEQGGMVILTTHQD 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
346-535 |
3.62e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 77.61 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLY-----QPSAGTVSLNG--VPLDGRTSEWHREHFAAIFADFYLF----A 414
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGkdIYDLDVDVLELRRRVGMVFQKPNPFpgsiY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 415 D-------VLGEGGqHDGLEARVEHYLERLGLAHKvqfVDGRLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDP 487
Cdd:cd03260 99 DnvayglrLHGIKL-KEELDERVEEALRKAALWDE---VKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 488 VFRHVFyHELLPELKAAgKTVIAITHD----DRyfdVADRIYRLDYGQLVHY 535
Cdd:cd03260 175 ISTAKI-EELIAELKKE-YTIVIVTHNmqqaAR---VADRTAFLLNGRLVEF 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
346-536 |
6.35e-16 |
|
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: 77.37 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG-VPldGRTSEWHREHFAAIFAD-------------FY 411
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVP--WKRRKKFLRRIGVVFGQktqlwwdlpvidsFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 412 LFADVLGEGGQHdgLEARVEHYLERLGLAHkvqFVDgrLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRH 491
Cdd:cd03267 118 LLAAIYDLPPAR--FKKRLDELSELLDLEE---LLD--TPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2733243359 492 VFYHELLPELKAAGKTVIAITHDDRyfDV---ADRIYRLDYGQLVhYD 536
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMK--DIealARRVLVIDKGRLL-YD 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
343-516 |
1.07e-15 |
|
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: 75.86 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE-----HFAAIFADFYLFADVL 417
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylgHLPGLKPELSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 418 GEGGQHDGLEARVEHYLERLGLAHKVQfvdgrLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHeL 497
Cdd:TIGR01189 96 FWAAIHGGAQRTIEDALAAVGLTGFED-----LPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG-L 169
|
170
....*....|....*....
gi 2733243359 498 LPELKAAGKTVIAITHDDR 516
Cdd:TIGR01189 170 LRAHLARGGIVLLTTHQDL 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
323-533 |
1.44e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 76.32 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL-----DGRtSE 397
Cdd:COG4181 9 IELRGLTKTVGTGAGELTI-LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldeDAR-AR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 398 WHREHFAAIFADFYLFA------DVL--GEGGQHDGLEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLLM 469
Cdd:COG4181 87 LRARHVGFVFQSFQLLPtltaleNVMlpLELAGRRDARARARALLERVGLGHRLDHYPAQLSG-----GEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 470 MEDREVFLLDEWAADQDPVFRHVFYhELLPEL-KAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQII-DLLFELnRERGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
323-545 |
2.01e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.20 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSL----NGVPLDGRTSEW 398
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 HREH--------------FAAIFADFYLFADVLGEG--------GQHDgLEAR--VEHYLERLGLahKVQFVDgrLSTTA 454
Cdd:PRK13631 102 NPYSkkiknfkelrrrvsMVFQFPEYQLFKDTIEKDimfgpvalGVKK-SEAKklAKFYLNKMGL--DDSYLE--RSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 455 LSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKIL 255
|
250
....*....|..
gi 2733243359 534 hydhATESPFQL 545
Cdd:PRK13631 256 ----KTGTPYEI 263
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
341-535 |
2.88e-15 |
|
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: 75.45 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 341 FQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEwhREHFAAIFADFYLFADVLGEG 420
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 GQHDGL----------EARVEHYLERLGLAHKVQfvdgRLSTTaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFR 490
Cdd:cd03299 91 NIAYGLkkrkvdkkeiERKVLEIAEMLGIDHLLN----RKPET-LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2733243359 491 HVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHY 535
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQV 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-524 |
3.15e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQS--DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRT-SEWH 399
Cdd:COG1129 5 LEMRGISKSFGGVKalDG-------VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REHFAAIFADFYLFAD-------VLGEGGQHDGL------EARVEHYLERLGLAhkvqfVDGRLSTTALSQGQRKRLALL 466
Cdd:COG1129 78 AAGIAIIHQELNLVPNlsvaeniFLGREPRRGGLidwramRRRARELLARLGLD-----IDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 467 LLMMEDREVFLLDE-WAA-DQDPVfRHVFyhELLPELKAAGKTVIAITHD-DRYFDVADRI 524
Cdd:COG1129 153 RALSRDARVLILDEpTASlTEREV-ERLF--RIIRRLKAQGVAIIYISHRlDEVFEIADRV 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
323-513 |
3.96e-15 |
|
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: 75.12 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAG-TVSLNGVPLdGRTSEW-HR 400
Cdd:COG1119 4 LELRNVTVRRGGK-----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERR-GGEDVWeLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHF----AAIFADFYL-----------FADVLG---EGGQHDglEARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKR 462
Cdd:COG1119 78 KRIglvsPALQLRFPRdetvldvvlsgFFDSIGlyrEPTDEQ--RERARELLELLGLAH---LADRPFGT--LSQGEQRR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 463 LALLLLMMEDREVFLLDEWAADQDPVFRHVFyHELLPELKAAG-KTVIAITH 513
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELL-LALLDKLAAEGaPTLVLVTH 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
346-543 |
4.55e-15 |
|
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: 74.81 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSE------------WhrehfAAIFADFYLF 413
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvvfqnysllpW-----LTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 414 ADVLGEGGQHDGLEARVEHYLERLGLAHKVqfvDGRlsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVF 493
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEHIALVGLTEAA---DKR--PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 494 YHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHYDHATESPF 543
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNGPAANIGQILEVPF 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
346-527 |
5.02e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.42 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGvpldGRTSEWHREHFAAIFADFYLFADVLGEGG-QHD 424
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLTVRDLVAMGRwARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 425 GL--------EARVEHYLERLGLAhkvQFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFyHE 496
Cdd:NF040873 87 GLwrrltrddRAAVDDALERVGLA---DLAGRQLGE--LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI-IA 160
|
170 180 190
....*....|....*....|....*....|.
gi 2733243359 497 LLPELKAAGKTVIAITHDDRYFDVADRIYRL 527
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
346-513 |
6.77e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.61 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE-----HFAAIFADFYLFADVLgEG 420
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRvgvvpQFDNLDPDFTVRENLL-VF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 GQHDGL-----EARVEHYLERLGLAHKvqfVDGRLSttALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYh 495
Cdd:PRK13537 105 GRYFGLsaaaaRALVPPLLEFAKLENK---ADAKVG--ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW- 178
|
170
....*....|....*...
gi 2733243359 496 ELLPELKAAGKTVIAITH 513
Cdd:PRK13537 179 ERLRSLLARGKTILLTTH 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
343-533 |
9.54e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYqPSAGTVSLNGVPLDG-------RTSEWHREHFAAIFA--DFYLF 413
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwsaaelaRHRAYLSQQQSPPFAmpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 414 ADVLGEGGQHDGLEARVEHYLERLGLAHKVqfvdGRlSTTALSQG--QRKRLALLLLMMEDR-----EVFLLDEWAADQD 486
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEALGLEDKL----SR-PLTQLSGGewQRVRLAAVLLQVWPTinpegQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2733243359 487 PVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:COG4138 166 VAQQAALD-RLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLV 212
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-540 |
9.73e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.20 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYqPSAGTVSLNGVPLdgrtSEW-------HREHFA------AIFAD 409
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPL----EAWsaaelarHRAYLSqqqtppFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 410 FYLFADVLGEGGQHDGLEARVEHYLERLGLAHKVqfvdGRlSTTALSQG--QRKRLALLLLMM-----EDREVFLLDEWA 482
Cdd:PRK03695 87 FQYLTLHQPDKTRTEAVASALNEVAEALGLDDKL----GR-SVNQLSGGewQRVRLAAVVLQVwpdinPAGQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2733243359 483 ADQDpVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHYDHATE 540
Cdd:PRK03695 162 NSLD-VAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
323-524 |
1.13e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.52 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYpgqsDDFAFqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSewHREH 402
Cdd:COG3842 6 LELENVSKRY----GDVTA-LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP--EKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLF-----ADVLGEGGQHDGL-----EARVEHYLERLGLAHKvqfvdGRLSTTALSQGQRKRLAL------- 465
Cdd:COG3842 79 VGMVFQDYALFphltvAENVAFGLRMRGVpkaeiRARVAELLELVGLEGL-----ADRYPHQLSGGQQQRVALaralape 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 466 --LLlmmedrevfLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRI 524
Cdd:COG3842 154 prVL---------LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqEEALALADRI 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
346-533 |
1.16e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH--------REHFAAIFADFYLF---- 413
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQqkglirqlRQHVGFVFQNFNLFphrt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 414 -------ADVLGEGGQHDGLEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLLMMEDREVFLLDEWAADQD 486
Cdd:PRK11264 102 vleniieGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSG-----GQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 487 PvfrhvfyhELLPE-------LKAAGKTVIAITHDDRYF-DVADRIYRLDYGQLV 533
Cdd:PRK11264 177 P--------ELVGEvlntirqLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIV 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
323-531 |
1.18e-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: 72.89 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLN--------------- 387
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPgsiayvsqepwiqng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 388 --------GVPLDgrtSEWHRE--HFAAIFADFYLFAD----VLGEGGqhdglearvehylerlglahkvqfvdgrlstT 453
Cdd:cd03250 81 tirenilfGKPFD---EERYEKviKACALEPDLEILPDgdltEIGEKG-------------------------------I 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 454 ALSQGQRKRLALLLLMMEDREVFLLDE--WAADQDpVFRHVFYHELLPELKaAGKTVIAITHDDRYFDVADRIYRLDYGQ 531
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDplSAVDAH-VGRHIFENCILGLLL-NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
323-533 |
1.65e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.65 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQS--DDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdgrtSEWHR 400
Cdd:PRK13548 3 LEARNLSVRLGGRTllDD-------VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL----ADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAIFA--------DF-YLFADVLGEGGQHDGLEAR-----VEHYLERLGLAHkvqfVDGRlSTTALSQGQRKR---- 462
Cdd:PRK13548 72 AELARRRAvlpqhsslSFpFTVEEVVAMGRAPHGLSRAeddalVAAALAQVDLAH----LAGR-DYPQLSGGEQQRvqla 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 463 --LALLLLMMEDREVFLLDEWAADQDPvfrhvfYH-----ELLPEL-KAAGKTVIAITHD----DRYfdvADRIYRLDYG 530
Cdd:PRK13548 147 rvLAQLWEPDGPPRWLLLDEPTSALDL------AHqhhvlRLARQLaHERGLAVIVVLHDlnlaARY---ADRIVLLHQG 217
|
...
gi 2733243359 531 QLV 533
Cdd:PRK13548 218 RLV 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-533 |
1.73e-14 |
|
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: 72.96 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 324 RLSNVHYRYPGQSDDFAFQlgPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHF 403
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILK--GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 404 AAIFADFYLFADVLGEG---GQHDGLEARVEHYLeRLGLAHKvqFVDG---RLST------TALSQGQRKRLALLLLMME 471
Cdd:cd03249 80 GLVSQEPVLFDGTIAENiryGKPDATDEEVEEAA-KKANIHD--FIMSlpdGYDTlvgergSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 472 DREVFLLDEWAADQDPVFRHVFyHELLPELkAAGKTVIAITHddRYFDV--ADRIYRLDYGQLV 533
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLV-QEALDRA-MKGRTTIVIAH--RLSTIrnADLIAVLQNGQVV 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
343-533 |
1.76e-14 |
|
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: 73.69 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVP---LDGRTSEWHREHFAAIFADFY-------L 412
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlyqLDRKQRRAFRRDVQLVFQDSPsavnprmT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 413 FADVLGEGGQH------DGLEARVEHYLERLGLAHKvqfvDGRLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQD 486
Cdd:TIGR02769 107 VRQIIGEPLRHltsldeSEQKARIAELLDMVGLRSE----DADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 487 PVFRHVFYhELLPELKAAGKTV-IAITHDDR---YFdvADRIYRLDYGQLV 533
Cdd:TIGR02769 183 MVLQAVIL-ELLRKLQQAFGTAyLFITHDLRlvqSF--CQRVAVMDKGQIV 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
346-530 |
2.05e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.68 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLY--QPSAGTVSLNGVPLDGRTSewhrehfaaIFADFYLFADVLgeggqh 423
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS---------LIDAIGRKGDFK------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 424 DGLEArvehyLERLGLAHKVQFvdgRLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELKA 503
Cdd:COG2401 114 DAVEL-----LNAVGLSDAVLW---LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARR 185
|
170 180 190
....*....|....*....|....*....|..
gi 2733243359 504 AGKTVIAITHDDryfDVA-----DRIYRLDYG 530
Cdd:COG2401 186 AGITLVVATHHY---DVIddlqpDLLIFVGYG 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
322-533 |
2.89e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYPGQsDDFAfqLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE 401
Cdd:PRK11176 341 DIEFRNVTFTYPGK-EVPA--LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 HFAAIFADFYLFADVLGEGGQHdgleARVEHY----LERLG-LAHKVQFV---DGRLST------TALSQGQRKRLALLL 467
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAY----ARTEQYsreqIEEAArMAYAMDFInkmDNGLDTvigengVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 468 LMMEDREVFLLDEWAADQDPVFRHVFyHELLPELKaAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAI-QAALDELQ-KNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
323-533 |
3.53e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.82 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDdfAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:PRK13642 5 LEVENLVFKYEKESD--VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFAD------FYLFADVLGEGGQHDGLEArvEHYLERLGLA-HKVQFVDGRLSTTA-LSQGQRKRLALLLLMMEDRE 474
Cdd:PRK13642 83 IGMVFQNpdnqfvGATVEDDVAFGMENQGIPR--EEMIKRVDEAlLAVNMLDFKTREPArLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 475 VFLLDEWAADQDPVFRHVFYhELLPELKAAGK-TVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIM-RVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEII 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
346-531 |
4.11e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 71.37 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE-----HFAAIFA------DFYLFA 414
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGllylgHAPGIKTtlsvleNLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 415 DvlgeggqhDGLEARVEHYLERLGLAHKvqfvdGRLSTTALSQGQRKRLALLLLMMEDREVFLLDE--WAADQDPVFRhv 492
Cdd:cd03231 99 A--------DHSDEQVEEALARVGLNGF-----EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEptTALDKAGVAR-- 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 2733243359 493 fYHELLPELKAAGKTVIAITHDDrYFDVADRIYRLDYGQ 531
Cdd:cd03231 164 -FAEAMAGHCARGGMVVLTTHQD-LGLSEAGARELDLGF 200
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
346-530 |
6.32e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.94 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSE---------------------------- 397
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiarmgvvrtfqhvrlfremtvienllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 398 -WHREHFAAIFADfyLFADVLGEGGQHDGLEaRVEHYLERLGLahkVQFVDGRLSTtaLSQGQRKRLALLLLMMEDREVF 476
Cdd:PRK11300 104 aQHQQLKTGLFSG--LLKTPAFRRAESEALD-RAATWLERVGL---LEHANRQAGN--LAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 477 LLDEWAADQDPVFRHVFyHELLPELKAA-GKTVIAITHDDRY-FDVADRIYRLDYG 530
Cdd:PRK11300 176 MLDEPAAGLNPKETKEL-DELIAELRNEhNVTVLLIEHDMKLvMGISDRIYVVNQG 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
326-533 |
6.77e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 326 SNVHYRYPGQSDDFAFQlgPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAA 405
Cdd:TIGR00958 482 QDVSFSYPNRPDVPVLK--GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 406 IFADFYLFADVLGEGGQHDGLEARVEHYLERLGLAHKVQFVDGRLST---------TALSQGQRKRLALLLLMMEDREVF 476
Cdd:TIGR00958 560 VGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgSQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 477 LLDEWAADQDPVFRHVFYHellpELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:TIGR00958 640 ILDEATSALDAECEQLLQE----SRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
323-533 |
6.87e-14 |
|
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: 70.75 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQ--SDDFafqlgpiDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEwHR 400
Cdd:cd03301 1 VELENVTKRFGNVtaLDDL-------NLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EhFAAIFADFYLF-----ADVLGEG-----GQHDGLEARVEHYLERLGLAHKVQfvdgRLsTTALSQGQRKRLALLLLMM 470
Cdd:cd03301 73 D-IAMVFQNYALYphmtvYDNIAFGlklrkVPKDEIDERVREVAELLQIEHLLD----RK-PKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 471 EDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
346-533 |
9.23e-14 |
|
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: 70.32 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWhrEHFAAIFADFYLFADVLGE------ 419
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPNLTARenlrll 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 420 GGQHDGLEARVEHYLERLGLAHkvqfvDGRLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPV----FRhvfyh 495
Cdd:cd03268 97 ARLLGIRKKRIDEVLDVVGLKD-----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDgikeLR----- 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 2733243359 496 ELLPELKAAGKTVIAITHDDRYFD-VADRIYRLDYGQLV 533
Cdd:cd03268 167 ELILSLRDQGITVLISSHLLSEIQkVADRIGIINKGKLI 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
305-533 |
1.20e-13 |
|
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: 73.30 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 305 GESVTFTEPEQAAAPFRE-----------------LRLSNVHYRYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKS 367
Cdd:TIGR03269 245 GEIKEEGTPDEVVAVFMEgvsevekecevevgepiIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKT 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 368 TLAKLMTGLYQPSAGTVSLN-----------GVPLDGRTSEW----HREHfaaifaDFYLFADVLGEGGQHDGLEARVE- 431
Cdd:TIGR03269 325 TLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGRGRAKRYigilHQEY------DLYPHRTVLDNLTEAIGLELPDEl 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 432 ------HYLERLGLAH-KVQFVDGRLSTTaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELKAA 504
Cdd:TIGR03269 399 armkavITLKMVGFDEeKAEEILDKYPDE-LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEM 477
|
250 260 270
....*....|....*....|....*....|
gi 2733243359 505 GKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:TIGR03269 478 EQTFIIVSHDmDFVLDVCDRAALMRDGKIV 507
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
328-536 |
1.21e-13 |
|
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: 70.02 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 328 VHYRYPGQSDDFAFQLgpidlsirRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL-DGRTS---EWHREHF 403
Cdd:cd03297 6 IEKRLPDFTLKIDFDL--------NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKinlPPQQRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 404 AAIFADFYLFAD-------VLGEGGQHDG-LEARVEHYLERLGLAHKVQfvdgrLSTTALSQGQRKRLALLLLMMEDREV 475
Cdd:cd03297 78 GLVFQQYALFPHlnvrenlAFGLKRKRNReDRISVDELLDLLGLDHLLN-----RYPAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 476 FLLDEWAADQDPVFRhvfyHELLPELKAAGK----TVIAITHD-DRYFDVADRIYRLDYGQLVHYD 536
Cdd:cd03297 153 LLLDEPFSALDRALR----LQLLPELKQIKKnlniPVIFVTHDlSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-524 |
1.64e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPG--QSDDfafqlgpIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEwhr 400
Cdd:COG3845 6 LELRGITKRFGGvvANDD-------VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 ehfAAI-------FADFYLFAD-------VLG-EGGQH-----DGLEARVEHYLERLGLAhkvqfVD-----GRLSTtal 455
Cdd:COG3845 76 ---DAIalgigmvHQHFMLVPNltvaeniVLGlEPTKGgrldrKAARARIRELSERYGLD-----VDpdakvEDLSV--- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 456 sqGQRKRLALLLLMMEDREVFLLDEwaadqdP--VF-----RHVFyhELLPELKAAGKTVIAITHD-DRYFDVADRI 524
Cdd:COG3845 145 --GEQQRVEILKALYRGARILILDE------PtaVLtpqeaDELF--EILRRLAAEGKSIIFITHKlREVMAIADRV 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
323-533 |
2.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.96 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPgQSDDFAFQ-LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH-- 399
Cdd:PRK13646 3 IRFDNVSYTYQ-KGTPYEHQaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 --REHFAAIF--ADFYLFADVLGE---------GGQHDGLEARVEHYLERLGLAHKVQfvdgRLSTTALSQGQRKRLALL 466
Cdd:PRK13646 82 pvRKRIGMVFqfPESQLFEDTVEReiifgpknfKMNLDEVKNYAHRLLMDLGFSRDVM----SQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 467 LLMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKA-AGKTVIAITHD----DRYfdvADRIYRLDYGQLV 533
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVM-RLLKSLQTdENKTIILVSHDmnevARY---ADEVIVMKEGSIV 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-532 |
2.19e-13 |
|
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: 69.81 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSD-----DFAFQLGPidlsirrGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSE 397
Cdd:cd03248 12 VKFQNVTFAYPTRPDtlvlqDVSFTLHP-------GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 398 WHREHFAAIFADFYLFADVLGEGGQHDGLEARVEHYLERLGLAHKVQFVDG---RLSTTA------LSQGQRKRLALLLL 468
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISElasGYDTEVgekgsqLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 469 MMEDREVFLLDEWAADQDPVFRHVFYHELLPELKAagKTVIAITHDDRYFDVADRIYRLDYGQL 532
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
323-533 |
2.36e-13 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 69.57 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYpgqsDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:cd03253 1 IEFENVTFAY----DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGEGGQHDGLEARVEHYLERLGLAHK----VQFVDGrLST------TALSQGQRKRLALLLLMMED 472
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIhdkiMRFPDG-YDTivgergLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYHELlpELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAAL--RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
323-534 |
3.28e-13 |
|
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: 69.00 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYpGQSDdfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEwhrEH 402
Cdd:cd03224 1 LEVENLNAGY-GKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH---ER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAA----------IFAD------FYLFADVLGEGGQHDGLEaRVEHYLERLglahkvqfvDGRLSTTA--LSQGQRKRLA 464
Cdd:cd03224 73 ARAgigyvpegrrIFPEltveenLLLGAYARRRAKRKARLE-RVYELFPRL---------KERRKQLAgtLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 465 LLLLMMEDREVFLLDEWAADQDPVF-RHVFyhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVH 534
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIvEEIF--EAIRELRDEGVTILLVEQNaRFALEIADRAYVLERGRVVL 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
323-533 |
3.59e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 69.19 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYpgqsDDFAfQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSewHREH 402
Cdd:cd03300 1 IELENVSKFY----GGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLF-----ADVLGEGGQHDGL-----EARVEHYLE--RL-GLAHKvqfvdgrlSTTALSQGQRKRLALLLLM 469
Cdd:cd03300 74 VNTVFQNYALFphltvFENIAFGLRLKKLpkaeiKERVAEALDlvQLeGYANR--------KPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2733243359 470 MEDREVFLLDEWAADQDPVFRhvfyHELLPELKA----AGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLR----KDMQLELKRlqkeLGITFVFVTHDqEEALTMSDRIAVMNKGKIQ 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
348-534 |
3.62e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.22 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 348 LSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL----DGRTSEWHREHFAAIFADFYLFA-----DVLG 418
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRRKKIAMVFQSFALMPhmtvlDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 EGGQHDGLEA--RVEHYLERLGLAHKVQFVDGrlSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHE 496
Cdd:PRK10070 129 FGMELAGINAeeRREKALDALRQVGLENYAHS--YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190
....*....|....*....|....*....|....*....
gi 2733243359 497 LLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVH 534
Cdd:PRK10070 207 LVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQ 245
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
325-524 |
4.52e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 325 LSNVHYRYPGQS--DDFAFqlgpidlSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE- 401
Cdd:PRK13536 44 LAGVSKSYGDKAvvNGLSF-------TVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARi 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 ----HFAAIFADFYLFADVLgEGGQHDGLEAR-----VEHYLERLGLAHKvqfVDGRLSTtaLSQGQRKRLALLLLMMED 472
Cdd:PRK13536 117 gvvpQFDNLDLEFTVRENLL-VFGRYFGMSTReieavIPSLLEFARLESK---ADARVSD--LSGGMKRRLTLARALIND 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHddrYFDVADRI 524
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIW-ERLRSLLARGKTILLTTH---FMEEAERL 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
346-540 |
7.31e-13 |
|
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: 67.78 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWhREHFAAIFAD------------FYLF 413
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV-RRRIGIVFQDlsvddeltgwenLYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 414 ADVLGEGGQHdgLEARVEHYLERLGLAhkvQFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFR-HV 492
Cdd:cd03265 98 ARLYGVPGAE--RRERIDELLDFVGLL---EAADRLVKT--YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRaHV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2733243359 493 FyhELLPELKAA-GKTVIAITHD-DRYFDVADRIYRLDYGQLVHYDHATE 540
Cdd:cd03265 171 W--EYIEKLKEEfGMTILLTTHYmEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
323-491 |
7.65e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFafqlgpiDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVplDGRTSEWHREH 402
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF-------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGEG----GQHDGL------EARVEHYLERLGLAHKVQfvdgRLStTALSQGQRKRLALLLLMMED 472
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQniglGLNPGLklnaaqREKLHAIARQMGIEDLLA----RLP-GQLSGGQRQRVALARCLVRE 147
|
170
....*....|....*....
gi 2733243359 473 REVFLLDEWAADQDPVFRH 491
Cdd:PRK10771 148 QPILLLDEPFSALDPALRQ 166
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
346-537 |
8.34e-13 |
|
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: 67.90 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGEG----G 421
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNldpfG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 422 QHDglEARVEHYLERLGLAHKVQFVDGRLSTTA------LSQGQRKRLALLLLMMEDREVFLLDEWAADQDP-------- 487
Cdd:cd03244 103 EYS--DEELWQALERVGLKEFVESLPGGLDTVVeeggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPetdaliqk 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2733243359 488 VFRHVFyhellpelkaAGKTVIAITHDDRYFDVADRIYRLDYGQLVHYDH 537
Cdd:cd03244 181 TIREAF----------KDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
314-519 |
8.83e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 314 EQAAAPFRELRLSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdg 393
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRT-----LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 394 rtSEWHREHFAAIFADF--------------------YLFADVLGEGGQHDglEARVEHYLERLGL---AHKVqfVDgrl 450
Cdd:PRK10575 76 --ESWSSKAFARKVAYLpqqlpaaegmtvrelvaigrYPWHGALGRFGAAD--REKVEEAISLVGLkplAHRL--VD--- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 451 sttALSQGQRKRLALLLLMMEDREVFLLDEWAADQDpVFRHVFYHELLPEL-KAAGKTVIAITHD----DRYFD 519
Cdd:PRK10575 147 ---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IAHQVDVLALVHRLsQERGLTVIAVLHDinmaARYCD 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
65-532 |
9.38e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 65 GVISQWLLVQIGHRLVYQLRLRLVAKVLGTAL----ERIERLGSPRIYNALTKDvttvATAFKQLPislynglLLLTGLa 140
Cdd:PLN03232 354 GVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLrlthEARKNFASGKVTNMITTD----ANALQQIA-------EQLHGL- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 141 ymaWlSVPFFVLT--------LGV--------IALGVGLDILLGRKIKALMRAVRQRDDQ---LTEQFEAAIDG-RCelg 200
Cdd:PLN03232 422 ---W-SAPFRIIVsmvllyqqLGVaslfgsliLFLLIPLQTLIVRKMRKLTKEGLQWTDKrvgIINEILASMDTvKC--- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 201 LSRERRhllYRHRLEPVASASLAASVRADTLWAVN---LNWTTLLV-FVLIGTLFFLGqglGLLDQQVVVGYVLAIMFLR 276
Cdd:PLN03232 495 YAWEKS---FESRIQGIRNEELSWFRKAQLLSAFNsfiLNSIPVVVtLVSFGVFVLLG---GDLTPARAFTSLSLFAVLR 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 277 TPISVILDAVPAVIRGHVALQAIDALALGESVTFTE--PEQAAAPfrELRLSNVHYRYPGQSDDFAfqLGPIDLSIRRGE 354
Cdd:PLN03232 569 SPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQnpPLQPGAP--AISIKNGYFSWDSKTSKPT--LSDINLEIPVGS 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 355 LIFVVGGNGSGKSTLAKLMTGLYQPSAGT-VSLNGVPLDGRTSEWhreHFAAIFADFYLFADvlgeggqhDGLEARVEHY 433
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGSVAYVPQVSW---IFNATVRENILFGS--------DFESERYWRA 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 434 LERLGLAHKVQFVDGRLST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQDP-VFRHVFYHELLPELKaaGK 506
Cdd:PLN03232 714 IDVTALQHDLDLLPGRDLTeigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELK--GK 791
|
490 500
....*....|....*....|....*.
gi 2733243359 507 TVIAITHDDRYFDVADRIYRLDYGQL 532
Cdd:PLN03232 792 TRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
323-514 |
1.19e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWhreh 402
Cdd:PRK11248 2 LQISHLYADYGGKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 fAAIFADFYL--FADVLGE---GGQHDGL-----EARVEHYLERLGLAHKvqfvdGRLSTTALSQGQRKRLALLLLMMED 472
Cdd:PRK11248 73 -GVVFQNEGLlpWRNVQDNvafGLQLAGVekmqrLEIAHQMLKKVGLEGA-----EKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD 514
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
63-297 |
1.27e-12 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 68.35 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAF-KQLPISLYNGLLLLTGLAY 141
Cdd:cd07346 54 LLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDG-RCELGLSRERRHLlyrHRLEPVASA 220
Cdd:cd07346 134 LFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGiRVVKAFAAEEREI---ERFREANRD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 221 SLAASVRADTLWAVNLNWTTLLVFVLIGTLFFLGqGL----GLLDQQVVVGYVLAIMFLRTPISVILDAVPAVIRGHVAL 296
Cdd:cd07346 211 LRDANLRAARLSALFSPLIGLLTALGTALVLLYG-GYlvlqGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
.
gi 2733243359 297 Q 297
Cdd:cd07346 290 E 290
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-514 |
2.23e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.83 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDgrtsEWHREHFAaifadfYL-----------FA 414
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIG------YLpeerglypkmkVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 415 DVLGEGGQHDGL-----EARVEHYLERLGLAH----KVQfvdgrlsttALSQGQRKRLALLLLMMEDREVFLLDEWAADQ 485
Cdd:COG4152 90 EQLVYLARLKGLskaeaKRRADEWLERLGLGDrankKVE---------ELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180
....*....|....*....|....*....
gi 2733243359 486 DPVFRHVFYHELLpELKAAGKTVIAITHD 514
Cdd:COG4152 161 DPVNVELLKDVIR-ELAAKGTTVIFSSHQ 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-535 |
3.23e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 339 FAFQLGPI----DLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLD--GRTSEWHREHFAAIFAD--- 409
Cdd:PRK13638 9 FRYQDEPVlkglNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQDpeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 410 --FYLFAD------VLGEGGQHDGLEARVEhylERLGLAHKVQFVDGRLSttALSQGQRKRLALLLLMMEDREVFLLDEW 481
Cdd:PRK13638 89 qiFYTDIDsdiafsLRNLGVPEAEITRRVD---EALTLVDAQHFRHQPIQ--CLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 482 AADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHY 535
Cdd:PRK13638 164 TAGLDPAGRTQMI-AIIRRIVAQGNHVIISSHDiDLIYEISDAVYVLRQGQILTH 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
322-533 |
3.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.35 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYPGQSddfAFQ---LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEW 398
Cdd:PRK13634 2 DITFQKVEHRYQYKT---PFErraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 H----REHFAAI--FADFYLFADVLGE----GGQHDGL-----EARVEHYLERLGLAHKVQfvdgRLSTTALSQGQRKRL 463
Cdd:PRK13634 79 KlkplRKKVGIVfqFPEHQLFEETVEKdicfGPMNFGVseedaKQKAREMIELVGLPEELL----ARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 464 ALL-LLMMEDrEVFLLDEWAADQDPVFRH----VFYhellpEL-KAAGKTVIAITH--DD--RYfdvADRIYRLDYGQLV 533
Cdd:PRK13634 155 AIAgVLAMEP-EVLVLDEPTAGLDPKGRKemmeMFY-----KLhKEKGLTTVLVTHsmEDaaRY---ADQIVVMHKGTVF 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
346-540 |
3.52e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.13 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSA---GTVSLNGVPLDGRTSEWHREHFAAIFA---DFYLFADVlgE 419
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKVGIVFQnpdNQFVGATV--G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 420 GGQHDGLEAR----------VEHYLERLGLAhkvQFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVF 489
Cdd:PRK13640 104 DDVAFGLENRavprpemikiVRDVLADVGML---DYIDSEPAN--LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 490 RHVFYHELLPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQLVHYDHATE 540
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
346-513 |
4.03e-12 |
|
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: 65.85 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGV-----PLDGRTS-----------EW--HREHFaAIF 407
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkePAEARRRlgfvsdstglyDRltARENL-EYF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 408 ADFYlfadvlgeGGQHDGLEARVEHYLERLGLAHkvqFVDGRlsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDP 487
Cdd:cd03266 103 AGLY--------GLKGDELTARLEELADRLGMEE---LLDRR--VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180
....*....|....*....|....*.
gi 2733243359 488 VFRHVFYhELLPELKAAGKTVIAITH 513
Cdd:cd03266 170 MATRALR-EFIRQLRALGKCILFSTH 194
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
323-533 |
1.12e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFQ----LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVP---LDGRT 395
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlakLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 396 SEWHREHFAAIFADF-------YLFADVLGEGGQH------DGLEARVEHYLERLGLAHKVqfVDGRlsTTALSQGQRKR 462
Cdd:PRK10419 84 RKAFRRDIQMVFQDSisavnprKTVREIIREPLRHllsldkAERLARASEMLRAVDLDDSV--LDKR--PPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 463 LALLLLMMEDREVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTV-IAITHDDR---YFdvADRIYRLDYGQLV 533
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVI-RLLKKLQQQFGTAcLFITHDLRlveRF--CQRVMVMDNGQIV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
346-535 |
1.17e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTV-----SLNGVPLDGRTsewhrehFAAIFADFYLF-----AD 415
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekRMNDVPPAERG-------VGMVFQSYALYphlsvAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 416 VLGEGGQHDG-----LEARVEHYLERLGLAHkvqFVDGRlsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFR 490
Cdd:PRK11000 95 NMSFGLKLAGakkeeINQRVNQVAEVLQLAH---LLDRK--PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 491 HVFYHELLPELKAAGKTVIAITHDD-RYFDVADRIYRLDYG---------QLVHY 535
Cdd:PRK11000 170 VQMRIEISRLHKRLGRTMIYVTHDQvEAMTLADKIVVLDAGrvaqvgkplELYHY 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
346-527 |
1.40e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG---VPLDGRTSEWHREHFAAIFADFYLFAD------- 415
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRRQIGMIFQDHHLLMDrtvydnv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 416 ---VLGEGGQHDGLEARVEHYLERLGLAHKvqfvdGRLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHV 492
Cdd:PRK10908 101 aipLIIAGASGDDIRRRVSAALDKVGLLDK-----AKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2733243359 493 FYhELLPELKAAGKTVIAITHDDRYfdVADRIYRL 527
Cdd:PRK10908 176 IL-RLFEEFNRVGVTVLMATHDIGL--ISRRSYRM 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
325-533 |
1.74e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 325 LSNVHYRYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH----R 400
Cdd:PRK13649 5 LQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDikqiR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAI--FADFYLFAD-VLGE---GGQHDGL-----EARVEHYLERLGLAHKVQfvdgRLSTTALSQGQRKRLALL-LL 468
Cdd:PRK13649 85 KKVGLVfqFPESQLFEEtVLKDvafGPQNFGVsqeeaEALAREKLALVGISESLF----EKNPFELSGGQMRRVAIAgIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 469 MMEDrEVFLLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITH--DDrYFDVADRIYRLDYGQLV 533
Cdd:PRK13649 161 AMEP-KILVLDEPTAGLDPKGRKELM-TLFKKLHQSGMTIVLVTHlmDD-VANYADFVYVLEKGKLV 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
323-533 |
1.93e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSewhREH 402
Cdd:PRK11288 5 LSFDGIGKTFPGVK-----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAA----IFADFYLFADV-------LGE----GGQHDG--LEARVEHYLERLGLAhkvqfVDGRLSTTALSQGQRKRLAL 465
Cdd:PRK11288 77 LAAgvaiIYQELHLVPEMtvaenlyLGQlphkGGIVNRrlLNYEAREQLEHLGVD-----IDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 466 LLLMMEDREVFLLDE-----WAADQDPVFRhvfyheLLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:PRK11288 152 AKALARNARVIAFDEptsslSAREIEQLFR------VIRELRAEGRVILYVSHRmEEIFALCDAITVFKDGRYV 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
321-547 |
1.96e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.03 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 321 RELRLSNVHYRYPGQSDdFAFQ-LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLN------GVPLDG 393
Cdd:PRK13645 5 KDIILDNVSYTYAKKTP-FEFKaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 394 RTSEWHRE-HFAAIFADFYLFADVLGE----GGQHDGlEARVEHYLERLGLAHKVQFVD--GRLSTTALSQGQRKRLALL 466
Cdd:PRK13645 84 EVKRLRKEiGLVFQFPEYQLFQETIEKdiafGPVNLG-ENKQEAYKKVPELLKLVQLPEdyVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 467 LLMMEDREVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVhydhATESPFQL 545
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVI----SIGSPFEI 238
|
..
gi 2733243359 546 TS 547
Cdd:PRK13645 239 FS 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
325-547 |
2.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.75 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 325 LSNVHYRYpgQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdgrTSE--WH-RE 401
Cdd:PRK13650 7 VKNLTFKY--KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEEnvWDiRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 HFAAIFA---DFYLFADV-----LG---EGGQHDGLEARVEHYLERLGLAhkvQFVDGRLSTtaLSQGQRKRLALLLLMM 470
Cdd:PRK13650 82 KIGMVFQnpdNQFVGATVeddvaFGlenKGIPHEEMKERVNEALELVGMQ---DFKEREPAR--LSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 471 EDREVFLLDEWAADQDPVFRhvfyHELLPELKAA----GKTVIAITHDDRYFDVADRIYRLDYGQLvhydHATESPFQLT 546
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGR----LELIKTIKGIrddyQMTVISITHDLDEVALSDRVLVMKNGQV----ESTSTPRELF 228
|
.
gi 2733243359 547 S 547
Cdd:PRK13650 229 S 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
323-531 |
2.62e-11 |
|
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: 61.70 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVslngvpldgrtsEWHReh 402
Cdd:cd03221 1 IELENLSKTYGGK-----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGS-- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 faaifadfylfadvlgeggqhdglearvehyleRLGLAHKVQfvdgrlsttaLSQGQRKRLALLLLMMEDREVFLLDEWA 482
Cdd:cd03221 62 ---------------------------------TVKIGYFEQ----------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 483 ADQDPVFRhvfyhELLPE-LKAAGKTVIAITHdDRYF--DVADRIYRLDYGQ 531
Cdd:cd03221 99 NHLDLESI-----EALEEaLKEYPGTVILVSH-DRYFldQVATKIIELEDGK 144
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
353-515 |
3.17e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 353 GELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGvplDGRTSEWHRE--HFAA---------IFADFYLF-ADVLGEG 420
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEacHYLGhrnamkpalTVAENLEFwAAFLGGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 gqhdglEARVEHYLERLGLAH--KVQFVDgrlsttaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFyHELL 498
Cdd:PRK13539 105 ------ELDIAAALEAVGLAPlaHLPFGY-------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF-AELI 170
|
170
....*....|....*..
gi 2733243359 499 PELKAAGKTVIAITHDD 515
Cdd:PRK13539 171 RAHLAQGGIVIAATHIP 187
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
346-534 |
4.02e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.19 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH--REHFAAIFADFYLFADVLG----- 418
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERliRQEAGMVFQQFYLFPHLTAlenvm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 ------EGGQHDGLEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRhv 492
Cdd:PRK09493 100 fgplrvRGASKEEAEKQARELLAKVGLAERAHHYPSELSG-----GQQQRVAIARALAVKPKLMLFDEPTSALDPELR-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2733243359 493 fyHELLP---ELKAAGKTVIAITHDDRYF-DVADRIYRLDYGQLVH 534
Cdd:PRK09493 173 --HEVLKvmqDLAEEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAE 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-536 |
4.84e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.95 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG-VPLDGRTSewHREHFAAIF------------AD-FY 411
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKRRKE--FARRIGVVFgqrsqlwwdlpaIDsFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 412 LFADV--LGEggqhDGLEARVEHYLERLGLAHKvqfvdgrLSTTA--LSQGQRKRLALLLLMMEDREVFLLDEwaadqdP 487
Cdd:COG4586 119 LLKAIyrIPD----AEYKKRLDELVELLDLGEL-------LDTPVrqLSLGQRMRCELAAALLHRPKILFLDE------P 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 488 -----VFRHVFYHELLPELKAA-GKTVIAITHDDRyfDV---ADRIYRLDYGQLVhYD 536
Cdd:COG4586 182 tigldVVSKEAIREFLKEYNRErGTTILLTSHDMD--DIealCDRVIVIDHGRII-YD 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
322-543 |
6.24e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 62.74 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYPGqsddfaFQ-LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG-----VPLDGRT 395
Cdd:cd03296 2 SIEVRNVSKRFGD------FVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 396 SEWHREHFaAIFADFYLFADV--------LGEGGQHDGLEARVEHYLERLGLAHKvqfvdGRLSTTALSQGQRKRLALLL 467
Cdd:cd03296 76 VGFVFQHY-ALFRHMTVFDNVafglrvkpRSERPPEAEIRAKVHELLKLVQLDWL-----ADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 468 LMMEDREVFLLDEWAADQDPVFR---HVFYHELLPELkaaGKTVIAITHD-DRYFDVADRIYRLDYGQLVH-------YD 536
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRkelRRWLRRLHDEL---HVTTVFVTHDqEEALEVADRVVVMNKGRIEQvgtpdevYD 226
|
....*..
gi 2733243359 537 HATeSPF 543
Cdd:cd03296 227 HPA-SPF 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-487 |
6.56e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.80 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDgRTSEWHREHFAAifadfYLFAD-VLG------ 418
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEYKRAKYIG-----RVFQDpMMGtapsmt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 --EG-------GQHDGL-----EARVEHYLERL-----GLAHkvqfvdgRLSTTA--LSQGQRKRLALLLLMMEDREVFL 477
Cdd:COG1101 99 ieENlalayrrGKRRGLrrgltKKRRELFRELLatlglGLEN-------RLDTKVglLSGGQRQALSLLMATLTKPKLLL 171
|
170
....*....|
gi 2733243359 478 LDEWAADQDP 487
Cdd:COG1101 172 LDEHTAALDP 181
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-480 |
1.33e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 62.86 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYPGqsddfaFQ-LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHR 400
Cdd:COG1118 2 SIEVRNISKRFGS------FTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 eHFAAIFADFYLF-----ADVLGEGGQHDGL-----EARVEHYLERLGLAHkvqfVDGRLSTTaLSQGQRKRLALLllmm 470
Cdd:COG1118 76 -RVGFVFQHYALFphmtvAENIAFGLRVRPPskaeiRARVEELLELVQLEG----LADRYPSQ-LSGGQRQRVALA---- 145
|
170
....*....|....*.
gi 2733243359 471 edR------EVFLLDE 480
Cdd:COG1118 146 --RalavepEVLLLDE 159
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
343-509 |
1.44e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPldGRTSEWHR-----EHFAAIFADFYLFADVL 417
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT--ATRGDRSRfmaylGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 418 GEGGQHdGLEARV--EHYLERLGLAHKVQFVdgrlsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYH 495
Cdd:PRK13543 105 FLCGLH-GRRAKQmpGSALAIVGLAGYEDTL-----VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNR 178
|
170
....*....|....
gi 2733243359 496 ELLPELKAAGKTVI 509
Cdd:PRK13543 179 MISAHLRGGGAALV 192
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
346-533 |
1.66e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWH--REHFAAIF--ADFYLFADVLGE-- 419
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdiRKKVGLVFqyPEYQLFEETIEKdi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 420 --GGQHDGLE-----ARVEHYLERLGLAHKVqFVDGrlSTTALSQGQRKRLALL-LLMMEDrEVFLLDEWAADQDPVFRh 491
Cdd:PRK13637 106 afGPINLGLSeeeieNRVKRAMNIVGLDYED-YKDK--SPFELSGGQKRRVAIAgVVAMEP-KILILDEPTAGLDPKGR- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2733243359 492 vfyHELLPELKAAGK----TVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:PRK13637 181 ---DEILNKIKELHKeynmTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
63-193 |
1.88e-10 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 62.07 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISLYNGLLLLTG-LAY 141
Cdd:cd18551 51 VLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGaVVL 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAI 193
Cdd:cd18551 131 MFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERAL 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
325-519 |
1.97e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 325 LSNVHYRYPGQS--DDFAFQlgpidlsIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLnGVPLDGRTSEWHReh 402
Cdd:PRK11147 322 MENVNYQIDGKQlvKDFSAQ-------VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHR-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 fAAIFADFYLFaDVLGEGGQHDGLEARVEHYlerLGLAHKVQFVDGRLST--TALSQGQRKRLALLLLMMEDREVFLLDE 480
Cdd:PRK11147 392 -AELDPEKTVM-DNLAEGKQEVMVNGRPRHV---LGYLQDFLFHPKRAMTpvKALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2733243359 481 WAADQDpvfrhVFYHELLPELKAAGK-TVIAITHDDRYFD 519
Cdd:PRK11147 467 PTNDLD-----VETLELLEELLDSYQgTVLLVSHDRQFVD 501
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
322-514 |
2.17e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.52 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYpGQSDdfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL---------- 391
Cdd:PRK10619 5 KLNVIDLHKRY-GEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 392 ---DGRTSEWHREHFAAIFADFYLFA------DVLGEGGQHDGL---EA--RVEHYLERLGLAHKVQfvdGRLSTTaLSQ 457
Cdd:PRK10619 80 kvaDKNQLRLLRTRLTMVFQHFNLWShmtvleNVMEAPIQVLGLskqEAreRAVKYLAKVGIDERAQ---GKYPVH-LSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 458 GQRKRLALLLLMMEDREVFLLDEWAADQDP-----VFRhvfyheLLPELKAAGKTVIAITHD 514
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPelvgeVLR------IMQQLAEEGKTMVVVTHE 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
327-535 |
2.25e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.74 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 327 NVHYRYPGQSDdfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAI 406
Cdd:PRK13652 8 DLCYSYSGSKE----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 407 F--ADFYLFADVLGE---------GGQHDGLEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLLMMEDREV 475
Cdd:PRK13652 84 FqnPDDQIFSPTVEQdiafgpinlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSG-----GEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 476 FLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHY 535
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAY 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
343-540 |
2.47e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.18 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYqpSAGTVSLNGVPLDGRTSEWH----------REHFAAIFADFYL 412
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI--TGDKSAGSHIELLGRTVQREgrlardirksRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 413 ------FADVL-GEGGQ-----------HDGLEARVEHYLERLGLAHkvqFVDGRLSTtaLSQGQRKRLALLLLMMEDRE 474
Cdd:PRK09984 98 vnrlsvLENVLiGALGStpfwrtcfswfTREQKQRALQALTRVGMVH---FAHQRVST--LSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 475 VFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQlVHYDHATE 540
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGH-VFYDGSSQ 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
324-533 |
3.57e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 324 RLSNVHYRYPGQSDDFAfQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGV---PLDGRTSEWHR 400
Cdd:PRK11153 3 ELKNISKVFPQGGRTIH-ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAIFADFYLFAD--VLG--------EGGQHDGLEARVEHYLERLGLAHKvqfvdgRLSTTA-LSQGQRKRLALLLLM 469
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrtVFDnvalplelAGTPKAEIKARVTELLELVGLSDK------ADRYPAqLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 470 MEDREVFLLDEWAADQDP-VFRHVFyhELLPEL-KAAGKTVIAITHD-DRYFDVADRIYRLDYGQLV 533
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPaTTRSIL--ELLKDInRELGLTIVLITHEmDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
330-547 |
5.29e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.11 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 330 YRYPGQS-DDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTvslngVPLDGRTSEWHREHfaaIFA 408
Cdd:cd03237 1 YTYPTMKkTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-----IEIELDTVSYKPQY---IKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 409 DF-----YLFADVLGEGGQHDGLEARVehyLERLGLAhkvQFVDGRLSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAA 483
Cdd:cd03237 73 DYegtvrDLLSSITKDFYTHPYFKTEI---AKPLQIE---QILDREVPE--LSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 484 DQD--------PVFRHVFYHellpelkaAGKTVIAITHDDRYFD-VADRIYRLDyGQLVHYDHATeSPFQLTS 547
Cdd:cd03237 145 YLDveqrlmasKVIRRFAEN--------NEKTAFVVEHDIIMIDyLADRLIVFE-GEPSVNGVAN-PPQSLRS 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
346-535 |
7.71e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAG-----------------------TVSLN---GVP-----LDgR 394
Cdd:TIGR03719 24 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpgikvgylpqepqldptkTVRENveeGVAeikdaLD-R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 395 TSEWHrEHFAAIFADFYLFADVLGE-------GGQHDgLEARVEHYLERLGLAhkvqfvDGRLSTTALSQGQRKRLALLL 467
Cdd:TIGR03719 103 FNEIS-AKYAEPDADFDKLAAEQAElqeiidaADAWD-LDSQLEIAMDALRCP------PWDADVTKLSGGERRRVALCR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 468 LMMEDREVFLLDEWA--ADQDPVF---RHvfyhellpeLKAAGKTVIAITHdDRYF--DVADRIYRLDYGQLVHY 535
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTnhLDAESVAwleRH---------LQEYPGTVVAVTH-DRYFldNVAGWILELDRGRGIPW 239
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
346-534 |
9.05e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.10 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVS--LNGVPLDGRTSEWHREHFAAI----------------- 406
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTKEKEKVLEKLViqktrfkkikkikeirr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 407 -------FADFYLFADVLGE----GGQHDGL---EA--RVEHYLERLGLahKVQFVDGrlSTTALSQGQRKRLALL-LLM 469
Cdd:PRK13651 106 rvgvvfqFAEYQLFEQTIEKdiifGPVSMGVskeEAkkRAAKYIELVGL--DESYLQR--SPFELSGGQKRRVALAgILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 470 MEDREVFlLDEWAADQDPVFRHVFYhELLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVH 534
Cdd:PRK13651 182 MEPDFLV-FDEPTAGLDPQGVKEIL-EIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKIIK 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
346-526 |
1.11e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE----------HFAAIFADFYLFAD 415
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqklgfiyQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 416 V----LGEGGQHDGLEARVEHYLERLGLAHKVQFvdgrlSTTALSQGQRKRLALLLLMMEDREVFLLDEWAA--DQ---D 486
Cdd:PRK11629 108 VamplLIGKKKPAEINSRALEMLAAVGLEHRANH-----RPSELSGGERQRVAIARALVNNPRLVLADEPTGnlDArnaD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2733243359 487 PVFrhvfyhELLPELKAA-GKTVIAITHDdryFDVADRIYR 526
Cdd:PRK11629 183 SIF------QLLGELNRLqGTAFLVVTHD---LQLAKRMSR 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
343-486 |
1.14e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFAD------V 416
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADtflanvT 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 417 LGEggqhDGLEARVEHYLERLGLAHKVQFVDGRLST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQD 486
Cdd:PRK10790 437 LGR----DISEEQVWQALETVQLAELARSLPDGLYTplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-533 |
1.46e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGL--YQpsaGTVSLNGVPL-DGRTSEWhREHFAAIFADFYLFADVLGE 419
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELrELDPESW-RKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 420 G---GQHDGLEARVEHYLER-----------LGLAHKVQFVDGRLSTtalsqGQRKRLALLLLMMEDREVFLLDEWAADQ 485
Cdd:PRK11174 442 NvllGNPDASDEQLQQALENawvseflpllpQGLDTPIGDQAAGLSV-----GQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 486 DPVF-RHVfyhelLPELKAA--GKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:PRK11174 517 DAHSeQLV-----MQALNAAsrRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
346-532 |
1.63e-09 |
|
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: 60.80 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE-----------HFAAIFADFYLFA 414
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSlgmcpqhnilfHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 415 DVLGEGGQHDGLEarVEHYLERLGLAHKVQfvdgrLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFY 494
Cdd:TIGR01257 1029 QLKGRSWEEAQLE--MEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190
....*....|....*....|....*....|....*....
gi 2733243359 495 HELLPelKAAGKTVIAITHDDRYFDV-ADRIYRLDYGQL 532
Cdd:TIGR01257 1102 DLLLK--YRSGRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
322-537 |
2.40e-09 |
|
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: 57.42 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYpgqSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE 401
Cdd:cd03369 6 EIEVENLSVRY---APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 HFAAIFADFYLFAdvlgeGGQHDGLEARVEHYLERLGLAHKVQfvDGRLSttaLSQGQRKRLALLLLMMEDREVFLLDEW 481
Cdd:cd03369 83 SLTIIPQDPTLFS-----GTIRSNLDPFDEYSDEEIYGALRVS--EGGLN---LSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 482 AADQDPVFRHVFYHELLPELKaaGKTVIAITHDDRYFDVADRIYRLDYGQLVHYDH 537
Cdd:cd03369 153 TASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
323-464 |
2.57e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 58.94 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDF-AfqLGPIDLSIRRGElIF-VVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDG-RTSEW- 398
Cdd:COG1135 2 IELENLSKTFPTKGGPVtA--LDDVSLTIEKGE-IFgIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 399 -HREHFAAIFADFYLFA--DVLG------EggqHDGL-----EARVEHYLERLGLAHKV-----QfvdgrlsttaLSQGQ 459
Cdd:COG1135 79 aARRKIGMIFQHFNLLSsrTVAEnvalplE---IAGVpkaeiRKRVAELLELVGLSDKAdaypsQ----------LSGGQ 145
|
....*
gi 2733243359 460 RKRLA 464
Cdd:COG1135 146 KQRVG 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
312-464 |
2.97e-09 |
|
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: 59.31 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 312 EPEQAAAPFRE-----LRLSNVHYRYPGQSDDFAFQLGP------IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLyQPS 380
Cdd:COG4172 260 EPRGDPRPVPPdapplLEARDLKVWFPIKRGLFRRTVGHvkavdgVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 381 AGTVSLNGVPLDGRTSEW---HREHFAAIFADFY-------LFADVLGEG--GQHDGL-----EARVEHYLERLGLAHKV 443
Cdd:COG4172 339 EGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPFgslsprmTVGQIIAEGlrVHGPGLsaaerRARVAEALEEVGLDPAA 418
|
170 180
....*....|....*....|....*..
gi 2733243359 444 ------QFvdgrlsttalSQGQRKRLA 464
Cdd:COG4172 419 rhryphEF----------SGGQRQRIA 435
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
338-522 |
6.31e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 338 DFAFQ----LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE-----HFAAIFA 408
Cdd:PRK13540 8 DFDYHdqplLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQlcfvgHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 409 DFYLFADVLGEGGQHDGlEARVEHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLLMMEDREVFLLDEWAADQDPV 488
Cdd:PRK13540 88 YLTLRENCLYDIHFSPG-AVGITELCRLFSLEHLIDYPCGLLSS-----GQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180 190
....*....|....*....|....*....|....
gi 2733243359 489 FRHVFYHElLPELKAAGKTVIAITHDDRYFDVAD 522
Cdd:PRK13540 162 SLLTIITK-IQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
312-533 |
7.33e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.43 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 312 EPEQAAAPFR---ELRLSNVHYRYPGQS---DDFAFQLGPidlsirrGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVS 385
Cdd:PRK13657 321 DPPGAIDLGRvkgAVEFDDVSFSYDNSRqgvEDVSFEAKP-------GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 386 LNGVPLDGRTSEWHREHFAAIFADFYLFADVLGEG---GQHDGLEARVEHYLERlglAHKVQFVD---GRLSTTA----- 454
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNirvGRPDATDEEMRAAAER---AQAHDFIErkpDGYDTVVgergr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 455 -LSQGQRKRLALLLLMMEDREVFLLDEWAADQDPvfrhvfyhELLPELKAA------GKTVIAITHddRYFDV--ADRIY 525
Cdd:PRK13657 471 qLSGGERQRLAIARALLKDPPILILDEATSALDV--------ETEAKVKAAldelmkGRTTFIIAH--RLSTVrnADRIL 540
|
....*...
gi 2733243359 526 RLDYGQLV 533
Cdd:PRK13657 541 VFDNGRVV 548
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
346-535 |
7.56e-09 |
|
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: 55.63 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGL--YQPSAGTVSLNGVPLDGRTsewhrehfaaifadfylFADVLGEGGQH 423
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRS-----------------FRKIIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 424 DglearvehylerlgLAHKVQFVDGRLSTTA----LSQGQRKRLALLLLMMEDREVFLLDEWAADQDPvFRHVFYHELLP 499
Cdd:cd03213 91 D--------------ILHPTLTVRETLMFAAklrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS-SSALQVMSLLR 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2733243359 500 ELKAAGKTVIAITHDDRY--FDVADRIYRLDYGQLVHY 535
Cdd:cd03213 156 RLADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYF 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
343-388 |
9.43e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 9.43e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG 388
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN 66
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
323-527 |
1.01e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREH 402
Cdd:PRK10247 8 LQLQNVGYLAGDAK-----ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLgeggqHDGL------------EARVEHYLERLGLAHKVQfvdgRLSTTALSQGQRKRLALLLLMM 470
Cdd:PRK10247 83 VSYCAQTPTLFGDTV-----YDNLifpwqirnqqpdPAIFLDDLERFALPDTIL----TKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 471 EDREVFLLDEWAADQDPVFRHV---FYHELLPELKAAgktVIAITHDDRYFDVADRIYRL 527
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNvneIIHRYVREQNIA---VLWVTHDKDEINHADKVITL 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
343-532 |
1.20e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.22 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRtsewhREHFAAIFADFYLFA------DV 416
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwkkvidNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 417 -LGEGG--QHDGLEArvehyLERLGLAHKVQfvdgrLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRhVF 493
Cdd:PRK11247 103 gLGLKGqwRDAALQA-----LAAVGLADRAN-----EWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR-IE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2733243359 494 YHELLPEL-KAAGKTVIAITHD-DRYFDVADRIYRLDYGQL 532
Cdd:PRK11247 172 MQDLIESLwQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
346-501 |
1.85e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGElIF-VVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE----------------------H 402
Cdd:NF033858 285 VSFRIRRGE-IFgFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRvgymsqafslygeltvrqnlelH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 fAAIFAdfylfadvLGEggqhDGLEARVEHYLERLGLAHkvqFVDGRLSttALSQGQRKRLALLLLMMEDREVFLLDEWA 482
Cdd:NF033858 364 -ARLFH--------LPA----AEIAARVAEMLERFDLAD---VADALPD--SLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170
....*....|....*....
gi 2733243359 483 ADQDPVFRHVFYhELLPEL 501
Cdd:NF033858 426 SGVDPVARDMFW-RLLIEL 443
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
346-534 |
2.36e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.07 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGL--YQPSAGTVSLNGVPLdgrtSEWHREHFAA--IF-------------- 407
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDI----LELSPDERARagIFlafqypveipgvsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 408 ADFYLFADVLGEGGQHDGLEAR--VEHYLERLGLAHKvqFVD-----GrlsttaLSQGQRKRLALLLLMMEDREVFLLDE 480
Cdd:COG0396 95 SNFLRTALNARRGEELSAREFLklLKEKMKELGLDED--FLDryvneG------FSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 481 -------WAadqdpvFRHVFyhELLPELKAAGKTVIAITHDDRYFD--VADRIYRLDYGQLVH 534
Cdd:COG0396 167 tdsgldiDA------LRIVA--EGVNKLRSPDRGILIITHYQRILDyiKPDFVHVLVDGRIVK 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
323-524 |
2.52e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.11 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEwHReH 402
Cdd:PRK09452 15 VELRGISKSFDGKE-----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-NR-H 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLF-----ADVLGEGGQ-----HDGLEARVehyLERLGLAHKVQFVDGRlsTTALSQGQRKRLALLLLMMED 472
Cdd:PRK09452 88 VNTVFQSYALFphmtvFENVAFGLRmqktpAAEITPRV---MEALRMVQLEEFAQRK--PHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYHELLPELKAAGKTVIAITHD-DRYFDVADRI 524
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRI 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
346-524 |
2.80e-08 |
|
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: 55.44 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQP---SAGTVSLNGVPLDGRTSEWHRE----HFAAIFADFY------- 411
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPMtslnpvm 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 412 ----LFADVL--GEGGQHDGLEARVEHYLERLGLAHKVQFVDgrlsttA----LSQGQRKR----LALLLlmmeDREVFL 477
Cdd:COG0444 104 tvgdQIAEPLriHGGLSKAEARERAIELLERVGLPDPERRLD------RypheLSGGMRQRvmiaRALAL----EPKLLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 478 LDEwaadqdP-------VFRHVFyhELLPELKAA-GKTVIAITHD---DRYfdVADRI 524
Cdd:COG0444 174 ADE------PttaldvtIQAQIL--NLLKDLQRElGLAILFITHDlgvVAE--IADRV 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
346-533 |
3.31e-08 |
|
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: 53.68 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGL--YQPSAGTVSLNGVPL-DGRTSEWHRehfAAIFADFYLFADVLGeggq 422
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDItDLPPEERAR---LGIFLAFQYPPEIPG---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 423 hdgleARVEHYLERLGlahkvqfvDGrlsttaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPV-FRHVFyhELLPEL 501
Cdd:cd03217 92 -----VKNADFLRYVN--------EG------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDaLRLVA--EVINKL 150
|
170 180 190
....*....|....*....|....*....|....
gi 2733243359 502 KAAGKTVIAITHDDRYFD--VADRIYRLDYGQLV 533
Cdd:cd03217 151 REEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
346-535 |
4.24e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSL-NGV---------PLD-GRTSewhREH------------ 402
Cdd:PRK11819 26 ISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIkvgylpqepQLDpEKTV---RENveegvaevkaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 ---------FAAIFADFYLFADVLGE-------GGQHDgLEARVEHYLERLGLAhkvqfvDGRLSTTALSQGQRKRLALL 466
Cdd:PRK11819 103 drfneiyaaYAEPDADFDALAAEQGElqeiidaADAWD-LDSQLEIAMDALRCP------PWDAKVTKLSGGERRRVALC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 467 LLMMEDREVFLLDE-----------WAAdqdpvfRHvfyhellpeLKAAGKTVIAITHdDRYF--DVADRIYRLDYGQLV 533
Cdd:PRK11819 176 RLLLEKPDMLLLDEptnhldaesvaWLE------QF---------LHDYPGTVVAVTH-DRYFldNVAGWILELDRGRGI 239
|
..
gi 2733243359 534 HY 535
Cdd:PRK11819 240 PW 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
346-513 |
4.42e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRT-SEWHR------EHFAAIFADFYLFADVLG 418
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQlgiylvPQEPLLFPNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 EGGQHDGLEARVEHYLERLGlahkVQFvDGRLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHElL 498
Cdd:PRK15439 110 GLPKRQASMQKMKQLLAALG----CQL-DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSR-I 183
|
170
....*....|....*
gi 2733243359 499 PELKAAGKTVIAITH 513
Cdd:PRK15439 184 RELLAQGVGIVFISH 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-525 |
6.89e-08 |
|
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: 52.43 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 342 QLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRT-SEWHREHFAaifadfYLFADVLGEG 420
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIA------YVPEDRKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 GqhdGLEARVEhylERLGLAHkvqfvdgrlsttALSQGQRKRLALLLLMMEDREVFLLDEwaadqdPvFRHV------FY 494
Cdd:cd03215 89 L---VLDLSVA---ENIALSS------------LLSGGNQQKVVLARWLARDPRVLILDE------P-TRGVdvgakaEI 143
|
170 180 190
....*....|....*....|....*....|..
gi 2733243359 495 HELLPELKAAGKTVIAITHD-DRYFDVADRIY 525
Cdd:cd03215 144 YRLIRELADAGKAVLLISSElDELLGLCDRIL 175
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
350-533 |
6.94e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.44 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 350 IRRGELIFVVGGNGSGKSTLAKLMTGLYQPS---AGTVSLNGVPLDGRtsEWH------------------REH--FAAI 406
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK--EMRaisayvqqddlfiptltvREHlmFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 407 FAdfylfadvLGEGGQHDGLEARVEHYLERLGL---AHKVQFVDGRLSttALSQGQRKRLALLLLMMEDREVFLLDEWAA 483
Cdd:TIGR00955 126 LR--------MPRRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRVK--GLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 484 DQDPVFRHVFYhELLPELKAAGKTVIAITHDDRY--FDVADRIYRLDYGQLV 533
Cdd:TIGR00955 196 GLDSFMAYSVV-QVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVA 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
346-514 |
7.47e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG--VPLDGRTSEWH-REHFA------AIFADFYLFADV 416
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAMSRSRLYTvRKRMSmlfqsgALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 417 LGEGGQHDGLEARVEHY-----LERLGLAHKVQfvdgrLSTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRH 491
Cdd:PRK11831 106 AYPLREHTQLPAPLLHStvmmkLEAVGLRGAAK-----LMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180
....*....|....*....|....
gi 2733243359 492 VFYhELLPEL-KAAGKTVIAITHD 514
Cdd:PRK11831 181 VLV-KLISELnSALGVTCVVVSHD 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
328-532 |
8.00e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 328 VHY--RYPGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL-----DGRtSEWHR 400
Cdd:PRK10584 9 VHHlkKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeEAR-AKLRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 401 EHFAAIFADFYLF------------ADVLGEGGQHDGLEARveHYLERLGLAHKVQFVDGRLSTtalsqGQRKRLALLLL 468
Cdd:PRK10584 88 KHVGFVFQSFMLIptlnalenvelpALLRGESSRQSRNGAK--ALLEQLGLGKRLDHLPAQLSG-----GEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 469 MMEDREVFLLDEWAADQDpvfRHV--FYHELLPEL-KAAGKTVIAITHDDRYFDVADRIYRLDYGQL 532
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLD---RQTgdKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
305-402 |
1.28e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 305 GESVTFTEPEQAAAPFRE-LRLSNVHYRypgqSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGT 383
Cdd:COG3845 239 GREVLLRVEKAPAEPGEVvLEVENLSVR----DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS 314
|
90
....*....|....*....
gi 2733243359 384 VSLNGVPLDGRTSEWHREH 402
Cdd:COG3845 315 IRLDGEDITGLSPRERRRL 333
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
343-532 |
1.31e-07 |
|
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: 54.57 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG----VPldgrTSEWHREhfaAIFADFYLFADVLG 418
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsvayVP----QQAWIQN---DSLRENILFGKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 EGGQHDGLEA-RVEHYLERLGLAHKVQFVDGRLSttaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDP-VFRHVFYHE 496
Cdd:TIGR00957 727 EKYYQQVLEAcALLPDLEILPSGDRTEIGEKGVN---LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHV 803
|
170 180 190
....*....|....*....|....*....|....*.
gi 2733243359 497 LLPELKAAGKTVIAITHDDRYFDVADRIYRLDYGQL 532
Cdd:TIGR00957 804 IGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
306-529 |
1.84e-07 |
|
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: 54.02 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 306 ESVTFTEPEQAAAPFRE--LRLSNVHYRYPGqsddfaFQL----GpidlSIRRGELIFVVGGNGSGKSTLAKLMTGLYQP 379
Cdd:COG1245 323 EPIEFEVHAPRREKEEEtlVEYPDLTKSYGG------FSLevegG----EIREGEVLGIVGPNGIGKTTFAKILAGVLKP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 380 SAGTVSLN----------GVPLDGRTSEWHREHFAAIFADFYLFADVlgeggqhdglearvehyLERLGLaHKVqfVDGR 449
Cdd:COG1245 393 DEGEVDEDlkisykpqyiSPDYDGTVEEFLRSANTDDFGSSYYKTEI-----------------IKPLGL-EKL--LDKN 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 450 LSTtaLSQGQRKRLALLLLMMEDREVFLLDEWAADQD--------PVFRHVfyhellpeLKAAGKTVIAITHDdryfdva 521
Cdd:COG1245 453 VKD--LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRRF--------AENRGKTAMVVDHD------- 515
|
....*...
gi 2733243359 522 drIYRLDY 529
Cdd:COG1245 516 --IYLIDY 521
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
306-529 |
1.97e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 306 ESVTFTEPEQAAAPFRE--LRLSNVHYRYPGqsddfaFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGT 383
Cdd:PRK13409 322 EPIEFEERPPRDESEREtlVEYPDLTKKLGD------FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 384 VSLN----------GVPLDGRTSEWHREHfAAIFADFYLFADVlgeggqhdglearvehyLERLGLAHkvqFVDGRLSTt 453
Cdd:PRK13409 396 VDPElkisykpqyiKPDYDGTVEDLLRSI-TDDLGSSYYKSEI-----------------IKPLQLER---LLDKNVKD- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 454 aLSQGQRKRLALLLLMMEDREVFLLDEWAADQD--------PVFRHVfyhellpeLKAAGKTVIAITHDdryfdvadrIY 525
Cdd:PRK13409 454 -LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRRI--------AEEREATALVVDHD---------IY 515
|
....
gi 2733243359 526 RLDY 529
Cdd:PRK13409 516 MIDY 519
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
348-533 |
2.01e-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: 51.89 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 348 LSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSA---GTVSLNGVPLDGRTSEWH----------------RE--HFAAI 406
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKCvayvrqddillpgltvREtlTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 407 FADFYLFADVLgeggqhdgLEARVEHYLERLgLAHKVqfVDGRLsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQD 486
Cdd:cd03234 108 LRLPRKSSDAI--------RKKRVEDVLLRD-LALTR--IGGNL-VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 487 PvfrHVFYH--ELLPELKAAGKTVIAITHDDR--YFDVADRIYRLDYGQLV 533
Cdd:cd03234 176 S---FTALNlvSTLSQLARRNRIVILTIHQPRsdLFRLFDRILLLSSGEIV 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
343-536 |
2.06e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL-DGRTSEWHREHFAAIFADFYLFADV-LGEG 420
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAKIMREAVAIVPEGRRVFSRMtVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 GQHDGLEARVEHYLERLGLAHKV--QFVDGRLSTTA-LSQGQRKRLALLLLMMEDREVFLLDEWAADQDP-VFRHVFyhE 496
Cdd:PRK11614 101 LAMGGFFAERDQFQERIKWVYELfpRLHERRIQRAGtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPiIIQQIF--D 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2733243359 497 LLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQLVHYD 536
Cdd:PRK11614 179 TIEQLREQGMTIFLVEQNaNQALKLADRGYVLENGHVVLED 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
346-532 |
2.18e-07 |
|
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: 51.77 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGV-----PLDGRTS--------EwhrehfAAIFADF-- 410
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMHKRARlgigylpqE------ASIFRKLtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 411 ----YLFADVLGEGGQhdGLEARVEHYLERLGLAHkvqfVDGRLSTTaLSQGQRKRLALLLLMMEDREVFLLDEWAADQD 486
Cdd:cd03218 93 eeniLAVLEIRGLSKK--EREEKLEELLEEFHITH----LRKSKASS-LSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2733243359 487 PVFRHVFyHELLPELKAAGKTVIAITHDDR-YFDVADRIYRLDYGQL 532
Cdd:cd03218 166 PIAVQDI-QKIIKILKDRGIGVLITDHNVReTLSITDRAYIIYEGKV 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
345-409 |
2.56e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 2.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 345 PIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHREHFAAIFAD 409
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQD 95
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
338-513 |
4.01e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 338 DFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVpldgrtsewhrehfAAifadfyLFADVL 417
Cdd:PRK13545 35 EYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--------------AA------LIAISS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 418 GEGGQHDGLEaRVEHYLERLGLAHK---------VQFVD-GRL---STTALSQGQRKRLALLLLMMEDREVFLLDEWAAD 484
Cdd:PRK13545 95 GLNGQLTGIE-NIELKGLMMGLTKEkikeiipeiIEFADiGKFiyqPVKTYSSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180
....*....|....*....|....*....
gi 2733243359 485 QDPVFRHVFYhELLPELKAAGKTVIAITH 513
Cdd:PRK13545 174 GDQTFTKKCL-DKMNEFKEQGKTIFFISH 201
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
346-540 |
4.28e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.03 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEwHREhFAAIFADFYLF-----ADVLGEG 420
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRD-ICMVFQSYALFphmslGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 GQHDGL-----EARVEHYLERLGLA-HKVQFVDgrlsttALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFy 494
Cdd:PRK11432 103 LKMLGVpkeerKQRVKEALELVDLAgFEDRYVD------QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2733243359 495 HELLPEL-KAAGKTVIAITHDD-RYFDVADRIYRLDYGQLVHYDHATE 540
Cdd:PRK11432 176 REKIRELqQQFNITSLYVTHDQsEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
67-256 |
7.29e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 50.97 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 67 ISQWLLVQIGHRLVYQLRLRLVAkvlgtaleRIERLgSPRIYNA---------LTKDVTTVATAFKQLPISLYNGLLLLT 137
Cdd:cd18564 73 AGTYLTALVGQRVVLDLRRDLFA--------HLQRL-SLSFHDRrrtgdllsrLTGDVGAIQDLLVSGVLPLLTNLLTLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 138 G-LAYMAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLT---EQFEAAIdgRCELGLSRERRHllyRHR 213
Cdd:cd18564 144 GmLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALAsvaQESLSAI--RVVQAFGREEHE---ERR 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2733243359 214 LEPVASASLAASVRAdTLWAVNLNWTTLLVfVLIGTLFFLGQG 256
Cdd:cd18564 219 FARENRKSLRAGLRA-ARLQALLSPVVDVL-VAVGTALVLWFG 259
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
343-524 |
8.35e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.24 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLdGRTSEWHR------EHFaAIFADFYLFADV 416
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRkvgfvfQHY-ALFRHMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 417 -LG-------EGGQHDGLEARVEHYLERLGLAHKVQfvdgRLSTTaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPV 488
Cdd:PRK10851 96 aFGltvlprrERPNAAAIKAKVTQLLEMVQLAHLAD----RYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2733243359 489 FR---HVFYHELLPELKAagkTVIAITHD-DRYFDVADRI 524
Cdd:PRK10851 171 VRkelRRWLRQLHEELKF---TSVFVTHDqEEAMEVADRV 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
345-541 |
9.19e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 345 PIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRT---------------------------SE 397
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdairagimlcpedrkaegiipvhsvAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 398 ----WHREHFaaIFADFYLfadvlgeggqHDGLEAR-VEHYLERLglahKVQFVDGRLSTTALSQGQRKRLALLLLMMED 472
Cdd:PRK11288 351 niniSARRHH--LRAGCLI----------NNRWEAEnADRFIRSL----NIKTPSREQLIMNLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 473 REVFLLDEWAADQDPVFRHVFYHeLLPELKAAGKTVIAITHD-DRYFDVADRIYRLDYGQL---VHYDHATES 541
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYN-VIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRIageLAREQATER 486
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
293-528 |
1.29e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.96 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 293 HVALQAIDALALGESvTFTEPEQAAAPFRELRLsnvhyrypgQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKL 372
Cdd:COG4178 339 EEALEAADALPEAAS-RIETSEDGALALEDLTL---------RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 373 MTGLYQPSAGTVSLngvPLDGRTsewhrehfaaifadfyLF------------ADVL---GEGGQHDglEARVEHYLERL 437
Cdd:COG4178 409 IAGLWPYGSGRIAR---PAGARV----------------LFlpqrpylplgtlREALlypATAEAFS--DAELREALEAV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 438 GLAHKVqfvdGRLSTTA-----LSQGQRKRLAL--LLLMMEDreVFLLDEWAADQDPVFRHVFYHELLPELKAAgkTVIA 510
Cdd:COG4178 468 GLGHLA----ERLDEEAdwdqvLSLGEQQRLAFarLLLHKPD--WLFLDEATSALDEENEAALYQLLREELPGT--TVIS 539
|
250
....*....|....*...
gi 2733243359 511 ITHDDRYFDVADRIYRLD 528
Cdd:COG4178 540 VGHRSTLAAFHDRVLELT 557
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
346-540 |
1.60e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.51 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG-----VPLDGRTSE--WHREHFAAIFADFYLFADVLG 418
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARARRgiGYLPQEASIFRRLSVYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 EGGQHDGL-----EARVEHYLERLGLAHKVQFVDgrlstTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVfRHVF 493
Cdd:PRK10895 102 VLQIRDDLsaeqrEDRANELMEEFHIEHLRDSMG-----QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI-SVID 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2733243359 494 YHELLPELKAAGKTVIAITHDDR-YFDVADRIYRLDYGQLVHYDHATE 540
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
345-395 |
3.91e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.63 E-value: 3.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2733243359 345 PIDLSIRRGElIFVVGG-NGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRT 395
Cdd:COG1129 270 DVSFSVRAGE-ILGIAGlVGAGRTELARALFGADPADSGEIRLDGKPVRIRS 320
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
63-195 |
4.67e-06 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 48.57 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISL-YNGLLLLTGLAY 141
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLvRDPLTVIGLLGV 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDG 195
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSG 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
337-524 |
4.84e-06 |
|
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: 49.16 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 337 DDFAFQLGPidlsirrGELIFVVGGNGSGKSTLAKLMTGLYQPSAG------TVSLNGV-----PLDGRTSEWhrehfaa 405
Cdd:TIGR03719 339 DDLSFKLPP-------GGIVGVIGPNGAGKSTLFRMITGQEQPDSGtieigeTVKLAYVdqsrdALDPNKTVW------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 406 ifadfylfaDVLGEGGQH---DGLEARVEHYLERLGL--AHKVQFVDgrlsttALSQGQRKRLALLLLMMEDREVFLLDE 480
Cdd:TIGR03719 405 ---------EEISGGLDIiklGKREIPSRAYVGRFNFkgSDQQKKVG------QLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2733243359 481 WAADQDPvfrhvfyhELLPELKAA-----GKTVIaITHdDRYFdvADRI 524
Cdd:TIGR03719 470 PTNDLDV--------ETLRALEEAllnfaGCAVV-ISH-DRWF--LDRI 506
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-513 |
5.43e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.63 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQSDDFAFQLGpidLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSEWHRE- 401
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLC---VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNm 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 402 ----HFAAI------FADFYLFADVLGEGGQHdgLEARVEHYLERLGLAhkvQFVDgRLSTTaLSQGQRKRLALLLLMME 471
Cdd:TIGR01257 2015 gycpQFDAIddlltgREHLYLYARLRGVPAEE--IEKVANWSIQSLGLS---LYAD-RLAGT-YSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2733243359 472 DREVFLLDEWAADQDPVFRHVFYHELLPELKaAGKTVIAITH 513
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSH 2128
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
352-528 |
6.70e-06 |
|
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: 46.21 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 352 RGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVslngvpldgrtsewhrehfaaifadFYLFADVLgeggqhdglearve 431
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------IYIDGEDI-------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 432 hyleRLGLAHKVQFVDGRLSTTALSQGQRKRLALLLLMMEDREVFLLDEW-----AADQDPVFRHVFYHELLPELKAAGK 506
Cdd:smart00382 42 ----LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEItslldAEQEALLLLLEELRLLLLLKSEKNL 117
|
170 180
....*....|....*....|..
gi 2733243359 507 TVIAITHDDRYFDVADRIYRLD 528
Cdd:smart00382 118 TVILTTNDEKDLGPALLRRRFD 139
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
322-391 |
7.81e-06 |
|
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: 48.66 E-value: 7.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 322 ELRLSNVHYRYPGQSDdfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL 391
Cdd:COG5265 357 EVRFENVSFGYDPERP----ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI 422
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
343-544 |
8.24e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.75 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG-VPLDGRTSeW-----HREHFaaIFA---DFYLF 413
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQTS-WimpgtIKDNI--IFGlsyDEYRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 414 ADVLGeggqhdglEARVEHYLERLGLAHKVQFVDGRLSttaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVF 493
Cdd:TIGR01271 519 TSVIK--------ACQLEEDIALFPEKDKTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 494 YHELLPELkAAGKTVIAITHDDRYFDVADRIYRLDYGqlVHYDHATESPFQ 544
Cdd:TIGR01271 588 FESCLCKL-MSNKTRILVTSKLEHLKKADKILLLHEG--VCYFYGTFSELQ 635
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
343-535 |
9.12e-06 |
|
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: 47.54 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG-VPLDGRTSeW-----HREH-FAAIFADFYLFAD 415
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQFS-WimpgtIKENiIFGVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 416 VLGeggqhdglEARVEHYLERLGLAHKVQFVDGRLSttaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYH 495
Cdd:cd03291 132 VVK--------ACQLEEDITKFPEKDNTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2733243359 496 ELLPELkAAGKTVIAITHDDRYFDVADRIYRLDYGQLVHY 535
Cdd:cd03291 201 SCVCKL-MANKTRILVTSKMEHLKKADKILILHEGSSYFY 239
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
289-534 |
9.57e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 289 VIRGHVALQAIDALaLGESVTFTEPEQAAAPFR-ELRLSNVHYRYPGQSDDfafQLGPIDLSIRRGELIFVVGGNGSGKS 367
Cdd:PRK10789 280 VERGSAAYSRIRAM-LAEAPVVKDGSEPVPEGRgELDVNIRQFTYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 368 TLAKLMTGLYQPSAGTVSLNGVPL-DGRTSEWhREHFAAIFADFYLFADVLGEG---GQHDGLEARVEHyLERLGLAHK- 442
Cdd:PRK10789 356 TLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSW-RSRLAVVSQTPFLFSDTVANNialGRPDATQQEIEH-VARLASVHDd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 443 -VQFVDGRLSTTA-----LSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELlpELKAAGKTVIAITHDDR 516
Cdd:PRK10789 434 iLRLPQGYDTEVGergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLS 511
|
250
....*....|....*...
gi 2733243359 517 YFDVADRIYRLDYGQLVH 534
Cdd:PRK10789 512 ALTEASEILVMQHGHIAQ 529
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
323-480 |
1.06e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.92 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 323 LRLSNVHYRYPGQsddfAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSlngvpLDGR---TSEWH 399
Cdd:PRK11650 4 LKLQAVRKSYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW-----IGGRvvnELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 400 REHFAAIFADFYLF-----ADVLGEGGQHDGL-----EARVEHYLERLGLAhkvQFVDGRlsTTALSQGQRKRLALLLLM 469
Cdd:PRK11650 75 DRDIAMVFQNYALYphmsvRENMAYGLKIRGMpkaeiEERVAEAARILELE---PLLDRK--PRELSGGQRQRVAMGRAI 149
|
170
....*....|.
gi 2733243359 470 MEDREVFLLDE 480
Cdd:PRK11650 150 VREPAVFLFDE 160
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
323-388 |
1.16e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2733243359 323 LRLSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNG 388
Cdd:PRK10762 5 LQLKGIDKAFPGVK-----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG 65
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-533 |
1.35e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.83 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQ--PSA---GTVSLNGVPLDGRTSEWHREHFAAIFA------DFY 411
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQipnpipNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 412 LFADV-LGEG-----GQHDGLEARVEHYLERLGLAHKVQfvdGRLSTTA--LSQGQRKRLALLLLMMEDREVFLLDEWAA 483
Cdd:PRK14247 99 IFENVaLGLKlnrlvKSKKELQERVRWALEKAQLWDEVK---DRLDAPAgkLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2733243359 484 DQDPVfRHVFYHELLPELKAAgKTVIAITH-DDRYFDVADRIYRLDYGQLV 533
Cdd:PRK14247 176 NLDPE-NTAKIESLFLELKKD-MTIVLVTHfPQQAARISDYVAFLYKGQIV 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-533 |
1.56e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 333 PGQSDDFaFQLGP------IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTV----SLNGVPldgrTSEWhreH 402
Cdd:PTZ00243 661 KMKTDDF-FELEPkvllrdVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIAYVP----QQAW---I 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 403 FAAIFADFYLFADVLGEGGQHDGLeaRVEHylerlgLAHKVQFVDGRLST------TALSQGQRKRLALLLLMMEDREVF 476
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAV--RVSQ------LEADLAQLGGGLETeigekgVNLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 477 LLDEWAADQDP-VFRHVFYHELLPELkaAGKTVIAITHDDRYFDVADRIYRLDYGQLV 533
Cdd:PTZ00243 805 LLDDPLSALDAhVGERVVEECFLGAL--AGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
359-532 |
1.70e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 359 VGGNGSGKSTLAKLMTGLYQPSAGTVSL-NGVPLdGRTSE----------------WHREHFA------AIFA------- 408
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLdPNERL-GKLRQdqfafeeftvldtvimGHTELWEvkqerdRIYAlpemsee 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 409 DFYLFADVLGEGGQHDGL--EARVEHYLerLGLAHKVQFVDGRLSttALSQGQRKRLALLLLMMEDREVFLLDE------ 480
Cdd:PRK15064 112 DGMKVADLEVKFAEMDGYtaEARAGELL--LGVGIPEEQHYGLMS--EVAPGWKLRVLLAQALFSNPDILLLDEptnnld 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 481 -----WAADqdpvfrhvfyhellpELKAAGKTVIAITHdDRYF------DVADriyrLDYGQL 532
Cdd:PRK15064 188 intirWLED---------------VLNERNSTMIIISH-DRHFlnsvctHMAD----LDYGEL 230
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
63-279 |
1.95e-05 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 46.48 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQ-LPISLYNGLLLLTGLAY 141
Cdd:pfam00664 56 ILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEkLGLLFQSLATIVGGIIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDG----RCELGLSRERRHllYRHRLEPV 217
Cdd:pfam00664 136 MFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGirtvKAFGREEYELEK--YDKALEEA 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2733243359 218 asasLAASVRADTLWAVNLNWTTLLVFVLIGTLFFLGQGL---GLLDQQVVVGYVLAIMFLRTPI 279
Cdd:pfam00664 214 ----LKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLvisGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
70-181 |
2.02e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 46.71 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 70 WLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAF-KQLPISLYNGLLLLTGLAYMAWLSVP 148
Cdd:cd18575 58 YLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVgSSLSIALRNLLLLIGGLVMLFITSPK 137
|
90 100 110
....*....|....*....|....*....|...
gi 2733243359 149 FFVLTLGVIALGVGLDILLGRKIKALMRAVRQR 181
Cdd:cd18575 138 LTLLVLLVIPLVVLPIILFGRRVRRLSRASQDR 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
347-386 |
5.35e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 5.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2733243359 347 DLSIR--RGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSL 386
Cdd:PRK11819 342 DLSFSlpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
346-480 |
5.82e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTV--SLNGVPldGRTSEWHREHFAaifADFYLFaDVLGEGGQH 423
Cdd:PRK15064 338 LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANI--GYYAQDHAYDFE---NDLTLF-DWMSQWRQE 411
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 424 DGLEARVEHYLERLGLAHKvqfvDGRLSTTALSQGQRKRLALLLLMMEDREVFLLDE 480
Cdd:PRK15064 412 GDDEQAVRGTLGRLLFSQD----DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
343-389 |
7.31e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.96 E-value: 7.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGV 389
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ 77
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
346-410 |
1.12e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTG--LYQPSAGTVSLNGVPLDGRTSEwHREHfAAIFADF 410
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPE-ERAH-LGIFLAF 90
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
333-516 |
1.13e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 333 PGQSDDFAFQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGvpldgrtsewhrehfaaifaDFYL 412
Cdd:PRK13546 30 PKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------------------EVSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 413 FADVLGEGGQHDGLEaRVEHYLERLGLAHK---------VQFVD-GRL---STTALSQGQRKRLALLLLMMEDREVFLLD 479
Cdd:PRK13546 90 IAISAGLSGQLTGIE-NIEFKMLCMGFKRKeikamtpkiIEFSElGEFiyqPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 2733243359 480 EWAADQDPVFRHVFYHELLpELKAAGKTVIAITHDDR 516
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIY-EFKEQNKTIFFVSHNLG 204
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
63-181 |
1.33e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 44.01 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALE-----RIERLGSpRIYNaltkDVTTVATAFKQ-LPISLYNGLLLL 136
Cdd:cd18576 51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSffherRVGELTS-RLSN----DVTQIQDTLTTtLAEFLRQILTLI 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2733243359 137 TGLAYMAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQR 181
Cdd:cd18576 126 GGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDE 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
346-377 |
1.51e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 1.51e-04
10 20 30
....*....|....*....|....*....|..
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLY 377
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY 55
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-397 |
2.49e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 2.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733243359 325 LSNVHYRYPGQSddfafQLGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLDGRTSE 397
Cdd:PRK10982 1 MSNISKSFPGVK-----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK 68
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
275-534 |
2.97e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 275 LRTPISVILDAVPAVIRGHVALQAIDALALGESVTFT-----EPEQAAapfreLRLSNVHYRYPGQSDDFAfqLGPIDLS 349
Cdd:PLN03130 567 LRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLpnpplEPGLPA-----ISIKNGYFSWDSKAERPT--LSNINLD 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 350 IRRGELIFVVGGNGSGKSTLAKLMTGLYQP-SAGTVSLNG----VPldgrTSEWhreHFAAIFADFYLFadvlgeGGQHD 424
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGtvayVP----QVSW---IFNATVRDNILF------GSPFD 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 425 glEARVEHYLERLGLAHKVQFVDGRLST------TALSQGQRKRLALLLLMMEDREVFLLDEWAADQDP-VFRHVFYHEL 497
Cdd:PLN03130 707 --PERYERAIDVTALQHDLDLLPGGDLTeigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCI 784
|
250 260 270
....*....|....*....|....*....|....*..
gi 2733243359 498 LPELKaaGKTVIAITHDDRYFDVADRIYrldygqLVH 534
Cdd:PLN03130 785 KDELR--GKTRVLVTNQLHFLSQVDRII------LVH 813
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
326-384 |
3.46e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 3.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2733243359 326 SNVHYRYPGQSDDFAFQLGPIDLSIRrgelIFVVGGNGSGKSTLAKLMTGLYQPSAGTV 384
Cdd:PLN03073 512 SDASFGYPGGPLLFKNLNFGIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
63-293 |
3.96e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 42.55 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTV-ATAFKQLPISLYNGLLLLTGLAY 141
Cdd:cd18557 51 VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLII 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQFEAAIDG-RCELGLSRERRHL-LYRHRLEpvas 219
Cdd:cd18557 131 LFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNiRTVRSFSAEEKEIrRYSEALD---- 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2733243359 220 ASLAASVRADTLWAVNLNWTTLLVFVLIGTLFFLGQGLgLLDQQVVVG----YVLAIMFLRTPISVILDAVPAVIRGH 293
Cdd:cd18557 207 RSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYL-VLSGQLTVGeltsFILYTIMVASSVGGLSSLLADIMKAL 283
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
346-409 |
4.10e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.77 E-value: 4.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPL-DGRTSEWH--REHFAAIFAD 409
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDEWRavRSDIQMIFQD 106
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
343-488 |
4.20e-04 |
|
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: 43.36 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQpSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADV------ 416
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTfrknld 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 417 ---------LGEGGQHDGLEARVEHYLERLGLahkvQFVDGrlsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDP 487
Cdd:TIGR01271 1314 pyeqwsdeeIWKVAEEVGLKSVIEQFPDKLDF----VLVDG---GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
.
gi 2733243359 488 V 488
Cdd:TIGR01271 1387 V 1387
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
343-535 |
4.43e-04 |
|
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: 41.48 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGL----YQPSaGTVSLNGVPLDGRTSEWHREhfaAIFAdfylfadvlG 418
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYKEFAEKYPGE---IIYV---------S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 419 EGGQHDGlEARVEHYLERLGLAHKVQFVDGrlsttaLSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFYHELL 498
Cdd:cd03233 90 EEDVHFP-TLTVRETLDFALRCKGNEFVRG------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 2733243359 499 PELKAAGKTVIAITH--DDRYFDVADRIYRLDYGQLVHY 535
Cdd:cd03233 163 TMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQIYY 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
343-384 |
5.97e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 41.64 E-value: 5.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTV 384
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI 61
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
346-536 |
9.88e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.38 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQpSAGTVSLNGVPLDGRTSEWHREHFAAIFADFYLFADVLGEG----G 421
Cdd:cd03289 23 ISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNldpyG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 422 QHD-----------GLEARVEHYLERLGLahkvQFVDGrlsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFR 490
Cdd:cd03289 102 KWSdeeiwkvaeevGLKSVIEQFPGQLDF----VLVDG---GCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2733243359 491 HVFYHELLPELkaAGKTVIAITHDDRYFDVADRIYRLDYGQLVHYD 536
Cdd:cd03289 175 QVIRKTLKQAF--ADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
321-415 |
9.97e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 321 RELRLSNVHYRYPGQSDDFAFQlgPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGV-PLDGRTSEWH 399
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRKDVEIYK--DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWW 458
|
90
....*....|....*.
gi 2733243359 400 REHFAAIFADFYLFAD 415
Cdd:PTZ00265 459 RSKIGVVSQDPLLFSN 474
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
346-377 |
1.31e-03 |
|
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: 41.35 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|..
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLY 377
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVY 51
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
346-377 |
1.42e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|..
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLY 377
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSGVY 51
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-533 |
1.56e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.60 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQ--PSA---GTVSLNGV--------PLDGRTSEWHREHFAAIFADFYL 412
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRniyspdvdPIEVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 413 FADVL------GEGGQHDGLEARVEHYLERLGLAHKVQfvdGRLSTTA--LSQGQRKRLALLLLMMEDREVFLLDEWAAD 484
Cdd:PRK14267 103 YDNVAigvklnGLVKSKKELDERVEWALKKAALWDEVK---DRLNDYPsnLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2733243359 485 QDPVFRHVFyHELLPELKAAgKTVIAITHDD-RYFDVADRIYRLDYGQLV 533
Cdd:PRK14267 180 IDPVGTAKI-EELLFELKKE-YTIVLVTHSPaQAARVSDYVAFLYLGKLI 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
346-385 |
1.95e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 1.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVS 385
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
343-480 |
2.07e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 343 LGPIDLSIRRGELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSL-NGVPLdGRTSEWHREhfaaifadfYLFADvlgEGG 421
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKL-GYFAQHQLE---------FLRAD---ESP 394
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733243359 422 -QH------DGLEARVEHYLERLGL-AHKVQFVDGRLSTtalsqGQRKRLALLLLMMEDREVFLLDE 480
Cdd:PRK10636 395 lQHlarlapQELEQKLRDYLGGFGFqGDKVTEETRRFSG-----GEKARLVLALIVWQRPNLLLLDE 456
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
65-188 |
2.34e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 40.16 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 65 GVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQ-LPISLYNGLLLLTGLAYMA 143
Cdd:cd18550 56 GVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGtLTSVVSNVVTLVATLVAML 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2733243359 144 WLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLTEQ 188
Cdd:cd18550 136 ALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSI 180
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
63-186 |
3.45e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 39.69 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQ-LPISLYNGLLLLTGLAY 141
Cdd:cd18548 54 IAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMlLRMLVRAPIMLIGAIIM 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2733243359 142 MAWLSVPF---FVLTLGVIALGVgldILLGRKIKALMRAVRQRDDQLT 186
Cdd:cd18548 134 AFRINPKLaliLLVAIPILALVV---FLIMKKAIPLFKKVQKKLDRLN 178
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
353-524 |
4.39e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.84 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 353 GELIFVVGGNGSGKSTLAKLMTGLYQPSAGTVSLNGVPLD---GRTSEWHREHFAAIFADFYLFAD---VLGEG------ 420
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQDPYASLDprqTVGDSimeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 421 ----GQHDGLEARVEHYLERLGL--AHKVQFvdgrlsTTALSQGQRKRLALLLLMMEDREVFLLDEWAADQDPVFRHVFY 494
Cdd:PRK10261 430 vhglLPGKAAAARVAWLLERVGLlpEHAWRY------PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190
....*....|....*....|....*....|
gi 2733243359 495 HELLPELKAAGKTVIAITHDdryFDVADRI 524
Cdd:PRK10261 504 NLLLDLQRDFGIAYLFISHD---MAVVERI 530
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-395 |
4.80e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.91 E-value: 4.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 346 IDLSIRRGELIFVVGGNGSGKS-----TLAKLMTGLYQpSAGTVSLNGVP-----LDGRT 395
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPvapcaLRGRK 80
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
70-186 |
7.11e-03 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 38.65 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 70 WLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQ-LPISLYNGLLLLTGLAYMAWLSVP 148
Cdd:cd18573 63 YLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQnLSDGLRSLVSGVGGIGMMLYISPK 142
|
90 100 110
....*....|....*....|....*....|....*...
gi 2733243359 149 FFVLTLGVIALGVGLDILLGRKIKALMRAVRQRDDQLT 186
Cdd:cd18573 143 LTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADAT 180
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
63-181 |
9.02e-03 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 38.14 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733243359 63 ISGVISQWLLVQIGHRLVYQLRLRLVAKVLGTALERIERLGSPRIYNALTKDVTTVATAFKQLPISLYNGLLLLTG-LAY 141
Cdd:cd18544 56 LLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGiLIA 135
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2733243359 142 MAWLSVPFFVLTLGVIALGVGLDILLGRKIKALMRAVRQR 181
Cdd:cd18544 136 MFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREK 175
|
|
| |
