|
Name |
Accession |
Description |
Interval |
E-value |
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-577 |
0e+00 |
|
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: 528.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 2 ANFIRLLKLCRPHYKAMLLGTFLASLTVLANVGLLAISGWFLASMAAAGIAsvhMNYFTPAGTIRFLAIVRTASRYAERL 81
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPI---LNLFVPIVGVRAFAIGRTVFRYLERL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 82 VTHNATFLLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNV 161
Cdd:COG4987 78 VSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 162 ALICFVGIIIIGVIIPAILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDLLSEQYNQQLFIRHK 241
Cdd:COG4987 158 ALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 242 ALGNADGLSLLIVQLAMLSSIVTIVPLVFSGAMVNVELAMLSLFVLASFESVLLLPNAFIELPYVLKAAERLFILEDKTL 321
Cdd:COG4987 238 LSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 322 STNNVSTTdiELLNKHWALSLNNVSYHY--GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQ 399
Cdd:COG4987 318 AVTEPAEP--APAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 400 SdkeiISLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRN 479
Cdd:COG4987 396 G----VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 480 VSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQG 559
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
570
....*....|....*...
gi 1949233634 560 SHQQLLNEHPDYVALTTR 577
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-578 |
1.85e-129 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 390.73 E-value: 1.85e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 1 MANFIRLLKLCRPHYKAMLLGTFLASLTVLANVGLLAISGWFLASMAAAGIASVHM-NYFTPAGTIRFLAIVRTASRYAE 79
Cdd:PRK11160 1 MRALLPFLKLYKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSfNYMLPAAGVRGAAIGRTAGRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 80 RLVTHNATFLLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNV 159
Cdd:PRK11160 81 RLVSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 160 NVALICFVGIIIIGVIIPAILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDllseQYNQQLFIR 239
Cdd:PRK11160 161 TLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLE----QTEQQWLAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 240 HKALGNADGLSLLIVQLAmlSSIVTIVPLVFSGAMVNVEL---AMLSLFV---LASFESVLLLPNAFIELPYVLKAAERL 313
Cdd:PRK11160 237 QRRQANLTGLSQALMILA--NGLTVVLMLWLAAGGVGGNAqpgALIALFVfaaLAAFEALMPVAGAFQHLGQVIASARRI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 314 FILEDKTLSTNNVSTTDIEllNKHWALSLNNVSYHY--GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPL 391
Cdd:PRK11160 315 NEITEQKPEVTFPTTSTAA--ADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 392 QQGTINLqSDKEIislHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGwFSELKQGLKT 471
Cdd:PRK11160 393 QQGEILL-NGQPI---ADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEK-LLEDDKGLNA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 472 RLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLD 551
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMD 547
|
570 580
....*....|....*....|....*..
gi 1949233634 552 SGQIIAQGSHQQLLNEHPDYVALTTRF 578
Cdd:PRK11160 548 NGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-538 |
1.05e-107 |
|
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: 333.17 E-value: 1.05e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 6 RLLKLCRPHYKAMLLGTFLASLTVLANVGLLAISGWFLAsmaAAGIASVHMNYFTPAGTIRFLAIVRTASRYAERLVTHN 85
Cdd:TIGR02868 3 RILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLIS---RAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 86 ATFLLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALIC 165
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 166 FVGIIIIGVIIPAIlSKQLDKNSHQ-ETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDLLSEQYNQQLFIRHKALG 244
Cdd:TIGR02868 160 AAGLLLAGFVAPLV-SLRAARAAEQaLARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 245 NADGLSLLIVQLAMLSSIVTIVPLVFSGAMVNVELAMLSLFVLASFESVLLLPNAFIELPYVLKAAERLF-ILEDKTLST 323
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVeVLDAAGPVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 324 NNVSTTDIELLNKHWALSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdk 402
Cdd:TIGR02868 319 EGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG-- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 403 eiISLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQ 482
Cdd:TIGR02868 397 --VPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 483 GQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDP 538
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-571 |
1.99e-93 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 297.85 E-value: 1.99e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 1 MANFIRLLKLCRPHYKAMLLGTFLASLTVLANVGLLAISGWFLAsmaaAGIASVHMNYFTPAGTIRF-LAIVRTASRYAE 79
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIID----ALLAGGDLSALLLLLLLLLgLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 80 RLVTHNATFLLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNV 159
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 160 NVALICFVGIIIIGVIIpAILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDLLSEQYNQQLFIR 239
Cdd:COG1132 162 RLALIVLLVLPLLLLVL-RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 240 HKALGNADGLSLLIVQLAMLSSIVTIVPLVFSGAMVNVELAMLSLFVLASFESVLLLPNAFIELPYVLKAAERLFILEDK 319
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 320 TLSTNNVSTTdIELLNKHWALSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInl 398
Cdd:COG1132 321 PPEIPDPPGA-VPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI-- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 399 qsdkEI--ISLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTG 476
Cdd:COG1132 398 ----LIdgVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 477 GRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQII 556
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570
....*....|....*
gi 1949233634 557 AQGSHQQLLNEHPDY 571
Cdd:COG1132 554 EQGTHEELLARGGLY 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-569 |
1.25e-82 |
|
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: 268.93 E-value: 1.25e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 6 RLLKLCRPHYKAMLLGTFLASLTVLANVGLLAISGWFLASMAAAGIASVHMnyFTPAGTIRFLAIVRTASRYAERLVTHN 85
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSAL--LPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 86 ATFLLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALIC 165
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 166 FVGIiiigviiPAI----------LSKQLDKNSHQETLLSAQLraelSDTLTGLRELNIYQARNQQLTKCDLLSEQYnqq 235
Cdd:COG4988 165 LVTA-------PLIplfmilvgkgAAKASRRQWRALARLSGHF----LDRLRGLTTLKLFGRAKAEAERIAEASEDF--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 236 lfiRHKALgnadglSLLIVQL---------AMLSSIVTIVPLVFSgaMVNVELAMLS-LFVLasfesvLLLPNAFIELPY 305
Cdd:COG4988 231 ---RKRTM------KVLRVAFlssavleffASLSIALVAVYIGFR--LLGGSLTLFAaLFVL------LLAPEFFLPLRD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 306 V----------LKAAERLFILEDKTLSTNNVSTTDIELlNKHWALSLNNVSYHYGQ-KQALNNVSFELPAKQKVAIVGRS 374
Cdd:COG4988 294 LgsfyharangIAAAEKIFALLDAPEPAAPAGTAPLPA-AGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 375 GSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALT 454
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILING----VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 455 QAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI 534
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILI 528
|
570 580 590
....*....|....*....|....*....|....*
gi 1949233634 535 THDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHP 569
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
27-314 |
1.93e-81 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 257.02 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 27 LTVLANVGLLAISGWFLASMAAAGIASVHMNYFTPAGTIRFLAIVRTASRYAERLVTHNATFLLLSEIRVNMFATLSKLN 106
Cdd:cd18585 3 LTLLASIGLLALSGWFISAAALAGLAAPTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEPLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 107 NLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALICFVGIIIIGVIIPAILSKQLDK 186
Cdd:cd18585 83 PARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 187 NSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDLLSEQY--NQQLFIRHKALGNAdgLSLLIVQLAMLSSIVT 264
Cdd:cd18585 163 IGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALikEQRRLARLSGLSQA--LMILLSGLTVWLVLWL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1949233634 265 IVPLVFSGAMVNVELAMLSLFVLASFESVLLLPNAFIELPYVLKAAERLF 314
Cdd:cd18585 241 GAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-574 |
8.75e-77 |
|
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: 257.07 E-value: 8.75e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 4 FIRLLKLCRPHYKAMLLGTFLASLTVLA----------------NVGLLaisgWFLAS-MAAAGIASVHMNYftpagtIR 66
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALAtplftqvvidrvlpnqDLSTL----WVLAIgLLLALLFEGLLRL------LR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 67 FLAIVRTASRyaerlvthnatflLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQnDVDALDKFYLNVLLPMLVALLT 146
Cdd:COG2274 217 SYLLLRLGQR-------------IDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 147 VPIIMLFMSAYNVNVALICFVGIIIIGVIIpAILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCD 226
Cdd:COG2274 283 VLIFLIVLFFYSPPLALVVLLLIPLYVLLG-LLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 227 LLSEQYNQQLFiRHKALGN-ADGLSLLIVQLAMLSSIVTIVPLVFS-----GAMVNVElaMLSLFVLASFESvllLPNAF 300
Cdd:COG2274 362 NLLAKYLNARF-KLRRLSNlLSTLSGLLQQLATVALLWLGAYLVIDgqltlGQLIAFN--ILSGRFLAPVAQ---LIGLL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 301 IELPYVLKAAERLF-ILEDKTLSTNNVSTTDIELLNKHwaLSLNNVSYHYGQ--KQALNNVSFELPAKQKVAIVGRSGSG 377
Cdd:COG2274 436 QRFQDAKIALERLDdILDLPPEREEGRSKLSLPRLKGD--IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 378 KTTLVNLLSSLWPLQQGTINLqsDKeiISLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAE 457
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILI--DG--IDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAG 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 458 LGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHD 537
Cdd:COG2274 590 LHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHR 669
|
570 580 590
....*....|....*....|....*....|....*..
gi 1949233634 538 PALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVAL 574
Cdd:COG2274 670 LSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-548 |
1.16e-54 |
|
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: 193.66 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 12 RPHYKAMLLGtFLASLTVLANVGLLA--ISGWFLASMAAAGIAsvhmnyfTPAGTIRFLAIVRTASRYAERLVTHNATFL 89
Cdd:TIGR02857 3 RALALLALLG-VLGALLIIAQAWLLArvVDGLISAGEPLAELL-------PALGALALVLLLRALLGWLQERAAARAAAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 90 LLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFY--------LNVLLPMLVA--------------LLTV 147
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFarylpqlvLAVIVPLAILaavfpqdwisglilLLTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 148 PIIMLFMsaynvnvALIcfvgiiiigviipaiLSKQLDKNSHQETLLSaQLRAELSDTLTGLRELNIYQARNQQLTKCDL 227
Cdd:TIGR02857 155 PLIPIFM-------ILI---------------GWAAQAAARKQWAALS-RLSGHFLDRLRGLPTLKLFGRAKAQAAAIRR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 228 LSEQYnqqlfiRHKALGnadglsllIVQLAMLSSIVTIVPLVFSGAMVNVELAMLSLF-VLASFES--VLLL-PNAFIEL 303
Cdd:TIGR02857 212 SSEEY------RERTMR--------VLRIAFLSSAVLELFATLSVALVAVYIGFRLLAgDLDLATGlfVLLLaPEFYLPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 304 PYV----------LKAAERLF-ILEDKTLSTNN---VSTTDIellnkhWALSLNNVSYHY-GQKQALNNVSFELPAKQKV 368
Cdd:TIGR02857 278 RQLgaqyharadgVAAAEALFaVLDAAPRPLAGkapVTAAPA------SSLEFSGVSVAYpGRRPALRPVSFTVPPGERV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 369 AIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQ 448
Cdd:TIGR02857 352 ALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG----VPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAE 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 449 MIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH 528
Cdd:TIGR02857 428 IREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG 507
|
570 580
....*....|....*....|
gi 1949233634 529 ASVLTITHDPALLSQMDSVI 548
Cdd:TIGR02857 508 RTVLLVTHRLALAALADRIV 527
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
340-574 |
5.22e-52 |
|
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: 177.81 E-value: 5.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQ--ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLNNEsra 416
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhDVRDYTLASLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 ktLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQ 496
Cdd:cd03251 78 --IGLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 497 KPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVAL 574
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-574 |
1.87e-49 |
|
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: 180.30 E-value: 1.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 4 FIRLLKLCRPhYKAMLLgtflasLTVLANVGLLAISGWFLASMA-----AAGIASVHMNYFTPAGTIrFLAIVRTASRYA 78
Cdd:TIGR02203 2 FRRLWSYVRP-YKAGLV------LAGVAMILVAATESTLAALLKpllddGFGGRDRSVLWWVPLVVI-GLAVLRGICSFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 79 ERLVTHNATFLLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYN 158
Cdd:TIGR02203 74 STYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 159 VNVALICFVGIIIIGVIIPAIlSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDllseQYNQQLFI 238
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRV-SKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD----AVSNRNRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 239 RHKALGNADGLSLLIVQLAMLSSIVTIVPLVFS---------GAMVNVELAMLSLFvlasfESVLLLPNAFIELPYVLKA 309
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFqaqagsltaGDFTAFITAMIALI-----RPLKSLTNVNAPMQRGLAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 310 AERLFILEDktlSTNNVSTTDIELLNKHWALSLNNVSYHYG--QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSS 387
Cdd:TIGR02203 304 AESLFTLLD---SPPEKDTGTRAIERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 388 LWPLQQGTINLQSDK-EIISLHDLNNEsraktLNILAQQHHIFDGTLSENLAYAAP-DATSQQMIAALTQAELGGWFSEL 465
Cdd:TIGR02203 381 FYEPDSGQILLDGHDlADYTLASLRRQ-----VALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 466 KQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMD 545
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
570 580
....*....|....*....|....*....
gi 1949233634 546 SVIWLDSGQIIAQGSHQQLLNEHPDYVAL 574
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
342-577 |
6.20e-48 |
|
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: 166.95 E-value: 6.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQK---QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKeiisLHDLNNESRAKT 418
Cdd:cd03249 3 FKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD----IRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKP 498
Cdd:cd03249 79 IGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVALTTR 577
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
340-554 |
1.07e-47 |
|
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: 164.09 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYG--QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAK 417
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG----VDLRDLDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIFDGTLSENLayaapdatsqqmiaaltqaelggwfselkqglktrlgtggrnVSQGQSRRIALAQALLQK 497
Cdd:cd03228 77 NIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQ 554
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
339-559 |
4.30e-47 |
|
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: 164.30 E-value: 4.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHY-GQKQ-ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLNnesr 415
Cdd:cd03245 2 RIEFRNVSFSYpNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtDIRQLDPADLR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 aKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALL 495
Cdd:cd03245 78 -RNIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 496 QKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQG 559
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
352-568 |
7.86e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.11 E-value: 7.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 352 KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQqGTINLQSdkeiISLHDLNNESRAKTLNILAQQHHIFDG 431
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKING----IELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 432 TLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLD 511
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 512 NISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEH 568
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
340-574 |
3.17e-46 |
|
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: 162.40 E-value: 3.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ-KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNneSRAKT 418
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI--DGQDIREVTLD--SLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKP 498
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVAL 574
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
343-565 |
4.52e-46 |
|
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: 162.01 E-value: 4.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 343 NNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKTLNI 421
Cdd:cd03254 6 ENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG----IDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 422 LAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAIL 501
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 502 VLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
344-560 |
2.94e-41 |
|
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: 148.41 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEI--ISLHDLnnesRAKtLNI 421
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI-DGVDIskIGLHDL----RSR-ISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 422 LAQQHHIFDGTLSENLayaAPD--ATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPA 499
Cdd:cd03244 83 IPQDPVLFSGTIRSNL---DPFgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 500 ILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGS 560
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
340-574 |
8.49e-41 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 155.95 E-value: 8.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQ--ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiislHDLNN---ES 414
Cdd:PRK11176 342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG-------HDLRDytlAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RAKTLNILAQQHHIFDGTLSENLAYAAPDATS-QQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQA 493
Cdd:PRK11176 415 LRNQVALVSQNVHLFNDTIANNIAYARTEQYSrEQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 494 LLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVA 573
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
.
gi 1949233634 574 L 574
Cdd:PRK11176 575 L 575
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
340-559 |
9.80e-41 |
|
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: 145.53 E-value: 9.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYG--QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEIISLHDlnneSRAK 417
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-DGVPVSDLEK----ALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIFDGTLSENLayaapdatsqqmiaaltqaelggwfselkqglktrlgtgGRNVSQGQSRRIALAQALLQK 497
Cdd:cd03247 76 LISVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQG 559
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
340-574 |
6.43e-38 |
|
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: 139.93 E-value: 6.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYG--QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDL---NNES 414
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-------LVDGHDLalaDPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQAL 494
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVAL 574
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
340-568 |
1.34e-37 |
|
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: 139.22 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKtL 419
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG----EDVRKEPREARRQ-I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYAAPDATSQQMIAALTQAELGGWFsELKQGLKTRLGTggrnVSQGQSRRIALAQALLQKP 498
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL-GLEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLNEH 568
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEI 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
339-565 |
2.16e-37 |
|
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: 146.50 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQG--TINLQsdkeiiSLHDLNNESR 415
Cdd:COG5265 357 EVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGriLIDGQ------DIRDVTQASL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALL 495
Cdd:COG5265 431 RAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 496 QKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDpalLSQM---DSVIWLDSGQIIAQGSHQQLL 565
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHR---LSTIvdaDEILVLEAGRIVERGTHAELL 580
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
344-555 |
2.93e-37 |
|
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: 137.99 E-value: 2.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQK---QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDlnNESRAKTLN 420
Cdd:cd03248 16 NVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL--DGKPISQYE--HKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 421 ILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAI 500
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 501 LVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQI 555
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
340-568 |
2.99e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 135.15 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIislhdlnnesRAKT 418
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKDI----------TKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQ---------HHIFDGTLSENLAYA------APDATSQQMIAALTQAELggwfSELKQglktrlgtggRNV--- 480
Cdd:COG1122 70 LRELRRKvglvfqnpdDQLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGL----EHLAD----------RPPhel 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 481 SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQ 558
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVAD 215
|
250
....*....|
gi 1949233634 559 GSHQQLLNEH 568
Cdd:COG1122 216 GTPREVFSDY 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-571 |
1.64e-35 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 141.01 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 6 RLLKLCRPHYKAMLLGTFLASLTVLANV-GLLAISgWFLASMAAAGiasvHMNYFTPAG---TIRFLAIVRTASRYAERL 81
Cdd:PRK10790 13 RLLAYGSPWRKPLGLAVLMLWVAAAAEVsGPLLIS-YFIDNMVAKG----NLPLGLVAGlaaAYVGLQLLAAGLHYAQSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 82 VTHNATFLLLSEIRVN-MFATLSK-LNNLDlaMSRSADLVNRLQNDVDALDKFYLNVLLPML--VALLTVPIIMLFMSAY 157
Cdd:PRK10790 88 LFNRAAVGVVQQLRTDvMDAALRQpLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVATVLrsAALIGAMLVAMFSLDW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 158 NVN-VALICFvgiiiigviiPAILSKQLdKNSHQETLLSAQLRAELSDTLTGLRE----LNIYQARNQQLTKCDLLSEQY 232
Cdd:PRK10790 166 RMAlVAIMIF----------PAVLVVMV-IYQRYSTPIVRRVRAYLADINDGFNEvingMSVIQQFRQQARFGERMGEAS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 233 NQQLFIRHKALgNADGLsLLIVQLAMLSSIVTIVPLV---FSGAmvnvelAMLSLFVLASFESVL-LLPNAFIELP---- 304
Cdd:PRK10790 235 RSHYMARMQTL-RLDGF-LLRPLLSLFSALILCGLLMlfgFSAS------GTIEVGVLYAFISYLgRLNEPLIELTtqqs 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 305 ---YVLKAAERLFILEDKTLSTNNvstTDIELLNKHwALSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTT 380
Cdd:PRK10790 307 mlqQAVVAGERVFELMDGPRQQYG---NDDRPLQSG-RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKST 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 381 LVNLLSSLWPLQQGTINLQSDkeiiSLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAApDATSQQMIAALTQAELGG 460
Cdd:PRK10790 383 LASLLMGYYPLTEGEIRLDGR----PLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 461 WFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPAL 540
Cdd:PRK10790 458 LARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLST 537
|
570 580 590
....*....|....*....|....*....|.
gi 1949233634 541 LSQMDSVIWLDSGQIIAQGSHQQLLNEHPDY 571
Cdd:PRK10790 538 IVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
340-577 |
1.67e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.27 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESRA--K 417
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEV-------RVLGEDVARDPAEvrR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIFDG-TLSENLAYAA-----PDATSQQMIAALtqaelggwfseLKQ-GLKTRLGTGGRNVSQGQSRRIAL 490
Cdd:COG1131 74 RIGYVPQEPALYPDlTVRENLRFFArlyglPRKEARERIDEL-----------LELfGLTDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLNEH 568
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL 222
|
250
....*....|.
gi 1949233634 569 PD--YVALTTR 577
Cdd:COG1131 223 LEdvFLELTGE 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-574 |
4.00e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 137.55 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 5 IRLLKLCRPHYKAMLLGTFLASLTVLANVGLLAISGWFLASMAAAGiasvhmNYFTPAGTIRFLAIVRTASRYAERL--- 81
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDK------GPPALASAIFFMCLLSIASSVSAGLrgg 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 82 VTHNATFLLLSEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDK---FYLNVLLPMLVALLTVPIIMLFMSAYN 158
Cdd:TIGR00958 224 SFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRslsLNVNVLLRNLVMLLGLLGFMLWLSPRL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 159 VNVALIcfvgIIIIGVIIPAILSKQLDKNSH--QETLLSAQLRAElsDTLTGLRELNIYQARNQQLTKcdllseqYNQQL 236
Cdd:TIGR00958 304 TMVTLI----NLPLVFLAEKVFGKRYQLLSEelQEAVAKANQVAE--EALSGMRTVRSFAAEEGEASR-------FKEAL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 237 -----FIRHKALGNAdgLSLLIVQLAMLSSIVTI----VPLVFSGAMvnvELAMLSLFVLASFEsvllLPNAFIELPYV- 306
Cdd:TIGR00958 371 eetlqLNKRKALAYA--GYLWTTSVLGMLIQVLVlyygGQLVLTGKV---SSGNLVSFLLYQEQ----LGEAVRVLSYVy 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 307 ------LKAAERLFILEDKTLSTNNVSTTDIELLNKhwALSLNNVSYHY---GQKQALNNVSFELPAKQKVAIVGRSGSG 377
Cdd:TIGR00958 442 sgmmqaVGASEKVFEYLDRKPNIPLTGTLAPLNLEG--LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 378 KTTLVNLLSSLWPLQQGTINLqsDKEIISlhDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAE 457
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLL--DGVPLV--QYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAAN 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 458 LGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSvlqlKEHAS--VLTIT 535
Cdd:TIGR00958 596 AHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES----RSRASrtVLLIA 671
|
570 580 590
....*....|....*....|....*....|....*....
gi 1949233634 536 HDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVAL 574
Cdd:TIGR00958 672 HRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
340-555 |
5.01e-34 |
|
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: 128.38 E-value: 5.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ----KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHDLNNES- 414
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTDISKLSEKELAAf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RAKTLNILAQQHHIFDG-TLSENLAYAapdatsqQMIAALTQAELGGWFSEL--KQGLKTRLGTGGRNVSQGQSRRIALA 491
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDlTALENVELP-------LLLAGVPKKERRERAEELleRVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 492 QALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPALLSQMDSVIWLDSGQI 555
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
339-558 |
2.01e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 124.39 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQK----QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIislHDLNNES 414
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID-GQDI---SSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RAK----TLNILAQQHHIFDgTLS--ENLAYAApdatsqqMIAALTQAELGGWFSELkqgLKtRLGTGGR------NVSQ 482
Cdd:COG1136 80 LARlrrrHIGFVFQFFNLLP-ELTalENVALPL-------LLAGVSRKERRERAREL---LE-RVGLGDRldhrpsQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 483 GQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPALLSQMDSVIWLDSGQIIAQ 558
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
340-555 |
5.59e-32 |
|
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: 121.55 E-value: 5.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQA--LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNNesRAK 417
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL--DGADISQWDPNE--LGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIFDGTLSENLayaapdatsqqmiaaltqaelggwfselkqglktrlgtggrnVSQGQSRRIALAQALLQK 497
Cdd:cd03246 77 HVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALLSQMDSVIWLDSGQI 555
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
331-578 |
3.48e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 128.15 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 331 IELLNKHWALSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHD 409
Cdd:PRK13657 326 IDLGRVKGAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG----TDIRT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 410 LNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIA 489
Cdd:PRK13657 402 VTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLlnehp 569
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL----- 556
|
....*....
gi 1949233634 570 dyVALTTRF 578
Cdd:PRK13657 557 --VARGGRF 563
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
340-564 |
2.51e-30 |
|
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: 118.44 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQ-----GTINLqSDKEIISLHDLNNES 414
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLL-DGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RaKTLNILAQQHHIFDGTLSENLAYAAP-------DATSQQMIAALTQAELGGwfsELKQGLKtrlgtgGRNVSQGQSRR 487
Cdd:cd03260 80 R-RRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWD---EVKDRLH------ALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 488 IALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQL 564
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
355-507 |
3.99e-30 |
|
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: 115.44 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKTLNILAQQHHIFDG-TL 433
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG----QDLTDDERKSLRKEIGYVFQDPQLFPRlTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 434 SENLAYAAP------DATSQQMIAALTQAELGGWfselkqgLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPT 507
Cdd:pfam00005 77 RENLRLGLLlkglskREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
341-559 |
6.26e-30 |
|
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: 116.00 E-value: 6.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDLNNESRAKTLN 420
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK----DLASLSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 421 ILAQqhhifdgtlsenlayaapdatsqqmiaALTQAELggwfSELKQglktrlgtggRNVSQ---GQSRRIALAQALLQK 497
Cdd:cd03214 77 YVPQ---------------------------ALELLGL----AHLAD----------RPFNElsgGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQLKEHA--SVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
341-554 |
1.24e-29 |
|
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: 114.26 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhDLNNESRAKTLN 420
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------LIDGKDIAKLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 421 ILAQQHhifdgtlsenlayaapdatsqqmIAALTQAelggwfselkqglktrlgtggrnvSQGQSRRIALAQALLQKPAI 500
Cdd:cd00267 69 EELRRR-----------------------IGYVPQL------------------------SGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 501 LVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQ-MDSVIWLDSGQ 554
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
340-555 |
1.57e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 114.42 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESRA--K 417
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI-------KVLGKDIKKEPEEvkR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIFDG-TLSENLAYaapdatsqqmiaaltqaelggwfselkqglktrlgtggrnvSQGQSRRIALAQALLQ 496
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 497 KPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQM-DSVIWLDSGQI 555
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
340-559 |
3.06e-29 |
|
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: 115.68 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY----GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHDLNNESR 415
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-GKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNILAQ------------QHHIFDgTLSENLAYAAPDATSQQMIAALTQAELggwfselkqgLKTRLGTGGRNVSQG 483
Cdd:cd03257 81 RKEIQMVFQdpmsslnprmtiGEQIAE-PLRIHGKLSKKEARKEAVLLLLVGVGL----------PEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-568 |
9.25e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 9.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhDLNNESRAKT 418
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV------------RLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILA--QQHHIFDGTLsenlayaaPdATSQQMIAALTQAELgGWFSELKQGLKT-------RLGTGG---RNVSQ---G 483
Cdd:COG1121 74 RRRIGyvPQRAEVDWDF--------P-ITVRDVVLMGRYGRR-GLFRRPSRADREavdealeRVGLEDladRPIGElsgG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALLSQM-DSVIWLDsGQIIAQGSH 561
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYfDRVLLLN-RGLVAHGPP 222
|
....*..
gi 1949233634 562 QQLLNEH 568
Cdd:COG1121 223 EEVLTPE 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-556 |
2.78e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.63 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISL---HDLNNESRAkt 418
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLpqePPLDDDLTV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDGTLSE-NLAYAAPDATSQQM--IAALTQ--AELGGW-----FSELKQGLKTRLGTGGRNVSQ---GQS 485
Cdd:COG0488 79 LDTVLDGDAELRALEAElEELEAKLAEPDEDLerLAELQEefEALGGWeaearAEEILSGLGFPEEDLDRPVSElsgGWR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDniskqavMNSVLQLKEH-----ASVLTITHDPALLSQM-DSVIWLDSGQII 556
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEEFlknypGTVLVVSHDRYFLDRVaTRILELDRGKLT 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
340-572 |
3.02e-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: 112.98 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKTL 419
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG----EDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 N---ILAQQHHIFDG-TLSENLAY------AAPDATSQQMIAA-LTQAELGG----WFSELkqglktrlgtggrnvSQGQ 484
Cdd:cd03261 77 RrmgMLFQSGALFDSlTVFENVAFplrehtRLSEEEIREIVLEkLEAVGLRGaedlYPAEL---------------SGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHD-PALLSQMDSVIWLDSGQIIAQGSH 561
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTP 221
|
250
....*....|.
gi 1949233634 562 QQLLNEHPDYV 572
Cdd:cd03261 222 EELRASDDPLV 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
336-560 |
6.00e-28 |
|
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: 111.35 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 336 KHWALSLNNVSYHYGQK--QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLNN 412
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGiDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 esrakTLNILAQQHHIFDGTLSENL----AYaapdaTSQQMIAALTQAElggwfselkqglktrlgtGGRNVSQGQSRRI 488
Cdd:cd03369 83 -----SLTIIPQDPTLFSGTIRSNLdpfdEY-----SDEEIYGALRVSE------------------GGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGS 560
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-554 |
7.14e-28 |
|
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: 111.02 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHY--GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKT 418
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG----KDLTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQ--QHHIFDGTLSENLAYAA-----PDATSQQMIAALtqAELGGwFSELKQglktrlgtggRNVSQ---GQSRRI 488
Cdd:cd03225 77 VGLVFQnpDDQFFGPTVEEEVAFGLenlglPEEEIEERVEEA--LELVG-LEGLRD----------RSPFTlsgGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITHDPALLSQ-MDSVIWLDSGQ 554
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
341-556 |
2.22e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 109.65 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHYGQKQ-ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDlnnesRAKTL 419
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL--NGKPIKAKE-----RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQ--QHHIFDGTLSENLAYAAPDATSQQMIAALTQAELggWFSELKQGLKTRLgtggrnvSQGQSRRIALAQALLQK 497
Cdd:cd03226 74 GYVMQdvDYQLFTDSVREELLLGLKELDAGNEQAETVLKDL--DLYALKERHPLSL-------SGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQM-DSVIWLDSGQII 556
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
340-567 |
2.82e-27 |
|
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: 109.83 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISL--HDLNnesrAK 417
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-GRDITGLppHERA----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIFdGTLS--ENL---AYAAPDATSQQMIAALTQAelggwFSELKQglktRLGTGGRNVSQGQSRRIALAQ 492
Cdd:cd03224 76 GIGYVPEGRRIF-PELTveENLllgAYARRRAKRKARLERVYEL-----FPRLKE----RRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 493 ALLQKPAILVLDEPTEGLD-NISKQaVMNSVLQLKEH-ASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLApKIVEE-IFEAIRELRDEgVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLAD 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
340-541 |
3.08e-27 |
|
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: 109.11 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIislhDLNNESRAKTL 419
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-GEPI----RDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYAA----PDATSQQMIAALTQAELGGwfselkqglktRLGTGGRNVSQGQSRRIALAQAL 494
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAG-----------LADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALL 541
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARgGAVLLTTHQPLEL 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
339-569 |
1.10e-26 |
|
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: 108.53 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHDLNNESRAKT 418
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDG-TLSENLAY------AAPDATSQQMIA-ALTQAELGGWF----SELkqglktrlgtggrnvSQGQSR 486
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFplrehtDLSEAEIRELVLeKLELVGLPGAAdkmpSEL---------------SGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHD-PALLSQMDSVIWLDSGQIIAQGSHQQ 563
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDlDSAFAIADRVAVLADGKIIAEGTPEE 228
|
....*..
gi 1949233634 564 LLN-EHP 569
Cdd:COG1127 229 LLAsDDP 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
340-569 |
7.02e-26 |
|
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: 111.53 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQK-----QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHDLNNES 414
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-GKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RAKTLNILAQ--------QHHIFDgTLSE---NLAYAAPDATSQQMIAALTQAELGGWF-----SELkqglktrlgtggr 478
Cdd:COG1123 340 LRRRVQMVFQdpysslnpRMTVGD-IIAEplrLHGLLSRAERRERVAELLERVGLPPDLadrypHEL------------- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 479 nvSQGQSRRIALAQALLQKPAILVLDEPTEGLDnISKQA-VMNSVLQLKE--HASVLTITHDPALLSQM-DSVIWLDSGQ 554
Cdd:COG1123 406 --SGGQRQRVAIARALALEPKLLILDEPTSALD-VSVQAqILNLLRDLQRelGLTYLFISHDLAVVRYIaDRVAVMYDGR 482
|
250
....*....|....*..
gi 1949233634 555 IIAQGSHQQLLN--EHP 569
Cdd:COG1123 483 IVEDGPTEEVFAnpQHP 499
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
339-567 |
8.41e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 111.73 E-value: 8.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQ--ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRA 416
Cdd:PRK10789 313 ELDVNIRQFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD----IPLTKLQLDSWR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQ 496
Cdd:PRK10789 389 SRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 497 KPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-568 |
2.48e-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: 109.61 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHY--GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPlQQGTINLQSDKEIISLHDLNNESRA 416
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP-HGGRISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQ--QHHIFDGTLSENLAYA------APDATSQQMIAALTQAelggwfselkqGLKTRLGTGGRNVSQGQSRRI 488
Cdd:COG1123 83 RRIGMVFQdpMTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAV-----------GLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSV--LQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLL 565
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEIL 231
|
...
gi 1949233634 566 NEH 568
Cdd:COG1123 232 AAP 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-567 |
2.58e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.46 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 335 NKHWALSLNNVSYHYG--QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLnN 412
Cdd:PRK13632 3 NKSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI--DGITISKENL-K 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 ESRAKTLNILAQQHHIFDG-TLSENLAYA-----APDATSQQMIAALTQaelggwfselKQGLKTRLGTGGRNVSQGQSR 486
Cdd:PRK13632 80 EIRKKIGIIFQNPDNQFIGaTVEDDIAFGlenkkVPPKKMKDIIDDLAK----------KVGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHAS--VLTITHD--PALLSqmDSVIWLDSGQIIAQGSHQ 562
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKktLISITHDmdEAILA--DKVIVFSEGKLIAQGKPK 227
|
....*
gi 1949233634 563 QLLNE 567
Cdd:PRK13632 228 EILNN 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
340-564 |
4.10e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY--GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKeiislhdLNNES--- 414
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-------LSEETvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 -RAKTLNILAQQHHIFDG-TLSENLAYAAPD--ATSQQMIAALTQAelggwfseLKQ-GLKTRLGTGGRNVSQGQSRRIA 489
Cdd:PRK13635 79 vRRQVGMVFQNPDNQFVGaTVQDDVAFGLENigVPREEMVERVDQA--------LRQvGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQL 564
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
339-551 |
7.88e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVS-YHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIIslhdlnnesrak 417
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVL------------ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 tlnILAQQHHIFDGTLSENLAY--AAPDATSQQMIAALTQAELGGwfselkqgLKTRLGTG---GRNVSQGQSRRIALAQ 492
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGH--------LAERLDEEadwDQVLSLGEQQRLAFAR 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLD 551
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELT 557
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
340-554 |
7.91e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 101.49 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEIISLHDLNNESRAKTl 419
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-DGEDLTDLEDELPPLRRRI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYAapdatsqqmiaaltqaelggwfselkqglktrlgtggrnVSQGQSRRIALAQALLQKP 498
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSVLQLKEHA--SVLTITHDPALLSQM-DSVIWLDSGQ 554
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
340-556 |
9.87e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINlqsdkeiislhdlnnesRAKTL 419
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-----------------LGETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NI--LAQQHHIFDG--TLSENLAYAAPDATSQQmIAALtqaeLGGW-FSELKQGLKTrlgtggRNVSQGQSRRIALAQAL 494
Cdd:COG0488 379 KIgyFDQHQEELDPdkTVLDELRDGAPGGTEQE-VRGY----LGRFlFSGDDAFKPV------GVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSvlqLKEHA-SVLTITHDPALLSQM-DSVIWLDSGQII 556
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEA---LDDFPgTVLLVSHDRYFLDRVaTRILEFEDGGVR 508
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
340-566 |
5.24e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 100.97 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISL--HDLNNESRAK 417
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLppHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAqqhhIFDG-TLSENLAYAAPDATSQQMIAALTQAELggwfSELKQ---------GLKTRLGTGGRNVSQGQSRR 487
Cdd:cd03219 80 TFQIPR----LFPElTVLENVMVAAQARTGSGLLLARARREE----REAREraeellervGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 488 IALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLL 565
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVR 231
|
.
gi 1949233634 566 N 566
Cdd:cd03219 232 N 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-559 |
6.25e-24 |
|
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: 99.92 E-value: 6.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhDLNNESRAKTLN 420
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI------------RVFGKPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 421 ILA--QQHHIFDgtlsenlaYAAPdATSQQMIA--ALTQAELGGWFS-----ELKQGLKtRLGTGG---RNVSQ---GQS 485
Cdd:cd03235 69 RIGyvPQRRSID--------RDFP-ISVRDVVLmgLYGHKGLFRRLSkadkaKVDEALE-RVGLSEladRQIGElsgGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALLSQ-MDSVIWLDsGQIIAQG 559
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
340-556 |
9.91e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 99.74 E-value: 9.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQ-ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESRAK- 417
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQV-------LVNGQDLSRLKRREi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 -----TLNILAQQHH-IFDGTLSENLAYA-----APDATSQQMIAALtqaelggwfseLKQ-GLKTRLGTGGRNVSQGQS 485
Cdd:COG2884 75 pylrrRIGVVFQDFRlLPDRTVYENVALPlrvtgKSRKEIRRRVREV-----------LDLvGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHDPALLSQMDS-VIWLDSGQII 556
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLELVDRMPKrVLELEDGRLV 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
339-567 |
1.08e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEiisLHDLNNESRAKT 418
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN-GRP---LADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHI-FDGTLSE-----NLAYAAPDATSQQMI-AALTQAELggwfselkQGLKTRLgtgGRNVSQGQSRRIALA 491
Cdd:PRK13548 78 RAVLPQHSSLsFPFTVEEvvamgRAPHGLSRAEDDALVaAALAQVDL--------AHLAGRD---YPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 492 QALLQ------KPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQ 562
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYaDRIVLLHQGRLVADGTPA 226
|
....*
gi 1949233634 563 QLLNE 567
Cdd:PRK13548 227 EVLTP 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
340-570 |
2.27e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.06 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQkQALNnVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsdkeiislhdlNNESRAKT- 418
Cdd:COG3840 2 LRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW------------NGQDLTALp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 -----LNILAQQHHIFDG-TLSENLAYA-APD-----ATSQQMIAALTQAELGGwfselkqgLKTRLGtggRNVSQGQSR 486
Cdd:COG3840 68 paerpVSMLFQENNLFPHlTVAQNIGLGlRPGlkltaEQRAQVEQALERVGLAG--------LLDRLP---GQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEH-ASVLTITHDPA-LLSQMDSVIWLDSGQIIAQGSHQQ 563
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcRERgLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAA 216
|
....*..
gi 1949233634 564 LLNEHPD 570
Cdd:COG3840 217 LLDGEPP 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
340-564 |
3.39e-23 |
|
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: 97.96 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVS--YHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESRAK 417
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-------YINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNI-LAQQHHIFDGTLS--ENLAYAAP---------DATSQQMIAALtqaelggwfsELKQGLKTRLgtggRNVSQGQS 485
Cdd:cd03263 74 RQSLgYCPQFDALFDELTvrEHLRFYARlkglpkseiKEEVELLLRVL----------GLTDKANKRA----RTLSGGMK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPA---LLSqmDSVIWLDSGQIIAQGSHQ 562
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDeaeALC--DRIAIMSDGKLRCIGSPQ 217
|
..
gi 1949233634 563 QL 564
Cdd:cd03263 218 EL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
344-564 |
4.99e-23 |
|
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: 97.44 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGtinlqsdKEIISLHDLNNESRA--KTLNI 421
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-------RATVAGHDVVREPREvrRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 422 LAQQHhIFDGTLS--ENLA-----YAAPDATSQQMIAALTQaelggwFSELKQGLKTRLGTggrnVSQGQSRRIALAQAL 494
Cdd:cd03265 78 VFQDL-SVDDELTgwENLYiharlYGVPGAERRERIDELLD------FVGLLEAADRLVKT----YSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQL 564
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfgMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
340-559 |
6.54e-23 |
|
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: 96.88 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQkVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRaKTL 419
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG----QDVLKQPQKLR-RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYAA-----PDATS-QQMIAALTQAELGgwfselkQGLKTRLGTggrnVSQGQSRRIALAQ 492
Cdd:cd03264 75 GYLPQEFGVYPNfTVREFLDYIAwlkgiPSKEVkARVDEVLELVNLG-------DRAKKKIGS----LSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
340-537 |
1.77e-22 |
|
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: 96.00 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYG----QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIIslhdlnNESR 415
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV--DGEPV------TGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNILaQQHHIFD-GTLSENLAYAapdATSQQMIAALTQAELGGWFSELkqGLKtrlgtGGRN-----VSQGQSRRIA 489
Cdd:cd03293 73 PDRGYVF-QQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLELV--GLS-----GFENayphqLSGGMRQRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHD 537
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHD 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
340-576 |
1.89e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQ-----ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsdKEIISLHDLNNES 414
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV---GDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RA---------------KTLNILAQ--QHHIFDGTLSENLAYAaPDATSQQMIAAltqAELGGWFSElKQGLK-TRLGTG 476
Cdd:PRK13631 99 LItnpyskkiknfkelrRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEA---KKLAKFYLN-KMGLDdSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 477 GRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITHD-PALLSQMDSVIWLDSGQ 554
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTmEHVLEVADEVIVMDKGK 253
|
250 260
....*....|....*....|..
gi 1949233634 555 IIAQGSHQQLLNEhPDYVALTT 576
Cdd:PRK13631 254 ILKTGTPYEIFTD-QHIINSTS 274
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
340-559 |
3.06e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 95.28 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLhdlnnESRAKTL 419
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-GRDVTGV-----PPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYA-----APDATSQQMIAALtqAELGGWFSELKqglktrlgtggRNVSQ---GQSRRIAL 490
Cdd:cd03259 75 GMVFQDYALFPHlTVAENIAFGlklrgVPKAEIRARVREL--LELVGLEGLLN-----------RYPHElsgGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDNISKQAVMNSV--LQLKEHASVLTITHDPA-LLSQMDSVIWLDSGQIIAQG 559
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELkeLQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
340-568 |
3.78e-22 |
|
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: 95.71 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ-KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESRAKT 418
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSV-------LIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQ-----QHHIFDGTLS--ENLAYAAPDATS--QQMIAALTQAELGGWFSELKQ-GLKTRLGTGGRNVSQGQSRRI 488
Cdd:cd03256 74 RQLRRQigmifQQFNLIERLSvlENVLSGRLGRRStwRSLFGLFPKEEKQRALAALERvGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPAL-LSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELT 233
|
...
gi 1949233634 566 NEH 568
Cdd:cd03256 234 DEV 236
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
340-554 |
8.41e-22 |
|
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: 93.69 E-value: 8.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQ-----ALNNVSFELPAKQKVAIVGRSGSGKTTLVN-LLSSLwPLQQGTINLQSdkeiislhdlnne 413
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 414 srakTLNILAQQHHIFDGTLSENLAYAAP----------DAtsqqmiAALTQAelggwFSELKQGLKTRLGTGGRNVSQG 483
Cdd:cd03250 67 ----SIAYVSQEPWIQNGTIRENILFGKPfdeeryekviKA------CALEPD-----LEILPDGDLTEIGEKGINLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQ--LKEHASVLTITHDPALLSQMDSVIWLDSGQ 554
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILglLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-551 |
1.24e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 91.83 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQAL-NNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIIslhdlnnesrakt 418
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 lnILAQQHHIFDGTLSENLAYAapdatsqqmiaaltqaelggWFSELkqglktrlgtggrnvSQGQSRRIALAQALLQKP 498
Cdd:cd03223 68 --FLPQRPYLPLGTLREQLIYP--------------------WDDVL---------------SGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNsvlQLKEH-ASVLTITHDPALLSQMDSVIWLD 551
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQ---LLKELgITVISVGHRPSLWKFHDRVLDLD 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
357-566 |
1.73e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 99.33 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 357 NVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPL---------------------QQG----TINLQSDKEI------- 404
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdYQGdeeqNVGMKNVNEFsltkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 405 ------------------ISLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYAAPDATSQQMIAALTQAELGGWFSELK 466
Cdd:PTZ00265 1266 sgedstvfknsgkilldgVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLP 1345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 467 QGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA--SVLTITHDPALLSQM 544
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRS 1425
|
250 260
....*....|....*....|....*..
gi 1949233634 545 DSVIWLD----SGQII-AQGSHQQLLN 566
Cdd:PTZ00265 1426 DKIVVFNnpdrTGSFVqAHGTHEELLS 1452
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-578 |
1.86e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.95 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLV---NLLSSLWPLQ--QGTINLqsDKEIISLHDLN-N 412
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIPGArvEGEILL--DGEDIYDPDVDvV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 ESRAKtLNILAQQHHIFDGTLSENLAYAAPDA--TSQQMIA-----ALTQAELggWfSELKqglkTRLGTGGRNVSQGQS 485
Cdd:COG1117 89 ELRRR-VGMVFQKPNPFPKSIYDNVAYGLRLHgiKSKSELDeiveeSLRKAAL--W-DEVK----DRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDP---ALLSQMDSVIWLdsGQIIAQGSHQ 562
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMqqaARVSDYTAFFYL--GELVEFGPTE 238
|
250 260
....*....|....*....|..
gi 1949233634 563 QLLnEHP------DYValTTRF 578
Cdd:COG1117 239 QIF-TNPkdkrteDYI--TGRF 257
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
339-557 |
1.94e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 93.27 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHY----GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNES 414
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG----QDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RAKTLN----ILAQQHHIFdGTLS--EN------LAyAAPDAtsqqmiAALTQAELGgwfselKQGLKTRLGTGGRNVSQ 482
Cdd:COG4181 84 RARLRArhvgFVFQSFQLL-PTLTalENvmlpleLA-GRRDA------RARARALLE------RVGLGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 483 GQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTI-THDPALLSQMDSVIWLDSGQIIA 557
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLvTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
357-578 |
2.78e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 95.55 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 357 NVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIisLHDlnnesRAKTLNILAQQHHI---F-DGT 432
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL--GGEV--LQD-----SARGIFLPPHRRRIgyvFqEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 433 L------SENLAYAAPDATSQQMIAALTQA-ELggwfseLkqGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDE 505
Cdd:COG4148 88 LfphlsvRGNLLYGRKRAPRAERRISFDEVvEL------L--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 506 PTEGLDNISKQAVMNSVLQLKEHAS--VLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLNeHPDYVALTTRF 578
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDipILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS-RPDLLPLAGGE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-567 |
5.43e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.41 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY-----GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHDL--NN 412
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPgpDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 ESRAKT-LNILAQQHHIFD-----GTLSENLAYAAPDATSQqMIAALTQAELGgwFSELKQglKTRLGTGGRNVSQGQSR 486
Cdd:TIGR03269 360 RGRAKRyIGILHQEYDLYPhrtvlDNLTEAIGLELPDELAR-MKAVITLKMVG--FDEEKA--EEILDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQ 563
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEE 514
|
....
gi 1949233634 564 LLNE 567
Cdd:TIGR03269 515 IVEE 518
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
340-568 |
6.25e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHDlnnESRAKTL 419
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG-DKPISMLSS---RQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYA-APDAT-----SQQMIAALTQAELGGWFSELKQGLKTRLgtggrnvSQGQSRRIALAQ 492
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRELVAYGrSPWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDL-------SGGQRQRAFLAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 493 ALLQKPAILVLDEPTEGLDnISKQA-VMNSVLQLK-EHASVLTITHDpalLSQM----DSVIWLDSGQIIAQGSHQQLLN 566
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLD-INHQVeLMRLMRELNtQGKTVVTVLHD---LNQAsrycDHLVVLANGHVMAQGTPEEVMT 227
|
..
gi 1949233634 567 EH 568
Cdd:PRK11231 228 PG 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
348-564 |
9.33e-21 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 92.84 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 348 HYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESRA--KTLNILAQQ 425
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTA-------RVAGYDVVREPRKvrRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 426 HHIFDG-TLSENLA-----YAAPDATSQQMIAALTQaelggwFSELKQGLKTRLGTggrnVSQGQSRRIALAQALLQKPA 499
Cdd:TIGR01188 75 ASVDEDlTGRENLEmmgrlYGLPKDEAEERAEELLE------LFELGEAADRPVGT----YSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 500 ILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTiTHDPALLSQM-DSVIWLDSGQIIAQGSHQQL 564
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEegVTILLT-THYMEEADKLcDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
340-555 |
9.89e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 90.67 E-value: 9.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLN-NESRAKT 418
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII--DGLKLTDDKKNiNELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 lNILAQQHHIFDG-TLSENLAYAAPDATSQQMIAALTQAElggwfSELKQ-GLKTRLGTGGRNVSQGQSRRIALAQALLQ 496
Cdd:cd03262 79 -GMVFQQFNLFPHlTVLENITLAPIKVKGMSKAEAEERAL-----ELLEKvGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 497 KPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQM-DSVIWLDSGQI 555
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
340-554 |
1.10e-20 |
|
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: 88.66 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIislhdlnnesraktl 419
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 nilaqqhhifdgtlsenlayaapdatsqqmiaaltqaelgGWFSELkqglktrlgtggrnvSQGQSRRIALAQALLQKPA 499
Cdd:cd03221 66 ----------------------------------------GYFEQL---------------SGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 500 ILVLDEPTEGLDNISKQAVMNsvlQLKEHA-SVLTITHDPALLSQM-DSVIWLDSGQ 554
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEE---ALKEYPgTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
115-565 |
1.28e-20 |
|
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: 96.55 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 115 SADLVNRLQNDVDALDKFYLNVLLPMLVALLTV--PIIMLFMSAYNVNVALICFVGIIIIGVIIPAILSKQLDKnshQET 192
Cdd:TIGR00957 1061 SGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVigALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKR---LES 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 193 LLSAQLRAELSDTLTGLRELNIYQARN----QQLTKCDLLSEQY------NQQLFIRHKALGNAdglsllIVQLAMLSSI 262
Cdd:TIGR00957 1138 VSRSPVYSHFNETLLGVSVIRAFEEQErfihQSDLKVDENQKAYypsivaNRWLAVRLECVGNC------IVLFAALFAV 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 263 VTIVPLvfSGAMVNVELAMlSLFVLASFESVLLLPNafiELPYVLKAAERL-----------FILEDKTLSTNNVSTTDI 331
Cdd:TIGR00957 1212 ISRHSL--SAGLVGLSVSY-SLQVTFYLNWLVRMSS---EMETNIVAVERLkeysetekeapWQIQETAPPSGWPPRGRV 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 332 ELLNKhwalslnNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDL 410
Cdd:TIGR00957 1286 EFRNY-------CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAKIGLHDL 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 nnesRAKtLNILAQQHHIFDGTLSENLayaapDATSQ----QMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSR 486
Cdd:TIGR00957 1359 ----RFK-ITIIPQDPVLFSGSLRMNL-----DPFSQysdeEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQ 1428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:TIGR00957 1429 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
334-555 |
1.66e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 334 LNKHWALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhdlnne 413
Cdd:PRK11247 7 LNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 414 sraktlnilaqqhhifdgtlsenLAYAAPDATSQQMIAALTQ-AEL---------------GGWFSELKQ-----GLKTR 472
Cdd:PRK11247 70 -----------------------LAGTAPLAEAREDTRLMFQdARLlpwkkvidnvglglkGQWRDAALQalaavGLADR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 473 LGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLD---NISKQAVMNSVLQlKEHASVLTITHDPALLSQM-DSVI 548
Cdd:PRK11247 127 ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltRIEMQDLIESLWQ-QHGFTVLLVTHDVSEAVAMaDRVL 205
|
....*..
gi 1949233634 549 WLDSGQI 555
Cdd:PRK11247 206 LIEEGKI 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
340-560 |
2.03e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.28 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDLNNESRAKT- 418
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGE----DITKLPPHERARAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIF-DGTLSENL--AYAAPDATSQQMIAaltqaELGGWFSELKQGLKTRlgtGGrNVSQGQSRRIALAQALL 495
Cdd:TIGR03410 77 IAYVPQGREIFpRLTVEENLltGLAALPRRSRKIPD-----EIYELFPVLKEMLGRR---GG-DLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 496 QKPAILVLDEPTEGLD-NISK--QAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGS 560
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQpSIIKdiGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
357-559 |
2.59e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 89.66 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 357 NVSFELPAkQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHDLNNESRAKTLNILAQQHHIFDG-TLSE 435
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 436 NLAYAAPDATS-------QQMIAALtqaelggwfselkqGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTE 508
Cdd:cd03297 95 NLAFGLKRKRNredrisvDELLDLL--------------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 509 GLDNISKQAVMNSVLQLKE--HASVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
344-569 |
2.69e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.15 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRA--KTLNI 421
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG----LKVNDPKVDERLirQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 422 LAQQHHIFDG-TLSENLAYAAPDATSQQMIAALTQAElggwfsEL--KQGLKTRLGTGGRNVSQGQSRRIALAQALLQKP 498
Cdd:PRK09493 82 VFQQFYLFPHlTALENVMFGPLRVRGASKEEAEKQAR------ELlaKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI-THDPALLSQMDS-VIWLDSGQIIAQGSHQQLLNEHP 569
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIKNPP 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
339-567 |
4.19e-20 |
|
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: 89.76 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSS-LWPLQQGTINLQ-SDKEIISLHDLnnesRA 416
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFgERRGGEDVWEL----RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KtLNIL-AQQHHIFDGTLS-ENLA----------YAAPDATsQQMIAALTQAELGgwFSELKQglkTRLGTggrnVSQGQ 484
Cdd:COG1119 79 R-IGLVsPALQLRFPRDETvLDVVlsgffdsiglYREPTDE-QRERARELLELLG--LAHLAD---RPFGT----LSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHA-SVLTITHDPA-LLSQMDSVIWLDSGQIIAQGSH 561
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGApTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPK 227
|
....*.
gi 1949233634 562 QQLLNE 567
Cdd:COG1119 228 EEVLTS 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
340-559 |
5.74e-20 |
|
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: 88.43 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKeiislhDLNNESRAKTL 419
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS------YQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYAA-----PDATSQQMIAALtqaelggwfselkqGLKTRLGTGGRNVSQGQSRRIALAQA 493
Cdd:cd03268 75 GALIEAPGFYPNlTARENLRLLArllgiRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 494 LLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHdpaLLSQM----DSVIWLDSGQIIAQG 559
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSH---LLSEIqkvaDRIGIINKGKLIEEG 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
340-578 |
8.83e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.06 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTL---VNLLSSLWP--LQQGTINLQSdKEIISLHDLNNES 414
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLNPevTITGSIVYNG-HNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RaKTLNILAQQHHIFDGTLSENLAYA--APDATSQQMIAALTQAELGGwfSELKQGLKTRLGTGGRNVSQGQSRRIALAQ 492
Cdd:PRK14239 85 R-KEIGMVFQQPNPFPMSIYENVVYGlrLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGS-HQQLLN---- 566
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDtKQMFMNpkhk 241
|
250
....*....|..
gi 1949233634 567 EHPDYValTTRF 578
Cdd:PRK14239 242 ETEDYI--SGKF 251
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
350-565 |
1.46e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWP---LQQGTINLQSDKEiislhdlnNESRAKTLNILAQQH 426
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI--------DAKEMRAISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 427 HIFDGTLS--ENLAYAA----PDATS----QQMIAALTQaELGgwfseLKQGLKTRLGTGGR--NVSQGQSRRIALAQAL 494
Cdd:TIGR00955 108 DLFIPTLTvrEHLMFQAhlrmPRRVTkkekRERVDEVLQ-ALG-----LRKCANTRIGVPGRvkGLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQavmnSVLQ-LKEHA----SVLTITHDPA--LLSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAY----SVVQvLKGLAqkgkTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
350-559 |
1.60e-19 |
|
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: 86.84 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSslwplqqGTINLQSDKEIISLHDLNNESRA-KTLNILAQQHHI 428
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-------GRRTGLGVSGEVLINGRPLDKRSfRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 429 FDGTLS--ENLAYAApdatsqqmiaaltqaelggwfsELkqglktrlgtggRNVSQGQSRRIALAQALLQKPAILVLDEP 506
Cdd:cd03213 93 LHPTLTvrETLMFAA----------------------KL------------RGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 507 TEGLDNISKQAVMNSVLQL-KEHASVLTITHDPA--LLSQMDSVIWLDSGQIIAQG 559
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
347-566 |
2.51e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 92.73 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 347 YHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLNnesraKTLNILAQQ 425
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcDVAKFGLTDLR-----RVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 426 HHIFDGTLSENLayaapDATSQQMIA----ALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAIL 501
Cdd:PLN03232 1319 PVLFSGTVRFNI-----DPFSEHNDAdlweALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 502 VLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLN 566
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
340-574 |
3.80e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQK---QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNNESRA 416
Cdd:PRK13642 5 LEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI--DGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQQHHIFDGTLSENLAYAAPDA--TSQQMIAALTQAELGGWFSELKQGLKTRLgtggrnvSQGQSRRIALAQAL 494
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGMENQgiPREEMIKRVDEALLAVNMLDFKTREPARL-------SGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYV 572
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMV 235
|
..
gi 1949233634 573 AL 574
Cdd:PRK13642 236 EI 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
344-569 |
4.49e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 86.62 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHdlnneSRAKTLNILA 423
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-GEDATDVP-----VQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 424 QQHHIFDG-TLSENLAYA-----APDATSQQMIAALTQAELggwfsELKQ--GLKTRLGTggrNVSQGQSRRIALAQALL 495
Cdd:cd03296 81 QHYALFRHmTVFDNVAFGlrvkpRSERPPEAEIRAKVHELL-----KLVQldWLADRYPA---QLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 496 QKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI--THDPA-LLSQMDSVIWLDSGQIIAQGSHQQLLnEHP 569
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEeALEVADRVVVMNKGRIEQVGTPDEVY-DHP 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
339-573 |
5.03e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.62 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISL--HDLNnesra 416
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-GRDVTGLppEKRN----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 ktLNILAQQH----HIfdgTLSENLAY------AAPDATSQQMIAALTQAELGGwFselkqglktrlgtGGRNVSQ---G 483
Cdd:COG3842 79 --VGMVFQDYalfpHL---TVAENVAFglrmrgVPKAEIRARVAELLELVGLEG-L-------------ADRYPHQlsgG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSV--LQLKEHASVLTITHDP--AL-LSqmDSVIWLDSGQIIAQ 558
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELrrLQRELGITFIYVTHDQeeALaLA--DRIAVMNDGRIEQV 217
|
250
....*....|....*..
gi 1949233634 559 GSHQQLLnEHP--DYVA 573
Cdd:COG3842 218 GTPEEIY-ERPatRFVA 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-569 |
6.33e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLV----NLLSSlwplQQGTINLqsDKEIISLHDLNN-- 412
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIriilGILAP----DSGEVLW--DGEPLDPEDRRRig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 ---ESRA--KTLNILAQqhhifdgtlsenLAYAApdatsQ--QMIAALTQAELGGWFSELkqGLKTRLGTGGRNVSQGQS 485
Cdd:COG4152 75 ylpEERGlyPKMKVGEQ------------LVYLA-----RlkGLSKAEAKRRADEWLERL--GLGDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHdpallsQMDSV-------IWLDSGQIIA 557
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSH------QMELVeelcdriVIINKGRKVL 209
|
250
....*....|..
gi 1949233634 558 QGSHQQLLNEHP 569
Cdd:COG4152 210 SGSVDEIRRQFG 221
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
27-304 |
6.37e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 87.34 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 27 LTVLANVGLLAISGWFLASMAAAGIASVHM-NYFTPAGTIRFLAIVRTASRYAERLVTHNATFLLLSEIRVNMFATLSKL 105
Cdd:cd18561 3 LLGLLITALYIAQAWLLARALARIFAGGPWeDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 106 NNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALICFvGIIIIGVIIPAILSKQLD 185
Cdd:cd18561 83 GPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILL-VFALLIPLSPALWDRLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 186 KNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDLLSEQYNQQLfIRHKALgnaDGLSLLIVQLAMLSSIVtI 265
Cdd:cd18561 162 DTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQAT-MKVLAV---SLLSSGIMGLATALGTA-L 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 1949233634 266 VPLVFSGAMVNVELAMLSLFVLasfesVLLLPNAFIELP 304
Cdd:cd18561 237 ALGVGALRVLGGQLTLSSLLLI-----LFLSREFFRPLR 270
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
352-559 |
1.34e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.02 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 352 KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSslwplqqgtiNLQSDKEIISLHDLNNE---SRAKTLNILA--QQH 426
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIS----------GRVEGGGTTSGQILFNGqprKPDQFQKCVAyvRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 427 HIFDGTLS--ENLAYAA--------PDATSQQMIAaltqaelggwFSELKQGLKTRLG-TGGRNVSQGQSRRIALAQALL 495
Cdd:cd03234 90 DILLPGLTvrETLTYTAilrlprksSDAIRKKRVE----------DVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 496 QKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPA--LLSQMDSVIWLDSGQIIAQG 559
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHQPRsdLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
349-559 |
1.54e-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: 84.51 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 349 YGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNnesraktlnilaqqhHI 428
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--RGRVSSLLGLG---------------GG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 429 FDGTLS--ENLAYAApdatsqqMIAALTQAELGGW------FSELKQGLKTRLgtggRNVSQGQSRRIALAQALLQKPAI 500
Cdd:cd03220 95 FNPELTgrENIYLNG-------RLLGLSRKEIDEKideiieFSELGDFIDLPV----KTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 501 LVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI-THDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILvSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
340-557 |
1.80e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNV--SYHYGQKQ--ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDLNNES- 414
Cdd:PRK10535 5 LELKDIrrSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ----DVATLDADAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 ---RAKTLNILAQQHHIFDG-TLSENLAYAApdatsqqMIAALTQAELggwfSELKQGLKTRLGTGGR------NVSQGQ 484
Cdd:PRK10535 81 aqlRREHFGFIFQRYHLLSHlTAAQNVEVPA-------VYAGLERKQR----LLRAQELLQRLGLEDRveyqpsQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQMDSVIWLDSGQIIA 557
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
340-569 |
1.99e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.74 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLwplqqgtinLQSDKEIISLH--DLNNESRAK 417
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL---------ETPDSGRIVLNgrDLFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNI--LAQQH----HIfdgTLSENLAYAAPDA-TSQQMIAALTQAELggwfsELKQ--GLKTRLGTggrNVSQGQSRRI 488
Cdd:COG1118 74 ERRVgfVFQHYalfpHM---TVAENIAFGLRVRpPSKAEIRARVEELL-----ELVQleGLADRYPS---QLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDP--AL-LSqmDSVIWLDSGQIIAQGSHQQ 563
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQeeALeLA--DRVVVMNQGRIEQVGTPDE 220
|
....*.
gi 1949233634 564 LLnEHP 569
Cdd:COG1118 221 VY-DRP 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
339-564 |
2.22e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYG-----QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINlqsdkeiISLHDLNNE 413
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT-------IAGYHITPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 414 SRAKTLNILAQ---------QHHIFDGTLSENLAYAAPD--ATSQQM-IAALTqaelggWFSelKQGLKTRLGTGGR-NV 480
Cdd:PRK13641 75 TGNKNLKKLRKkvslvfqfpEAQLFENTVLKDVEFGPKNfgFSEDEAkEKALK------WLK--KVGLSEDLISKSPfEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 481 SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQ-MDSVIWLDSGQIIAQ 558
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKH 226
|
....*.
gi 1949233634 559 GSHQQL 564
Cdd:PRK13641 227 ASPKEI 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-567 |
6.67e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.33 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQ-----KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQ----SDKEIiSLHDLNnes 414
Cdd:PRK13637 7 NLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvdiTDKKV-KLSDIR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 raKTLNILAQ--QHHIFDGTLSENLAYA------APDATSQQMIAALTQAELGgwFSELKQGLKTRLgtggrnvSQGQSR 486
Cdd:PRK13637 83 --KKVGLVFQypEYQLFEETIEKDIAFGpinlglSEEEIENRVKRAMNIVGLD--YEDYKDKSPFEL-------SGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI--TH---DPALLSqmDSVIWLDSGQIIAQGSH 561
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlvSHsmeDVAKLA--DRIIVMNKGKCELQGTP 229
|
....*.
gi 1949233634 562 QQLLNE 567
Cdd:PRK13637 230 REVFKE 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
340-567 |
1.23e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESRAKTL 419
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI-------VFDGKDITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 N----ILAQQHHIFDG-TLSENLAYAAPDATSQQMIAALtqAELGGWFSELKQGLKTRLGTggrnVSQGQSRRIALAQAL 494
Cdd:PRK11614 79 ReavaIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERI--KWVYELFPRLHERRIQRAGT----MSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPA--LLSQMDSVIWLDSGQIIAQGSHQQLL-NE 567
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLaNE 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
340-567 |
1.23e-17 |
|
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: 82.28 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIislHDLNNESRAktL 419
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD-GKDI---TNLPPHKRP--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYaapdatsqqmiaALTQAELGGwfSELKQGLKTRL------GTGGRNVSQ---GQSRRIA 489
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAF------------GLRLKKLPK--AEIKERVAEALdlvqleGYANRKPSQlsgGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDnisKQAVMNSVLQLKE-HASV----LTITHDPA-LLSQMDSVIWLDSGQIIAQGSHQQ 563
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALD---LKLRKDMQLELKRlQKELgitfVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEE 217
|
....
gi 1949233634 564 LLNE 567
Cdd:cd03300 218 IYEE 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
340-559 |
1.30e-17 |
|
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: 81.56 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHDL--------- 410
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 --NNESRAKTLNILAQQHHIfdgtlseNLAYAAPDATSQqmiaaLTQAELGGWfselkqgLKTRLgtggRNVSQGQSRRI 488
Cdd:cd03269 81 lyPKMKVIDQLVYLAQLKGL-------KKEEARRRIDEW-----LERLELSEY-------ANKRV----EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGkTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
339-562 |
1.36e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKeiislHDLNNESRAKT 418
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH-----FDFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILA-------QQHHIFDG-TLSENLAYAAPDATSQQMIAALTQAElggwfsELKQGLktRLGT-GGR---NVSQGQSR 486
Cdd:PRK11124 77 IRELRrnvgmvfQQYNLWPHlTVQQNLIEAPCRVLGLSKDQALARAE------KLLERL--RLKPyADRfplHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLD-NISKQAVmNSVLQLKE-HASVLTITHDPALLSQMDS-VIWLDSGQIIAQGSHQ 562
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDpEITAQIV-SIIRELAEtGITQVIVTHEVEVARKTASrVVYMENGHIVEQGDAS 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
336-578 |
1.83e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.20 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 336 KHWALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQ-----GTINLqSDKEIISlHDL 410
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRL-FGRNIYS-PDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 NNESRAKTLNILAQQHHIFDG-TLSENLAYA--------APDATSQQMIAALTQAELggWfselkQGLKTRLGTGGRNVS 481
Cdd:PRK14267 79 DPIEVRREVGMVFQYPNPFPHlTIYDNVAIGvklnglvkSKKELDERVEWALKKAAL--W-----DEVKDRLNDYPSNLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 482 QGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGS 560
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGP 231
|
250
....*....|....*...
gi 1949233634 561 HQQLLnEHPDYvALTTRF 578
Cdd:PRK14267 232 TRKVF-ENPEH-ELTEKY 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-559 |
1.93e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.27 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLV---NLLSSLWPLQQGTINLQSDKEIISLHDLNnESRA 416
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEARVSGEVYLDGQDIFKMDVI-ELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQQHHIFDGTLSENLAYA--------APDATSQQMIAALTQAELggWfselkQGLKTRLGTGGRNVSQGQSRRI 488
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGlklnrlvkSKKELQERVRWALEKAQL--W-----DEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
339-567 |
2.07e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.93 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHY--GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWplqqgtinlqsdkeiisLHDLNNESRA 416
Cdd:PRK13640 5 IVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-----------------LPDDNPNSKI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQQHHIFD------------------GTLSENLAYAAPD--ATSQQMIAALTQAelggwfseLKQ-GLKTRLGT 475
Cdd:PRK13640 68 TVDGITLTAKTVWDirekvgivfqnpdnqfvgATVGDDVAFGLENraVPRPEMIKIVRDV--------LADvGMLDYIDS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 476 GGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDPALLSQMDSVIWLDSG 553
Cdd:PRK13640 140 EPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDG 219
|
250
....*....|....
gi 1949233634 554 QIIAQGSHQQLLNE 567
Cdd:PRK13640 220 KLLAQGSPVEIFSK 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
349-559 |
2.95e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 81.22 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 349 YGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLwplqqgtinLQSDKEIISLHDL-----NNESRAKTLNILA 423
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL---------LQPTSGEVRVAGLvpwkrRKKFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 424 QQHH-IFDGTLSENLA-----YAAPDATSQQMIAALTQAelggwfSELKQGLKTRLgtggRNVSQGQSRRIALAQALLQK 497
Cdd:cd03267 102 QKTQlWWDLPVIDSFYllaaiYDLPPARFKKRLDELSEL------LDLEELLDTPV----RQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQL-KEH-ASVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYnRERgTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
340-569 |
3.15e-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: 81.09 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQK----QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHdlNNESR 415
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD-GTDLTLLS--GKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNI--LAQQHHIFDG-TLSENLAYAAPdatsqqmIAALTQAELGGWFSELKQ--GLKTRLGTGGRNVSQGQSRRIAL 490
Cdd:cd03258 79 KARRRIgmIFQHFNLLSSrTVFENVALPLE-------IAGVPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHdpallsQM-------DSVIWLDSGQIIAQGSH 561
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITH------EMevvkricDRVAVMEKGEVVEEGTV 225
|
....*...
gi 1949233634 562 QQLLNeHP 569
Cdd:cd03258 226 EEVFA-NP 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
342-560 |
3.62e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQK-----QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQG-TI--------NLQSDKEIISL 407
Cdd:PRK13645 9 LDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIvgdyaipaNLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 408 HdlnnesraKTLNILAQ--QHHIFDGTLSENLAYAAPDATSQQMIAALTQAELggwfSELKQGLKTRLGTGGRNVSQGQS 485
Cdd:PRK13645 89 R--------KEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL----LKLVQLPEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHAS-VLTITHD-PALLSQMDSVIWLDSGQIIAQGS 560
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKrIIMVTHNmDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
340-567 |
4.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ-----KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQ--------SDKEIIS 406
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 407 LHdlnnesraKTLNILAQ--QHHIFDGTLSENLAYAaPDATSQQMIAALTQA-----ELGgwFSelkqglktrlgtggRN 479
Cdd:PRK13646 83 VR--------KRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYAhrllmDLG--FS--------------RD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 480 V--------SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSV--LQLKEHASVLTITHDPALLSQ-MDSVI 548
Cdd:PRK13646 138 VmsqspfqmSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARyADEVI 217
|
250
....*....|....*....
gi 1949233634 549 WLDSGQIIAQGSHQQLLNE 567
Cdd:PRK13646 218 VMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
340-566 |
4.02e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.72 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQA--LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkEIISLHDLNnESRaK 417
Cdd:PRK13648 8 IVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--QAITDDNFE-KLR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQ--QHHIFDGTLSENLAY-----AAPDATSQQMIA-ALTQAELGGWFSELKQGLktrlgtggrnvSQGQSRRIA 489
Cdd:PRK13648 84 HIGIVFQnpDNQFVGSIVKYDVAFglenhAVPYDEMHRRVSeALKQVDMLERADYEPNAL-----------SGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLN 566
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-565 |
5.60e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 352 KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSD-----KEIISLHDLNNEsraKTLNILAQQH 426
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgKDIFQIDAIKLR---KEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 427 HIFDG-TLSENLAY-----AAPDATSQQMIAALTQAELGGWfselkQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAI 500
Cdd:PRK14246 100 NPFPHlSIYDNIAYplkshGIKEKREIKKIVEECLRKVGLW-----KEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 501 LVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLL 565
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
347-564 |
6.42e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.83 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 347 YHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEIIS--LHDLNnesraKTLNILAQ 424
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV-NGREIGAygLRELR-----RQFSMIPQ 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 425 QHHIFDGTLSENLayaAP--DATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQK-PAIL 501
Cdd:PTZ00243 1392 DPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFI 1468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 502 VLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQL 564
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
258-564 |
7.75e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 84.64 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 258 MLSSIVTIVPLVFSGAMVNV--------ELAMLSLFVLASFeSVLLLPNAF---IELPYVLKAAERLFILEDKTLSTN-- 324
Cdd:PLN03232 529 ILNSIPVVVTLVSFGVFVLLggdltparAFTSLSLFAVLRS-PLNMLPNLLsqvVNANVSLQRIEELLLSEERILAQNpp 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 325 ---NVSTTDIELLNKHWALSLnnvsyhygQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVN-LLSSLWPLQQGTINLQS 400
Cdd:PLN03232 608 lqpGAPAISIKNGYFSWDSKT--------SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 401 dkeiislhdlnnesrakTLNILAQQHHIFDGTLSENLAYAApDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNV 480
Cdd:PLN03232 680 -----------------SVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNI 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 481 SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQ--LKEHASVLtITHDPALLSQMDSVIWLDSGQIIAQ 558
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdeLKGKTRVL-VTNQLHFLPLMDRIILVSEGMIKEE 820
|
....*.
gi 1949233634 559 GSHQQL 564
Cdd:PLN03232 821 GTFAEL 826
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-570 |
9.84e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQqGTINLQSDKEIIslhDLNNESRAKT 418
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFF---NQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQ-------HHIFDGTLSENLAYAApdatsqQMIAALTQAELGGWF------SELKQGLKTRLGTGGRNVSQGQS 485
Cdd:PRK14258 83 LNRLRRQvsmvhpkPNLFPMSVYDNVAYGV------KIVGWRPKLEIDDIVesalkdADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSV--LQLKEHASVLTITHDPALLSQM-DSVIWLDS-----GQIIA 557
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLsDFTAFFKGnenriGQLVE 236
|
250
....*....|...
gi 1949233634 558 QGSHQQLLNEHPD 570
Cdd:PRK14258 237 FGLTKKIFNSPHD 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
179-534 |
9.89e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.31 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 179 ILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDLLSEQYNQQL----FIRHKALGNADGLSLLIV 254
Cdd:PTZ00265 216 ICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYIlkanFMESLHIGMINGFILASY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 255 QLAMLSSIVTIVPLV--------FSGAMVnveLAMLSLFVLASFESVLLLPNaFIELPYVLKAAERLF-ILEDKTLSTNN 325
Cdd:PTZ00265 296 AFGFWYGTRIIISDLsnqqpnndFHGGSV---ISILLGVLISMFMLTIILPN-ITEYMKSLEATNSLYeIINRKPLVENN 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 326 vstTDIELLNKHWALSLNNVSYHYGQKQAL---NNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDK 402
Cdd:PTZ00265 372 ---DDGKKLKDIKKIQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 403 eiiSLHDLNNESRAKTLNILAQQHHIFDGTLSENLAYA--------------APDATSQQ-------------------M 449
Cdd:PTZ00265 449 ---NLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGNDSQenknkrnscrakcagdlndM 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 450 IAALTQAEL------------------------GGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDE 505
Cdd:PTZ00265 526 SNTTDSNELiemrknyqtikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
410 420
....*....|....*....|....*....
gi 1949233634 506 PTEGLDNISKQAVMNSVLQLKEHASVLTI 534
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
340-559 |
1.11e-16 |
|
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: 79.07 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFelPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGtinlqsdkeIISLHDLN---NESRA 416
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSG---------RVLINGVDvtaAPPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQQHHIF---------DGTLSENLAYAAPDatSQQMIAALTQAELggwfselkQGLKTRLGtggRNVSQGQSRR 487
Cdd:cd03298 70 RPVSMLFQENNLFahltveqnvGLGLSPGLKLTAED--RQAIEVALARVGL--------AGLEKRLP---GELSGGERQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 488 IALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPALLSQMDS-VIWLDSGQIIAQG 559
Cdd:cd03298 137 VALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
340-537 |
1.19e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLV---NLLSSLWP--LQQGTINLQsDKEIISLHDLNNES 414
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPgfRVEGKVTFH-GKNLYAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RAKtLNILAQQHHIFDGTLSENLAYAAP--------DATSQQmiaALTQAELggWfSELKQGLKTrlgtGGRNVSQGQSR 486
Cdd:PRK14243 90 RRR-IGMVFQKPNPFPKSIYDNIAYGARingykgdmDELVER---SLRQAAL--W-DEVKDKLKQ----SGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHD 537
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHN 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-569 |
1.24e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.81 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTTL----VNLLSSlwplqQGTINLQSdkeiislHDLNNESRAKTLNILAQQ 425
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDG-------QDLDGLSRRALRPLRRRM 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 426 HHIF-D--GTLS----------ENLAYAAPDATSQQ----MIAALTQAELGGwfselkqglktrlGTGGR---NVSQGQS 485
Cdd:COG4172 365 QVVFqDpfGSLSprmtvgqiiaEGLRVHGPGLSAAErrarVAEALEEVGLDP-------------AARHRyphEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDnISKQAvmnSVLQL-----KEHA-SVLTITHDPALLSQM-DSVIWLDSGQIIAQ 558
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALD-VSVQA---QILDLlrdlqREHGlAYLFISHDLAVVRALaHRVMVMKDGKVVEQ 507
|
250
....*....|...
gi 1949233634 559 GSHQQLLN--EHP 569
Cdd:COG4172 508 GPTEQVFDapQHP 520
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
342-574 |
1.30e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.16 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQKQ---ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNEsrakt 418
Cdd:PRK13650 7 VKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-------IIDGDLLTEE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 lNILAQQHHI----------FDG-TLSENLAYAAPDA--TSQQMIAALTQA-ELGGwFSELKQGLKTRLgtggrnvSQGQ 484
Cdd:PRK13650 75 -NVWDIRHKIgmvfqnpdnqFVGaTVEDDVAFGLENKgiPHEEMKERVNEAlELVG-MQDFKEREPARL-------SGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQ 562
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPR 225
|
250
....*....|..
gi 1949233634 563 QLLNEHPDYVAL 574
Cdd:PRK13650 226 ELFSRGNDLLQL 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
340-573 |
1.36e-16 |
|
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: 79.65 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISLHDLnnESRAKt 418
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-GEDIREQDPV--ELRRK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFdgtlsenlayaaPDATSQQMIAALTQaeLGGWFSELKQ----------GL--KTRLGTGGRNVSQGQSR 486
Cdd:cd03295 77 IGYVIQQIGLF------------PHMTVEENIALVPK--LLKWPKEKIReradellalvGLdpAEFADRYPHELSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDpallsqMDSVIWL-------DSGQIIA 557
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHD------IDEAFRLadriaimKNGEIVQ 216
|
250
....*....|....*..
gi 1949233634 558 QGSHQQLL-NEHPDYVA 573
Cdd:cd03295 217 VGTPDEILrSPANDFVA 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
339-567 |
1.52e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYG-----QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNNE 413
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV--DDTLITSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 414 SRA--KTLNILAQ--QHHIFDGTLSENLAYAAPD-ATSQQMIAALTQAELG--GWFSELKqglktrlgtgGRN---VSQG 483
Cdd:PRK13649 80 IKQirKKVGLVFQfpESQLFEETVLKDVAFGPQNfGVSQEEAEALAREKLAlvGISESLF----------EKNpfeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLkeHASVLTI---TH---DPAllSQMDSVIWLDSGQIIA 557
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL--HQSGMTIvlvTHlmdDVA--NYADFVYVLEKGKLVL 225
|
250
....*....|
gi 1949233634 558 QGSHQQLLNE 567
Cdd:PRK13649 226 SGKPKDIFQD 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
351-573 |
1.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.06 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 351 QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiislHDLNNESRAKTLNILAQ------ 424
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE-------RVITAGKKNKKLKPLRKkvgivf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 425 ---QHHIFDGTLSENLAYA-----APDATSQQMIAALTqaELGGWFSELkqglktrLGTGGRNVSQGQSRRIALAQALLQ 496
Cdd:PRK13634 92 qfpEHQLFEETVEKDICFGpmnfgVSEEDAKQKAREMI--ELVGLPEEL-------LARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 497 KPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHA-SVLTITHdpallsQM-------DSVIWLDSGQIIAQGSHQQLLnE 567
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGlTTVLVTH------SMedaaryaDQIVVMHKGTVFLQGTPREIF-A 235
|
....*.
gi 1949233634 568 HPDYVA 573
Cdd:PRK13634 236 DPDELE 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
340-550 |
2.31e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISlhdLNNESRAKTL 419
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDIST---LKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDGTLSENLAYA------APDatSQQMIAALTQAELGgwfselkqglKTRLGTGGRNVSQGQSRRIALAQA 493
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPwqirnqQPD--PAIFLDDLERFALP----------DTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 494 LLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHA-SVLTITHDPALLSQMDSVIWL 550
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNiAVLWVTHDKDEINHADKVITL 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
355-568 |
2.66e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.86 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLNnesraKTLNILAQQHHIFDGTL 433
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcDISKFGLMDLR-----KVLGIIPQAPVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 434 SENLayaapDATSQQMIA----ALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEG 509
Cdd:PLN03130 1330 RFNL-----DPFNEHNDAdlweSLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 510 LDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLL-NEH 568
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEG 1464
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
340-570 |
2.70e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.88 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIISL--HDLNNESRAK 417
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR-GQHIEGLpgHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TL-------------NILAQQH-HIFDGTLSENLAYAAPDATSQQmiaALTQAELggWFSELkqGLKTRLGTGGRNVSQG 483
Cdd:PRK11300 85 TFqhvrlfremtvieNLLVAQHqQLKTGLFSGLLKTPAFRRAESE---ALDRAAT--WLERV--GLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHDPAL-LSQMDSVIWLDSGQIIAQGS 560
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLvMGISDRIYVVNQGTPLANGT 237
|
250
....*....|
gi 1949233634 561 HQQLLNeHPD 570
Cdd:PRK11300 238 PEEIRN-NPD 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
348-560 |
3.50e-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: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 348 HYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlQSDKEIISLHDLNnesraktlnilaqqhH 427
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV--EVNGRVSALLELG---------------A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 428 IFDGTLS--ENLAYAApdatsqqMIAALTQAELGG------WFSELKQGLKTRLgtggRNVSQGQSRRIALAQALLQKPA 499
Cdd:COG1134 98 GFHPELTgrENIYLNG-------RLLGLSRKEIDEkfdeivEFAELGDFIDQPV----KTYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 500 ILVLDeptEGLdniskqAVMNSVLQ----------LKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGS 560
Cdd:COG1134 167 ILLVD---EVL------AVGDAAFQkkclarirelRESGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGD 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
345-567 |
4.33e-16 |
|
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: 78.74 E-value: 4.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 345 VSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLwplqqgtINLQSDKEI--ISLHDLNNESRAKTLNIL 422
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-------LNTEGDIQIdgVSWNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 423 AQQHHIFDGTLSENL-AYAApdATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAIL 501
Cdd:cd03289 83 PQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 502 VLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
350-543 |
4.49e-16 |
|
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: 77.15 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEiislhDLNNESRAKTLNILAQQHHIf 429
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 430 DGTLS--ENLAYAAPDATSQQMIAALTQAELGGwFSELKQGlktrlgtggrNVSQGQSRRIALAQALLQKPAILVLDEPT 507
Cdd:cd03231 85 KTTLSvlENLRFWHADHSDEQVEEALARVGLNG-FEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1949233634 508 EGLDnisKQAVMNSVLQLKEHA----SVLTITHDPALLSQ 543
Cdd:cd03231 154 TALD---KAGVARFAEAMAGHCarggMVVLTTHQDLGLSE 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
345-565 |
4.63e-16 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 78.41 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 345 VSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLnnESRaktLNILA 423
Cdd:cd03288 27 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTL--RSR---LSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 424 QQHHIFDGTLSENLAyaaPD--ATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAIL 501
Cdd:cd03288 102 QDPILFSGSIRFNLD---PEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 502 VLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
63-567 |
5.08e-16 |
|
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: 81.88 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 63 GTIRFLAIVRTASRYAERLvtHNAtfLLLSEIRVNMfATLSKLnnldlamsRSADLVNRLQNDVDALDKF-------YLN 135
Cdd:TIGR01271 942 GFFRGLPLVHTLLTVSKRL--HEQ--MLHSVLQAPM-AVLNTM--------KAGRILNRFTKDMAIIDDMlpltlfdFIQ 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 136 VLLPMLVALLTVPIIM--LFMSAYNVNVALIcfvgiiiigviipaILSKQLDKNSHQETLLSAQLRAEL-SDTLTGLREL 212
Cdd:TIGR01271 1009 LTLIVLGAIFVVSVLQpyIFIAAIPVAVIFI--------------MLRAYFLRTSQQLKQLESEARSPIfSHLITSLKGL 1074
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 213 NIYQARNQQltkcdllseQYNQQLFirHKALGNADGLSLL-IVQLAMLSSIVTIVPLVFSGAMVNVELAM---------- 281
Cdd:TIGR01271 1075 WTIRAFGRQ---------SYFETLF--HKALNLHTANWFLyLSTLRWFQMRIDIIFVFFFIAVTFIAIGTnqdgegevgi 1143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 282 ---LSLFVLASFESVLllpNAFIELPYVLKAAERLFILED-------KTLSTN-NVSTTDIELLNKH----WA----LSL 342
Cdd:TIGR01271 1144 iltLAMNILSTLQWAV---NSSIDVDGLMRSVSRVFKFIDlpqeeprPSGGGGkYQLSTVLVIENPHaqkcWPsggqMDV 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 343 NNVSYHY--GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLvnlLSSLWPLqqgtinLQSDKEI----ISLHDLNNESRA 416
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALLRL------LSTEGEIqidgVSWNSVTLQTWR 1291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQQHHIFDGTLSENL-AYAapDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALL 495
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTFRKNLdPYE--QWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 496 QKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
282-569 |
6.66e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.71 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 282 LSLFVLASFeSVLLLPN---AFIELPYVLKAAERLFILEDKTLSTNNVSTTDIEllnkhwALSLNNVSYHY---GQKQAL 355
Cdd:PLN03130 561 LSLFAVLRF-PLFMLPNlitQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLP------AISIKNGYFSWdskAERPTL 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 356 NNVSFELPAKQKVAIVGRSGSGKTTLVN-LLSSLWPLQQGTINLQSdkeiislhdlnnesrakTLNILAQQHHIFDGTLS 434
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------------TVAYVPQVSWIFNATVR 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 435 ENLAYAAP-DATSQQmiAALTQAELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNI 513
Cdd:PLN03130 697 DNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 514 SKQAVMNSVL--QLKEHASVLtITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHP 569
Cdd:PLN03130 775 VGRQVFDKCIkdELRGKTRVL-VTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP 831
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
343-567 |
6.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.21 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 343 NNVSYHY------GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNESra 416
Cdd:PRK13633 8 KNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-------YVDGLDTSDEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 ktlnilaqqhHIFDGTLSENLAYAAPDatsQQMIAALTQAE-------LGGWFSELKQGLKTRLGTGGRN---------V 480
Cdd:PRK13633 79 ----------NLWDIRNKAGMVFQNPD---NQIVATIVEEDvafgpenLGIPPEEIRERVDESLKKVGMYeyrrhaphlL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 481 SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPALLSQMDSVIWLDSGQIIAQ 558
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
....*....
gi 1949233634 559 GSHQQLLNE 567
Cdd:PRK13633 226 GTPKEIFKE 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
340-567 |
8.23e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ-KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGtinlqsdKEIISLHDLNNESR--- 415
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKG-------KVLVSGIDTGDFSKlqg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 -AKTLNILAQQHHI-FDG-TLSENLAYAA------PDATSQQMIAALTQAELGGWFSELKQGLktrlgtggrnvSQGQSR 486
Cdd:PRK13644 75 iRKLVGIVFQNPETqFVGrTVEEDLAFGPenlclpPIEIRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
..
gi 1949233634 566 NE 567
Cdd:PRK13644 224 SD 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
340-574 |
8.60e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhdlnneSRAKTL 419
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------------KRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NI--LAQQHHIfDGTLS---ENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLktrlgtggrnvSQGQSRRIALAQAL 494
Cdd:PRK09544 68 RIgyVPQKLYL-DTTLPltvNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDPAL-LSQMDSVIWLDsGQIIAQGShQQLLNEHPDY 571
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCLN-HHICCSGT-PEVVSLHPEF 213
|
...
gi 1949233634 572 VAL 574
Cdd:PRK09544 214 ISM 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
354-555 |
9.87e-16 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 76.29 E-value: 9.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 354 ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEIISLHDLNNESRAKTLNILAQQHH-IFDGT 432
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRV-NGQDVSDLRGRAIPYLRRKIGVVFQDFRlLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 433 LSENLAYA------APDATSQQMIAALTQAELGGWFSELKQGLktrlgtggrnvSQGQSRRIALAQALLQKPAILVLDEP 506
Cdd:cd03292 95 VYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 507 TEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQMDS-VIWLDSGQI 555
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
339-565 |
1.01e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEIISLHDLNNESRA-- 416
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLSQQKGLir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 ---KTLNILAQQHHIF-DGTLSENLAyAAP---DATSQQMIAALTQAELGgwfselKQGLKTRLGTGGRNVSQGQSRRIA 489
Cdd:PRK11264 82 qlrQHVGFVFQNFNLFpHRTVLENII-EGPvivKGEPKEEATARARELLA------KVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI-THDPALLSQM-DSVIWLDSGQIIAQGSHQQLL 565
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDVaDRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
344-567 |
1.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQK-----QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINL----------QSDKEIISLH 408
Cdd:PRK13651 7 NIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkkTKEKEKVLEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 409 DLNNESRAKTLNILAQ------------QHHIFDGTLSENLAYAA-----PDATSQQMiaALTQAELGGWFSELkqglkt 471
Cdd:PRK13651 87 LVIQKTRFKKIKKIKEirrrvgvvfqfaEYQLFEQTIEKDIIFGPvsmgvSKEEAKKR--AAKYIELVGLDESY------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 472 rLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHD-PALLSQMDSVIW 549
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDlDNVLEWTKRTIF 237
|
250
....*....|....*...
gi 1949233634 550 LDSGQIIAQGSHQQLLNE 567
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
335-558 |
1.09e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 335 NKHWALSLNNVSYHYGQKQ----ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDL 410
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ----PMSKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 NNESRAKTLN----ILAQQHHIF-DGTLSENLAY---------AAPDATSQQMIAALtqaelggwfselkqGLKTRLGTG 476
Cdd:PRK11629 77 SSAAKAELRNqklgFIYQFHHLLpDFTALENVAMplligkkkpAEINSRALEMLAAV--------------GLEHRANHR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 477 GRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSV--LQLKEHASVLTITHDPALLSQMDSVIWLDSGQ 554
Cdd:PRK11629 143 PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGR 222
|
....
gi 1949233634 555 IIAQ 558
Cdd:PRK11629 223 LTAE 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-557 |
1.79e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 79.46 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 3 NFIRLLKlcRPHYKAMLLGTFLASLTVLANVGLLAisgwfLASMAAAGIASVHMNYFtpagtIRF---LAIVRTASRYAE 79
Cdd:COG4615 2 NLLRLLL--RESRWLLLLALLLGLLSGLANAGLIA-----LINQALNATGAALARLL-----LLFaglLVLLLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 80 RLVT---HNATFlllsEIRVNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYlnVLLPMLV--ALLTV------- 147
Cdd:COG4615 70 LLLTrlgQHAVA----RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF--VRLPELLqsVALVLgclayla 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 148 ---PIIMLFMSAYnVNVALICFVGIIIIGViipailsKQLDKNSHQETLLSAQLRAelsdTLTGLRELNIYQARNQQLTK 224
Cdd:COG4615 144 wlsPPLFLLTLVL-LGLGVAGYRLLVRRAR-------RHLRRAREAEDRLFKHFRA----LLEGFKELKLNRRRRRAFFD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 225 CDLL--SEQYnQQLFIRHKAL-GNADGLSLLIVqLAMLSSIVTIVPLVFSgamvnVELAMLSLFVLasfesVLL-----L 296
Cdd:COG4615 212 EDLQptAERY-RDLRIRADTIfALANNWGNLLF-FALIGLILFLLPALGW-----ADPAVLSGFVL-----VLLflrgpL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 297 PNAFIELPYVLK---AAERLFILEDK--TLSTNNVSTTDIELLNKHWALSLNNVSYHYGQKQ-----ALNNVSFELPAKQ 366
Cdd:COG4615 280 SQLVGALPTLSRanvALRKIEELELAlaAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 367 KVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHdlnnesraktlNILAQQHH---IF-DGTLSENLAYAAP 442
Cdd:COG4615 360 LVFIVGGNGSGKSTLAKLLTGLYRPESGEILL--DGQPVTAD-----------NREAYRQLfsaVFsDFHLFDRLLGLDG 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 443 DATSQQMIAALTQAELGGwfselkqglKTRLGTGG---RNVSQGQSRRIALAQALLQKPAILVLDE------P------- 506
Cdd:COG4615 427 EADPARARELLERLELDH---------KVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPefrrvfy 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 507 TEGLdniskqavmnsvLQLKEHA-SVLTITHDPALLSQMDSVIWLDSGQIIA 557
Cdd:COG4615 498 TELL------------PELKARGkTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
340-569 |
2.35e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLnNESRAKT 418
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrDGQLRDLYAL-SEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 L-----NILAQqhHIFDG---------TLSENLAyaapdATSQQMIAALtQAELGGWFSELKQGLKtRLGTGGRNVSQGQ 484
Cdd:PRK11701 86 LlrtewGFVHQ--HPRDGlrmqvsaggNIGERLM-----AVGARHYGDI-RATAGDWLERVEIDAA-RIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDnISKQA-----VMNSVLQLkeHASVLTITHDPA---LLSqmDSVIWLDSGQII 556
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArlldlLRGLVREL--GLAVVIVTHDLAvarLLA--HRLLVMKQGRVV 231
|
250
....*....|....*
gi 1949233634 557 AQGSHQQLLNE--HP 569
Cdd:PRK11701 232 ESGLTDQVLDDpqHP 246
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
342-578 |
2.98e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.43 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEIISLHdlnneSRAKTLNI 421
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF-HGTDVSRLH-----ARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 422 LAQQHHIFDG-TLSENLAYA--------APD--ATSQQMIAALTQAELggwfSELKQGLKTRLgtggrnvSQGQSRRIAL 490
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlprreRPNaaAIKAKVTQLLEMVQL----AHLADRYPAQL-------SGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH---ASVLtITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLN 566
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkfTSVF-VTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQVWR 226
|
250
....*....|..
gi 1949233634 567 EhPdyvalTTRF 578
Cdd:PRK10851 227 E-P-----ATRF 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
340-538 |
3.64e-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: 74.32 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhDLNNESRAKTL 419
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV------------RWNGTPLAEQR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHI------FDGTLS--ENLAYAAPD-ATSQQMI-AALTQAelggwfselkqGLKTRLGTGGRNVSQGQSRRIA 489
Cdd:TIGR01189 69 DEPHENILYlghlpgLKPELSalENLHFWAAIhGGAQRTIeDALAAV-----------GLTGFEDLPAAQLSAGQQRRLA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDnisKQAVMNSVLQLKEHA----SVLTITHDP 538
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALD---KAGVALLAGLLRAHLarggIVLLTTHQD 187
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
355-553 |
3.68e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.67 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLvnLLSSLWPLQ--QGTINLQSDKEIISLHDLNNESRAKTLNILAQQHHIFDGT 432
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 433 LSENLAYAAPdaTSQQMIAALTQA-ELGGWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLD 511
Cdd:cd03290 95 VEENITFGSP--FNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1949233634 512 -NISKQAVMNSVLQL--KEHASVLTITHDPALLSQMDSVIWLDSG 553
Cdd:cd03290 173 iHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
335-564 |
3.76e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.07 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 335 NKHWaLSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNES 414
Cdd:PRK11432 3 QKNF-VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-------FIDGEDVTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 -RAKTLNILAQQHHIFDG-TLSENLAYAApdatsqQMiaaltqaeLGGWFSELKQGLKTRL------GTGGRNVSQ---G 483
Cdd:PRK11432 75 iQQRDICMVFQSYALFPHmSLGENVGYGL------KM--------LGVPKEERKQRVKEALelvdlaGFEDRYVDQisgG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASV--LTITHDPA-LLSQMDSVIWLDSGQIIAQGS 560
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSeAFAVSDTVIVMNKGKIMQIGS 220
|
....
gi 1949233634 561 HQQL 564
Cdd:PRK11432 221 PQEL 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
353-559 |
4.27e-15 |
|
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: 74.71 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 353 QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLwplqqgtinLQSDKEIISLH--DLNNESRAKTLNI--LAQQHHI 428
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL---------LEPDAGFATVDgfDVVKEPAEARRRLgfVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 429 FDG-TLSENLAYAAPdatsqqmIAALTQAELGGWFSELKQ--GLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDE 505
Cdd:cd03266 90 YDRlTARENLEYFAG-------LYGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 506 PTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQM-DSVIWLDSGQIIAQG 559
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGkCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
339-567 |
5.57e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.54 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQ-KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdKEIislHDLNNESRAK 417
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG-REV---NAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQ--HHIFDGTLSENLAYAApdatsQQMiaALTQAELggwfselkqglKTRLGTGGRNV-------------SQ 482
Cdd:PRK13647 80 KVGLVFQDpdDQVFSSTVWDDVAFGP-----VNM--GLDKDEV-----------ERRVEEALKAVrmwdfrdkppyhlSY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 483 GQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQ-MDSVIWLDSGQIIAQGS 560
Cdd:PRK13647 142 GQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD 221
|
....*..
gi 1949233634 561 HQQLLNE 567
Cdd:PRK13647 222 KSLLTDE 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
340-569 |
6.01e-15 |
|
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: 75.86 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY----GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWP---LQQGTINLQsDKEIISL--HDL 410
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFD-GEDLLKLseKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 nNESRAK-----------TLN----ILAQ-----QHHifdGTLSENLAYAapdatsqQMIAALTQAELGGWFSELKQ--- 467
Cdd:COG0444 81 -RKIRGReiqmifqdpmtSLNpvmtVGDQiaeplRIH---GGLSKAEARE-------RAIELLERVGLPDPERRLDRyph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 468 ---GlktrlgtggrnvsqGQSRRIALAQALLQKPAILVLDEPTEGLDnISKQA-VMNSVLQLKE--HASVLTITHDPALL 541
Cdd:COG0444 150 elsG--------------GMRQRVMIARALALEPKLLIADEPTTALD-VTIQAqILNLLKDLQRelGLAILFITHDLGVV 214
|
250 260 270
....*....|....*....|....*....|.
gi 1949233634 542 SQM-DSVIWLDSGQIIAQGSHQQLLNE--HP 569
Cdd:COG0444 215 AEIaDRVAVMYAGRIVEEGPVEELFENprHP 245
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
339-565 |
6.54e-15 |
|
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: 78.45 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQ--ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiislhdlnnesra 416
Cdd:TIGR00957 636 SITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 kTLNILAQQHHIFDGTLSENLAYAAP--DATSQQMIAA---LTQAELggwfseLKQGLKTRLGTGGRNVSQGQSRRIALA 491
Cdd:TIGR00957 700 -SVAYVPQQAWIQNDSLRENILFGKAlnEKYYQQVLEAcalLPDLEI------LPSGDRTEIGEKGVNLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 492 QALLQKPAILVLDEPTEGLDNISKQAVMNSVL----QLKEHASVLtITHDPALLSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpegVLKNKTRIL-VTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-537 |
1.16e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.97 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQ--------SDKEIIslhdL 410
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegpgAERGVV----F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 NNESRAKTLNILAqqhHIFDGTLSENLAYAAPDATSQQMIAaltqaelggwfselKQGLKtrlGTGGRNVSQ---GQSRR 487
Cdd:PRK11248 77 QNEGLLPWRNVQD---NVAFGLQLAGVEKMQRLEIAHQMLK--------------KVGLE---GAEKRYIWQlsgGQRQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 488 IALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHD 537
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHD 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
340-560 |
1.18e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.34 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ-KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdKEIislhDLNNESRA-- 416
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPI----KYDKKSLLev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 -KTLNILAQQ--HHIFDGTLSENLAYAApdatsqqMIAALTQAELGgwfSELKQGLKtRLGTGG------RNVSQGQSRR 487
Cdd:PRK13639 77 rKTVGIVFQNpdDQLFAPTVEEDVAFGP-------LNLGLSKEEVE---KRVKEALK-AVGMEGfenkppHHLSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 488 IALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLS-QMDSVIWLDSGQIIAQGS 560
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
340-538 |
2.40e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.21 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHdlnnesraktl 419
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 niLAQQHHI--FDG-----TLSENLAY-AAPDATSQQMI-AALTQAELGGwFSELKqglktrlgtgGRNVSQGQSRRIAL 490
Cdd:PRK13539 72 --AEACHYLghRNAmkpalTVAENLEFwAAFLGGEELDIaAALEAVGLAP-LAHLP----------FGYLSAGQKRRVAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDNISKQAVMNSVL-QLKEHASVLTITHDP 538
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAAVALFAELIRaHLAQGGIVIAATHIP 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
350-566 |
2.45e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTT----LVNLLSS---LW----PLQQGT----INLQSDKEIIsLHDLNN-- 412
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSqgeIWfdgqPLHNLNrrqlLPVRHRIQVV-FQDPNSsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 ESRAKTLNILAQQHHIFDGTLSenlayaaPDATSQQMIAALTqaELGgwfseLKQGLKTRLGTggrNVSQGQSRRIALAQ 492
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTLS-------AAQREQQVIAVME--EVG-----LDPETRHRYPA---EFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 493 ALLQKPAILVLDEPTEGLD-NISKQ--AVMNSvLQLKEHASVLTITHD----PALLSQmdsVIWLDSGQIIAQGSHQQLL 565
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDkTVQAQilALLKS-LQQKHQLAYLFISHDlhvvRALCHQ---VIVLRQGEVVEQGDCERVF 514
|
.
gi 1949233634 566 N 566
Cdd:PRK15134 515 A 515
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-566 |
2.51e-14 |
|
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: 75.61 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSL--WPLQQGTI-------------NLQS---- 400
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyvERPSkvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 401 ---------DKEIISLHDLNNESRA---KTLNILAQQHHIF--DGTLSENLAYAAPDATSQQMIAALTQAELggwfseLK 466
Cdd:TIGR03269 81 pcpvcggtlEPEEVDFWNLSDKLRRrirKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVDL------IE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 467 Q-GLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPALLSQ 543
Cdd:TIGR03269 155 MvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|....
gi 1949233634 544 M-DSVIWLDSGQIIAQGSHQQLLN 566
Cdd:TIGR03269 235 LsDKAIWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
350-540 |
2.59e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 71.69 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHDLNneSRAKTLNILAQ--QHH 427
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLL--ERRQRVGLVFQdpDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 428 IFDGTLSENLAYA------APDATSQQMIAALTQAELGGWFSELKQGLktrlgtggrnvSQGQSRRIALAQALLQKPAIL 501
Cdd:TIGR01166 81 LFAADVDQDVAFGplnlglSEAEVERRVREALTAVGASGLRERPTHCL-----------SGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1949233634 502 VLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI-THDPAL 540
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIsTHDVDL 189
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
350-574 |
5.52e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.07 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQ------SDKEIISLH-------------DL 410
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgqdllkADPEAQKLLrqkiqivfqnpygSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 NneSRAKTLNILAQQHHIfdgtlSENLAYAAPDATSQQMIAaltqaelggwfselKQGLKTRlgTGGRN---VSQGQSRR 487
Cdd:PRK11308 106 N--PRKKVGQILEEPLLI-----NTSLSAAERREKALAMMA--------------KVGLRPE--HYDRYphmFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 488 IALAQALLQKPAILVLDEPTEGLDnISKQA-VMNSVLQLKE--HASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQ 563
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALD-VSVQAqVLNLMMDLQQelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQ 241
|
250
....*....|...
gi 1949233634 564 LLNE--HPDYVAL 574
Cdd:PRK11308 242 IFNNprHPYTQAL 254
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
344-573 |
5.97e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkEIISLHDLnNESRaKTLNIL 422
Cdd:PRK13652 8 DLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--EPITKENI-REVR-KFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 423 AQQ--HHIFDGTLSENLAYAAPDatsqqmiAALTQAELGGWFSELKQ--GLKTRLGTGGRNVSQGQSRRIALAQALLQKP 498
Cdd:PRK13652 84 FQNpdDQIFSPTVEQDIAFGPIN-------LGLDEETVAHRVSSALHmlGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHDPALLSQMDSVIW-LDSGQIIAQGSHQQLLNEhPDYVA 573
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEIFLQ-PDLLA 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
340-555 |
7.13e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQA----LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDLNNESR 415
Cdd:PRK10584 7 VEVHHLKKSVGQGEHelsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ----PLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKtlnILAQ------QHHIFDGTLS--ENLAYAA-----PDATSQQMIAALtqaelggwfseLKQ-GLKTRLGTGGRNVS 481
Cdd:PRK10584 83 AK---LRAKhvgfvfQSFMLIPTLNalENVELPAllrgeSSRQSRNGAKAL-----------LEQlGLGKRLDHLPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 482 QGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLT-ITHDPALLSQMDSVIWLDSGQI 555
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLIlVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-565 |
7.29e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkEIISLHDLNNESRakt 418
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG--EPVPSRARHARQR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQqhhiFDG-----TLSENLA-----YAAPDATSQQMIAALTQaelggwFSELKQGLKTRLgtggRNVSQGQSRRI 488
Cdd:PRK13537 82 VGVVPQ----FDNldpdfTVRENLLvfgryFGLSAAAARALVPPLLE------FAKLENKADAKV----GELSGGMKRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITH---DPALLSQMDSVIwlDSGQIIAQGSHQQL 564
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeEAERLCDRLCVI--EEGRKIAEGAPHAL 225
|
.
gi 1949233634 565 L 565
Cdd:PRK13537 226 I 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
340-572 |
7.35e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWplqQGTINLQSDKEIISlHDLNNE------ 413
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSAGSHIELLG-RTVQREgrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 414 ---SRAKTLNILAQQHHIFDGTLSENLayaapdatsqqMIAALTQAELG----GWFSELK-----QGLkTRLGTGG---- 477
Cdd:PRK09984 81 irkSRANTGYIFQQFNLVNRLSVLENV-----------LIGALGSTPFWrtcfSWFTREQkqralQAL-TRVGMVHfahq 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 478 --RNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH---ASVLTITHDPALLSQMDSVIWLDS 552
Cdd:PRK09984 149 rvSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgiTVVVTLHQVDYALRYCERIVALRQ 228
|
250 260
....*....|....*....|
gi 1949233634 553 GQIIAQGSHQQLLNEHPDYV 572
Cdd:PRK09984 229 GHVFYDGSSQQFDNERFDHL 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-573 |
7.73e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTIN----LQSDKEIISLHDLNNES 414
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvLLGGRSIFNYRDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 415 RakTLNILAQQHHIFDGTLSENL--AYAAPDATSQQMIAALTQA---ELGGWfselkQGLKTRLGTGGRNVSQGQSRRIA 489
Cdd:PRK14271 101 R--RVGMLFQRPNPFPMSIMDNVlaGVRAHKLVPRKEFRGVAQArltEVGLW-----DAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLN-- 566
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSsp 253
|
250
....*....|
gi 1949233634 567 ---EHPDYVA 573
Cdd:PRK14271 254 khaETARYVA 263
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
340-566 |
7.97e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.54 E-value: 7.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqSDKEIISLHDLNNESRA--- 416
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVV-NGQTINLVRDKDGQLKVadk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQ------QH-----HIfdgTLSENLAyaapDATSQQMIAALTQAELGGWFSELKQGLKTRL-GTGGRNVSQGQ 484
Cdd:PRK10619 85 NQLRLLRTrltmvfQHfnlwsHM---TVLENVM----EAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQMDS-VIWLDSGQIIAQGSHQ 562
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGkTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPE 237
|
....
gi 1949233634 563 QLLN 566
Cdd:PRK10619 238 QLFG 241
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
357-551 |
8.59e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 357 NVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKTLNIlaqQHH--IfDGTLS 434
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG----EPIRRQRDEYHQDLLYL---GHQpgI-KTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 435 --ENLAYAAP---DATSQQMIAALTQAELGGwFSELKqglktrlgtgGRNVSQGQSRRIALAQALLQKPAILVLDEPTEG 509
Cdd:PRK13538 91 alENLRFYQRlhgPGDDEALWEALAQVGLAG-FEDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1949233634 510 LDnisKQAVmnSVLQ--LKEHAS-----VLTITHDPALLSQMDSVIWLD 551
Cdd:PRK13538 160 ID---KQGV--ARLEalLAQHAEqggmvILTTHQDLPVASDKVRKLRLG 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
345-543 |
1.13e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 345 VSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInLQSDKEIISLHDLNNESRAKTLNILA 423
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-WFSGHDITRLKNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 424 QQHHIF-DGTLSENLAY------AAPDATSQQMIAALTqaelggwfselKQGLKTRLGTGGRNVSQGQSRRIALAQALLQ 496
Cdd:PRK10908 86 QDHHLLmDRTVYDNVAIpliiagASGDDIRRRVSAALD-----------KVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 497 KPAILVLDEPTEGLDNiskqAVMNSVLQLKEH-----ASVLTITHDPALLSQ 543
Cdd:PRK10908 155 KPAVLLADEPTGNLDD----ALSEGILRLFEEfnrvgVTVLMATHDIGLISR 202
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-568 |
1.28e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiiSLHDLNNESRAKT 418
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI---------TVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 ----LNILAQqhhiFDG-----TLSENL-AYAAPDATSQQMIAALTQAELGgwFSELKQGLKTRLGtggrNVSQGQSRRI 488
Cdd:PRK13536 112 ararIGVVPQ----FDNldlefTVRENLlVFGRYFGMSTREIEAVIPSLLE--FARLESKADARVS----DLSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAV---MNSVLQLKEhaSVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQL 564
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIwerLRSLLARGK--TILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHAL 259
|
....
gi 1949233634 565 LNEH 568
Cdd:PRK13536 260 IDEH 263
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
340-536 |
2.09e-13 |
|
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: 68.22 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhdlnnesraktl 419
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 nilaqqhhIFDGtlsENLAYAAPDATSQQMIAALTQaelggwfselkqglktrlgtggrnVSQGQSRRIALAQALLQKPA 499
Cdd:cd03216 58 --------LVDG---KEVSFASPRDARRAGIAMVYQ------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190
....*....|....*....|....*....|....*...
gi 1949233634 500 ILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITH 536
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISH 140
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
340-559 |
2.20e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.10 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLS--SLWPLQQGTINLQSDkeiiSLHDLNNESRAK 417
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGE----DILELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 tLNI-LAQQHHI-FDG-TLSENLAYAAPDATSQQMIAALTQAELGGWFSELkqGLKTRLGTGGRNV--SQGQSRRIALAQ 492
Cdd:COG0396 77 -AGIfLAFQYPVeIPGvSVSNFLRTALNARRGEELSAREFLKLLKEKMKEL--GLDEDFLDRYVNEgfSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITHDPALLSQM--DSVIWLDSGQIIAQG 559
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHYQRILDYIkpDFVHVLVDGRIVKSG 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-560 |
2.36e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.90 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 319 KTLSTNNVSTTDIellnkhwaLSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInl 398
Cdd:PRK09452 2 KKLNKQPSSLSPL--------VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 399 qsdkeIISLHDLNN---ESRakTLNILAQQHHIFDG-TLSENLAYAAP-DATSQQMIAALTqaelggwfselKQGLKT-R 472
Cdd:PRK09452 72 -----MLDGQDITHvpaENR--HVNTVFQSYALFPHmTVFENVAFGLRmQKTPAAEITPRV-----------MEALRMvQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 473 L-GTGGRNVSQ---GQSRRIALAQALLQKPAILVLDEPTEGLD-NISKQavMNS---VLQLKEHASVLTITHD-PALLSQ 543
Cdd:PRK09452 134 LeEFAQRKPHQlsgGQQQRVAIARAVVNKPKVLLLDESLSALDyKLRKQ--MQNelkALQRKLGITFVFVTHDqEEALTM 211
|
250
....*....|....*..
gi 1949233634 544 MDSVIWLDSGQIIAQGS 560
Cdd:PRK09452 212 SDRIVVMRDGRIEQDGT 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-556 |
6.84e-13 |
|
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: 71.12 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLwplqqgtinlqsDKEIislhdlNNESRAK-- 417
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------------DKDF------NGEARPQpg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 -TLNILAQQHH----------IFDG------TLSE----NLAYAAPDATSQQMIAalTQAEL-------GGWfsELKQGL 469
Cdd:TIGR03719 68 iKVGYLPQEPQldptktvrenVEEGvaeikdALDRfneiSAKYAEPDADFDKLAA--EQAELqeiidaaDAW--DLDSQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 470 KT-----RLGTGGRNV---SQGQSRRIALAQALLQKPAILVLDEPTEGLDniskqavMNSVLQLKEH-----ASVLTITH 536
Cdd:TIGR03719 144 EIamdalRCPPWDADVtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVAWLERHlqeypGTVVAVTH 216
|
250 260
....*....|....*....|....
gi 1949233634 537 DPALLsqmDSVI-W---LDSGQII 556
Cdd:TIGR03719 217 DRYFL---DNVAgWileLDRGRGI 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
340-567 |
7.29e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ-KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHDLNNESRAKT 418
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDGTLSENLAYAA-----PDATSQQMIAALTQaelggwfselKQGLKTRLGTGGRNVSQGQSRRIALAQA 493
Cdd:PRK13636 86 MVFQDPDNQLFSASVYQDVSFGAvnlklPEDEVRKRVDNALK----------RTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 494 LLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA--SVLTITHDPALLS-QMDSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
340-560 |
7.37e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKeiislhdLNNESRAktL 419
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-------LDYSKRG--L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQ---------HHIFDGTLSENLAYA------APDATSQQMIAALTQAELGGWFSELKQGLktrlgtggrnvSQGQ 484
Cdd:PRK13638 73 LALRQQvatvfqdpeQQIFYTDIDSDIAFSlrnlgvPEAEITRRVDEALTLVDAQHFRHQPIQCL-----------SHGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDNISKQ---AVMNSVLQLKEHasVLTITHDPALLSQM-DSVIWLDSGQIIAQGS 560
Cdd:PRK13638 142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTqmiAIIRRIVAQGNH--VIISSHDIDLIYEIsDAVYVLRQGQILTHGA 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-578 |
8.55e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNNESRaKTL 419
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII--DDEDISLLPLHARAR-RGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYAAP---DATSQQMiaALTQAELGGWF--SELKQGLktrlgtgGRNVSQGQSRRIALAQA 493
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAVLQirdDLSAEQR--EDRANELMEEFhiEHLRDSM-------GQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 494 LLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHD-PALLSQMDSVIWLDSGQIIAQGSHQQLL-NEHPD 570
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGlGVLITDHNvRETLAVCERAYIVSQGHLIAHGTPTEILqDEHVK 231
|
....*...
gi 1949233634 571 YVALTTRF 578
Cdd:PRK10895 232 RVYLGEDF 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
344-570 |
1.01e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 344 NVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDK-EIISLHDLNnESRaKTLNIL 422
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENiPAMSRSRLY-TVR-KRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 423 AQQHHIF-DGTLSENLAYAAPDATsqQMIAALTQAELggwFSELKQ-GLKTRLGTGGRNVSQGQSRRIALAQALLQKPAI 500
Cdd:PRK11831 90 FQSGALFtDMNVFDNVAYPLREHT--QLPAPLLHSTV---MMKLEAvGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 501 LVLDEPTEGLDNISKQAVMNSVLQLKeHASVLT---ITHD-PALLSQMDSVIWLDSGQIIAQGSHQQlLNEHPD 570
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELN-SALGVTcvvVSHDvPEVLSIADHAYIVADKKIVAHGSAQA-LQANPD 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
340-569 |
1.21e-12 |
|
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: 70.48 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ----KQALNNVSFELPAKQKVAIVGRSGSGKT----TLVNLLSSLWPLQQGTINLQsDKEIISLhdln 411
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFD-GQDLLGL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 412 NESRAKT----------------LNIL---AQQhhifdgtLSENLAY---AAPDATSQQMIAALTQAELggwfselkQGL 469
Cdd:COG4172 82 SERELRRirgnriamifqepmtsLNPLhtiGKQ-------IAEVLRLhrgLSGAAARARALELLERVGI--------PDP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 470 KTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLD-NISKQ--AVMNSvLQLKEHASVLTITHDPALLSQM-D 545
Cdd:COG4172 147 ERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDvTVQAQilDLLKD-LQRELGMALLLITHDLGVVRRFaD 225
|
250 260
....*....|....*....|....*.
gi 1949233634 546 SVIWLDSGQIIAQGSHQQLLN--EHP 569
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAELFAapQHP 251
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
353-567 |
1.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 353 QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINL--------QSDKEIISLHdlnnesraKTLNILAQ 424
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstSKQKEIKPVR--------KKVGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 425 --QHHIFDGTLSENLAYAAPD----ATSQQMIAAlTQAELGGWFSELKQGLKTRLgtggrnvSQGQSRRIALAQALLQKP 498
Cdd:PRK13643 92 fpESQLFEETVLKDVAFGPQNfgipKEKAEKIAA-EKLEMVGLADEFWEKSPFEL-------SGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 499 AILVLDEPTEGLD---NISKQAVMNSVLQLKEhaSVLTITH---DPAllSQMDSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:PRK13643 164 EVLVLDEPTAGLDpkaRIEMMQLFESIHQSGQ--TVVLVTHlmdDVA--DYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
340-574 |
1.39e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.00 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQK----QALNNVSFELPAKQKVAIVGRSGSGKTtlvnlLSSLWPLqqGTIN----LQSDKEIISLHDLN 411
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKS-----VSSLAIM--GLIDypgrVMAEKLEFNGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 412 NESRAKTLNIL-AQQHHIF-DGTLSENLAYAapdaTSQQMIAALtQAELGGWFSELKQ---------GL---KTRLGTGG 477
Cdd:PRK11022 77 RISEKERRNLVgAEVAMIFqDPMTSLNPCYT----VGFQIMEAI-KVHQGGNKKTRRQraidllnqvGIpdpASRLDVYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 478 RNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPALLSQM-DSVIWLDSGQ 554
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAaHKIIVMYAGQ 231
|
250 260
....*....|....*....|..
gi 1949233634 555 IIAQGSHQQLLNE--HPDYVAL 574
Cdd:PRK11022 232 VVETGKAHDIFRAprHPYTQAL 253
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
340-555 |
3.10e-12 |
|
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: 66.12 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeIISLHDLNNeSRAKTL 419
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-------YIGGRDVTD-LPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NI--LAQQHHIF-DGTLSENLAY------AAPDATSQQM--IAALTQAElggwfsELKQGLKTRLgtggrnvSQGQSRRI 488
Cdd:cd03301 73 DIamVFQNYALYpHMTVYDNIAFglklrkVPKDEIDERVreVAELLQIE------HLLDRKPKQL-------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASVLTI--THDPALLSQM-DSVIWLDSGQI 555
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIyvTHDQVEAMTMaDRIAVMNDGQI 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
340-569 |
4.06e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQ----ALNNVSFELPAKQKVAIVGRSGSGKTtlVNLLSSLWPLQQGTINLQSDKEII-----SLHDL 410
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKS--VTALALMRLLEQAGGLVQCDKMLLrrrsrQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 NNESRAKTLNIL-AQQHHIFdgtlSENLAYAAPDATSQQMIAALTQAELGG----WFSELKQGL--------KTRLGTGG 477
Cdd:PRK10261 91 SEQSAAQMRHVRgADMAMIF----QEPMTSLNPVFTVGEQIAESIRLHQGAsreeAMVEAKRMLdqvripeaQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 478 RNVSQGQSRRIALAQALLQKPAILVLDEPTEGLD-NISKQAV-MNSVLQLKEHASVLTITHDPALLSQM-DSVIWLDSGQ 554
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQILqLIKVLQKEMSMGVIFITHDMGVVAEIaDRVLVMYQGE 246
|
250
....*....|....*..
gi 1949233634 555 IIAQGSHQQLLN--EHP 569
Cdd:PRK10261 247 AVETGSVEQIFHapQHP 263
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
347-565 |
4.06e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 347 YHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNNESR---------AK 417
Cdd:PRK15112 21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI--DDHPLHFGDYSYRSQrirmifqdpST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIFDGTLSENLAYAAPdATSQQMIAALTQAELggwfselkqgLKTRLGTGGRNVSQGQSRRIALAQALLQK 497
Cdd:PRK15112 99 SLNPRQRISQILDFPLRLNTDLEPE-QREKQIIETLRQVGL----------LPDHASYYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLL 565
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKqgISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVL 238
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
352-559 |
6.07e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.89 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 352 KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInLQSDKEIislhDLNNESRAKTLNILAQQ----HH 427
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV-LVGGKDI----ETNLDAVRQSLGMCPQHnilfHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 428 IfdgTLSEN-LAYAAPDATSQQMiaalTQAELGGWFSElkQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEP 506
Cdd:TIGR01257 1018 L---TVAEHiLFYAQLKGRSWEE----AQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 507 TEGLDNISKQAVMNSVLQLKEHASVLTITHdpallsQMDSVIWL-DSGQIIAQG 559
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTH------HMDEADLLgDRIAIISQG 1136
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
340-578 |
7.03e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiislHDLNN-ESRAKT 418
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG-------VDLSHvPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDG-TLSENLAYA-APDATSQQMIAALTQAELGgwFSELKQGLKTRlgtgGRNVSQGQSRRIALAQALLQ 496
Cdd:PRK11607 93 INMMFQSYALFPHmTVEQNIAFGlKQDKLPKAEIASRVNEMLG--LVHMQEFAKRK----PHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 497 KPAILVLDEPTEGLDNISKQAVMNSVLQLKEHASV--LTITHDPALLSQMDSVIW-LDSGQIIAQGSHQQLLnEHPdyva 573
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVtcVMVTHDQEEAMTMAGRIAiMNRGKFVQIGEPEEIY-EHP---- 241
|
....*
gi 1949233634 574 lTTRF 578
Cdd:PRK11607 242 -TTRY 245
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-566 |
8.58e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.65 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 349 YGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLwpLQ--QGTI-------------NLqsdKEI--------- 404
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVptSGEVrvlgyvpfkrrkeFA---RRIgvvfgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 405 ----ISLHDlnnesrakTLNILAQQHHIFDGTLSENLAYaapdatsqqMIAALtqaelggwfsELKQGLKTRLgtggRNV 480
Cdd:COG4586 107 lwwdLPAID--------SFRLLKAIYRIPDAEYKKRLDE---------LVELL----------DLGELLDTPV----RQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 481 SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDpallsqM-------DSVIWLD 551
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHD------MddiealcDRVIVID 229
|
250
....*....|....*
gi 1949233634 552 SGQIIAQGSHQQLLN 566
Cdd:COG4586 230 HGRIIYDGSLEELKE 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
357-560 |
9.28e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 9.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 357 NVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDlnnesRAKTLNILAQQHHI---F-DGT 432
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR----VLFD-----AEKGICLPPEKRRIgyvFqDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 433 L------SENLAYAAPDATSQQmiaaltqaelggwFSELKQ--GLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLD 504
Cdd:PRK11144 87 LfphykvRGNLRYGMAKSMVAQ-------------FDKIVAllGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 505 EPTEGLDNISKQAVMNSVLQLKEHAS--VLTITHD-PALLSQMDSVIWLDSGQIIAQGS 560
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINipILYVSHSlDEILRLADRVVVLEQGKVKAFGP 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
340-560 |
2.80e-11 |
|
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: 62.93 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLS--SLWPLQQGTINLQsDKEIIslhDLNNESRAK 417
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFK-GEDIT---DLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHI-FDG-TLSENLayaapdatsqqmiaaltqaelggwfselkqglktrlgtggRNV----SQGQSRRIALA 491
Cdd:cd03217 77 LGIFLAFQYPPeIPGvKNADFL----------------------------------------RYVnegfSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 492 QALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITHDPALLSQM--DSVIWLDSGQIIAQGS 560
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-556 |
3.21e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.91 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHYG-QKQALNNV--SFeLPAKqKVAIVGRSGSGKTTLVNLLSSLwplqqgtinlqsDKEIislhdlNNESRAK 417
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDIslSF-FPGA-KIGVLGLNGAGKSTLLRIMAGV------------DKEF------EGEARPA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 ---TLNILAQQHHIFDG-TLSENL-------------------AYAAPDATSQQMIAalTQAEL-------GGWF--SEL 465
Cdd:PRK11819 68 pgiKVGYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAA--EQGELqeiidaaDAWDldSQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 466 KQGLKT-RLGTGGRNV---SQGQSRRIALAQALLQKPAILVLDEPTEGLDniskqavMNSVLQLKEH-----ASVLTITH 536
Cdd:PRK11819 146 EIAMDAlRCPPWDAKVtklSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-------AESVAWLEQFlhdypGTVVAVTH 218
|
250 260
....*....|....*....|....
gi 1949233634 537 DPALLsqmDSVI-W---LDSGQII 556
Cdd:PRK11819 219 DRYFL---DNVAgWileLDRGRGI 239
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
340-555 |
3.45e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.96 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsdkeiislhdlnneSRAKTL 419
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------------AKGIKL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIF---DGTLSENLAYAAPDATSQQMiaaltQAELGGW-FselkQGLKTRLGTGgrNVSQGQSRRIALAQALL 495
Cdd:PRK10636 378 GYFAQHQLEFlraDESPLQHLARLAPQELEQKL-----RDYLGGFgF----QGDKVTEETR--RFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 496 QKPAILVLDEPTEGLDNISKQAVMNSVLQLKehASVLTITHDPALL-SQMDSVIWLDSGQI 555
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDFE--GALVVVSHDRHLLrSTTDDLYLVHDGKV 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
340-556 |
3.67e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSD------------KEIISL 407
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprNVEGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 408 HDLNNESRAKTLNILAQQHHIFDGTLSEnlayaapdaTSQQMIAALTQAE-----LGGWF--SELKQGLKtRLGTGG--- 477
Cdd:PRK11147 84 YDFVAEGIEEQAEYLKRYHDISHLVETD---------PSEKNLNELAKLQeqldhHNLWQleNRINEVLA-QLGLDPdaa 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 478 -RNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKehASVLTITHDPALLSQMDSVIW-LDSGQI 555
Cdd:PRK11147 154 lSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ--GSIIFISHDRSFIRNMATRIVdLDRGKL 231
|
.
gi 1949233634 556 I 556
Cdd:PRK11147 232 V 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
340-574 |
3.70e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.45 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYgQKQALNnVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINlqsdkeiislhdLNNESRAKT- 418
Cdd:PRK10771 2 LKLTDITWLY-HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT------------LNGQDHTTTp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 -----LNILAQQHHIFDG-TLSENLAYA-AP-----DATSQQMIAALTQAELGGWFSELKQGLktrlgtggrnvSQGQSR 486
Cdd:PRK10771 68 psrrpVSMLFQENNLFSHlTVAQNIGLGlNPglklnAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDniskQAVMNSVLQL------KEHASVLTITH---DPALLSQMDSVIwlDSGQIIA 557
Cdd:PRK10771 137 RVALARCLVREQPILLLDEPFSALD----PALRQEMLTLvsqvcqERQLTLLMVSHsleDAARIAPRSLVV--ADGRIAW 210
|
250
....*....|....*..
gi 1949233634 558 QGSHQQLLNEHPDYVAL 574
Cdd:PRK10771 211 DGPTDELLSGKASASAL 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
342-560 |
5.29e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.44 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQK----QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInLQSDKEIISLHDlnNESRAK 417
Cdd:PRK11153 4 LKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVDGQDLTALSE--KELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNI-LAQQHhiFD----GTLSENLAYAAPdatsqqmIAALTQAELGGWFSELKQ--GLKTRLGTGGRNVSQGQSRRIAL 490
Cdd:PRK11153 81 RRQIgMIFQH--FNllssRTVFDNVALPLE-------LAGTPKAEIKARVTELLElvGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDniskQAVMNSVLQL-KE-----HASVLTITHDPALLSQM-DSVIWLDSGQIIAQGS 560
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALD----PATTRSILELlKDinrelGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
340-556 |
5.80e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY---------GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDL 410
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE----PLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 NNESRA---KTLNILAQ--------QHHIFDgTLSE------NLAYAAPDATSQQMIAALtqaelggwfsELKQGLKTRL 473
Cdd:PRK10419 80 NRAQRKafrRDIQMVFQdsisavnpRKTVRE-IIREplrhllSLDKAERLARASEMLRAV----------DLDDSVLDKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 474 gtgGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDnISKQAVMNSV---LQLKEHASVLTITHDPALLSQMDS-VIW 549
Cdd:PRK10419 149 ---PPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD-LVLQAGVIRLlkkLQQQFGTACLFITHDLRLVERFCQrVMV 224
|
....*..
gi 1949233634 550 LDSGQII 556
Cdd:PRK10419 225 MDNGQIV 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
343-565 |
7.30e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 343 NNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKeiisLHDLNNESRAKTLNIL 422
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH----IQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 423 AQQhhifdgtlsenlAYAAPDATSQQMIAA---LTQAELGGWFSELKQGLKTRLGTGG---------RNVSQGQSRRIAL 490
Cdd:PRK10253 87 AQN------------ATTPGDITVQELVARgryPHQPLFTRWRKEDEEAVTKAMQATGithladqsvDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDnISKQA---VMNSVLQLKEHASVLTITHDpalLSQ----MDSVIWLDSGQIIAQGSHQQ 563
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLD-ISHQIdllELLSELNREKGYTLAAVLHD---LNQacryASHLIALREGKIVAQGAPKE 230
|
..
gi 1949233634 564 LL 565
Cdd:PRK10253 231 IV 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
340-553 |
7.35e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.49 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYH----YGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSslwplQQGTINLQSDkEIIslhdLNNESR 415
Cdd:cd03232 4 LTWKNLNYTvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA-----GRKTAGVITG-EIL----INGRPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNIL---AQQHHIFDGTLSenlayaapdatsqqMIAALTqaelggwFSELKQGLktrlgtggrnvSQGQSRRIALAQ 492
Cdd:cd03232 74 DKNFQRStgyVEQQDVHSPNLT--------------VREALR-------FSALLRGL-----------SVEQRKRLTIGV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDP--ALLSQMDSVIWLDSG 553
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGqAILCTIHQPsaSIFEKFDRLLLLKRG 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
336-553 |
9.81e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 336 KHWALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSslwplQQGTINLQSDKEIISLHDLNNESR 415
Cdd:TIGR00956 760 FHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA-----ERVTTGVITGGDRLVNGRPLDSSF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNILAQQH-HIFDGTLSENLAYAA----PDATS--------QQMIAALtqaelggwfsELKQGLKTRLGTGGRNVSQ 482
Cdd:TIGR00956 835 QRSIGYVQQQDlHLPTSTVRESLRFSAylrqPKSVSksekmeyvEEVIKLL----------EMESYADAVVGVPGEGLNV 904
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 483 GQSRRIALAQALLQKPAILV-LDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPA--LLSQMDSVIWLDSG 553
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGqAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
339-565 |
1.04e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTIN-LQSDkeiislhdlnnesrak 417
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGD---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 tlniLAQQHHIFD-----------------GTLS--ENLAYAA-----PDATSQQMIAALTQA------------ELGGw 461
Cdd:NF033858 65 ----MADARHRRAvcpriaympqglgknlyPTLSvfENLDFFGrlfgqDAAERRRRIDELLRAtglapfadrpagKLSG- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 462 fselkqGLKTRLGtggrnvsqgqsrriaLAQALLQKPAILVLDEPTEGLDNISKQ---AVMNSVLQLKEHASVLTITH-- 536
Cdd:NF033858 140 ------GMKQKLG---------------LCCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRAERPGMSVLVATAym 198
|
250 260
....*....|....*....|....*....
gi 1949233634 537 DPAllSQMDSVIWLDSGQIIAQGSHQQLL 565
Cdd:NF033858 199 EEA--ERFDWLVAMDAGRVLATGTPAELL 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
257-574 |
1.46e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.55 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 257 AMLSSIVTIVPLVFSGAMVnvelaMLSLFVLASFESVL------LLPNA----FIELPYVLKAAERLFILEDKTLSTNnV 326
Cdd:TIGR01271 315 GFFVVFLSVVPYALIKGII-----LRRIFTTISYCIVLrmtvtrQFPGAiqtwYDSLGAITKIQDFLCKEEYKTLEYN-L 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 327 STTDIELLN--KHW-------------------------ALSLNNVSYHYgqKQALNNVSFELPAKQKVAIVGRSGSGKT 379
Cdd:TIGR01271 389 TTTEVEMVNvtASWdegigelfekikqnnkarkqpngddGLFFSNFSLYV--TPVLKNISFKLEKGQLLAVAGSTGSGKS 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 380 TLVNL-LSSLWPlqqgtinlqSDKEIislhdlnneSRAKTLNILAQQHHIFDGTLSENLAYAAP-DATSQQMIAALTQAE 457
Cdd:TIGR01271 467 SLLMMiMGELEP---------SEGKI---------KHSGRISFSPQTSWIMPGTIKDNIIFGLSyDEYRYTSVIKACQLE 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 458 LGgwFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVL-QLKEHASVLTITH 536
Cdd:TIGR01271 529 ED--IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLcKLMSNKTRILVTS 606
|
330 340 350
....*....|....*....|....*....|....*...
gi 1949233634 537 DPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDYVAL 574
Cdd:TIGR01271 607 KLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
339-555 |
1.62e-10 |
|
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: 60.14 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSyhygQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQ-SDKEIISLHDLNN----- 412
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgKPVTRRSPRDAIRagiay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 --ESRAKTLNILAQqhhifdgTLSENLAyaapdatsqqmiaaltqaeLGGWFSelkqglktrlgtGGrNVsQgqsrRIAL 490
Cdd:cd03215 80 vpEDRKREGLVLDL-------SVAENIA-------------------LSSLLS------------GG-NQ-Q----KVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITHD-PALLSQMDSVIWLDSGQI 555
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
335-555 |
1.64e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 335 NKHW-ALSLNNVSYHYG-QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDLNn 412
Cdd:PRK10522 317 FPDWqTLELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL--DGKPVTAEQPE- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 413 ESRAKTLNILAQqHHIFDGTLsENLAYAAPDATSQQmiaaltqaelggWFSELKQGLKTRLgTGGR----NVSQGQSRRI 488
Cdd:PRK10522 394 DYRKLFSAVFTD-FHLFDQLL-GPEGKPANPALVEK------------WLERLKMAHKLEL-EDGRisnlKLSKGQKKRL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVL-QLKEHA-SVLTITHDPALLSQMDSVIWLDSGQI 555
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRREFYQVLLpLLQEMGkTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
352-560 |
2.13e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 352 KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlqsdkeiislhdlnneSRAKTLNILAQQHHIFDG 431
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 432 TLSENLAYAAPDATSQ--------QMIAALTQaeLGGwfselkqGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVL 503
Cdd:PTZ00243 736 TVRGNILFFDEEDAARladavrvsQLEADLAQ--LGG-------GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 504 DEPTEGLDNISKQAVMNSVL--QLKEHASVLTiTHDPALLSQMDSVIWLDSGQIIAQGS 560
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECFlgALAGKTRVLA-THQVHVVPRADYVVALGDGRVEFSGS 864
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
340-571 |
3.49e-10 |
|
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: 61.03 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQkqALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINlqsdkeiislhdlnnesRAKTL 419
Cdd:cd03291 40 LFFSNLCLVGAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------------HSGRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDGTLSENLAYAAP-DATSQQMIAALTQAELGgwFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKP 498
Cdd:cd03291 101 SFSSQFSWIMPGTIKENIIFGVSyDEYRYKSVVKACQLEED--ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNS-VLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLNEHPDY 571
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-545 |
5.93e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInlQSDKEIIslhDLNNESRAKTL 419
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI--LFERQSI---KKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDG-TLSENLAYAAPDATSQQMIAALTQAELGGWFSELKQGLktrlgtggrnVSQGQSRRIALAQALLQKP 498
Cdd:PRK13540 77 CFVGHRSGINPYlTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSV-LQLKEHASVLTITHDPALLSQMD 545
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIqEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
340-560 |
6.54e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.86 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQK----QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInLQSDKEIISLHDlnNESR 415
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV-LVDGVDLTALSE--RELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNI---------LAQQhhifdgTLSENLAYaapdatsqqmiaALtqaELGGWF-SELKQ---------GLKTRLGTG 476
Cdd:COG1135 79 AARRKIgmifqhfnlLSSR------TVAENVAL------------PL---EIAGVPkAEIRKrvaellelvGLSDKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 477 GRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQavmnSVLQL------KEHASVLTITHdpallsQM------ 544
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR----SILDLlkdinrELGLTIVLITH------EMdvvrri 207
|
250
....*....|....*..
gi 1949233634 545 -DSVIWLDSGQIIAQGS 560
Cdd:COG1135 208 cDRVAVLENGRIVEQGP 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
347-572 |
9.05e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 347 YHYgqkqALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHDLNNESRAKTLNIlaQQH 426
Cdd:PRK13545 36 YHY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENI--ELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 427 HIFDGTLSENLAYAAPDatsqqmiaALTQAELGGWfseLKQGLKTrlgtggrnVSQGQSRRIALAQALLQKPAILVLDEP 506
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPE--------IIEFADIGKF---IYQPVKT--------YSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949233634 507 TEGLDNISKQAVMNSVLQLKEHA-SVLTITHDpalLSQMDS----VIWLDSGQIIAQGSHQQLLNEHPDYV 572
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKEQGkTIFFISHS---LSQVKSfctkALWLHYGQVKEYGDIKEVVDHYDEFL 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
341-566 |
1.18e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 341 SLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDLNNESRAKTLN 420
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ----PLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 421 ILAQQHHIFDG-TLSENLA------------YAAPDatSQQMIAALTQAELGGWFSELKQGLktrlgtggrnvSQGQSRR 487
Cdd:PRK10575 89 YLPQQLPAAEGmTVRELVAigrypwhgalgrFGAAD--REKVEEAISLVGLKPLAHRLVDSL-----------SGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 488 IALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA--SVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQL 564
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAEL 235
|
..
gi 1949233634 565 LN 566
Cdd:PRK10575 236 MR 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
354-559 |
1.27e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 57.72 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 354 ALNNVSFELPAKQKVAIVGRSGSGKTTLVNllsslwplqqGTINLQSDKEIISlhDLNNESRAKTlnilaqqhhIFDGTL 433
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN----------EGLYASGKARLIS--FLPKFSRNKL---------IFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 434 SenlayaapdatsqqmiaALTQAELGgwFSELKQGLKTrlgtggrnVSQGQSRRIALAQALLQ--KPAILVLDEPTEGLD 511
Cdd:cd03238 69 Q-----------------FLIDVGLG--YLTLGQKLST--------LSGGELQRVKLASELFSepPGTLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 512 NISKQAVMNSVLQL-KEHASVLTITHDPALLSQMDSVIWL------DSGQIIAQG 559
Cdd:cd03238 122 QQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
342-525 |
1.77e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPlqQGTIN-------LQSDKEII--------- 405
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGYSNdltlfgrRRGSGETIwdikkhigy 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 406 ---SLH-DLNNESRAKTLnILAQqhhIFDgtlSENLAYAAPDAtsQQMIAAltqaelgGWFSELkqGLKTRLGTGG-RNV 480
Cdd:PRK10938 341 vssSLHlDYRVSTSVRNV-ILSG---FFD---SIGIYQAVSDR--QQKLAQ-------QWLDIL--GIDKRTADAPfHSL 402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1949233634 481 SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL 525
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVL 447
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
340-553 |
2.54e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTlvnLLSSLWplqqGTINLQSDKEIISLHDLNNESRAKTL 419
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKST---LLRLLA----GALKGTPVAGCVDVPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDGT-------LSENLAYAAPdatsqqmiaaltqaelggwFSELkqglktrlgtggrnvSQGQSRRIALAQ 492
Cdd:COG2401 104 DAIGRKGDFKDAVellnavgLSDAVLWLRR-------------------FKEL---------------STGQKFRFRLAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEH-ASVLTITHDPALLS--QMDSVIWLDSG 553
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAgITLVVATHHYDVIDdlQPDLLIFVGYG 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
340-567 |
3.16e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiISLHDLNNESRAKT- 418
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN----INYNKLDHKLAAQLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDG-TLSENLaYAAPDATSQQM-IAALTQAELGGWFSE--LKQGLKTRLGTGGRNVSQGQSRRIALAQAL 494
Cdd:PRK09700 82 IGIIYQELSVIDElTVLENL-YIGRHLTKKVCgVNIIDWREMRVRAAMmlLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQ---AVMNsvlQL-KEHASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDylfLIMN---QLrKEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
340-552 |
4.94e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHY-GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTInLQSDKEIISLHDlnnesrakt 418
Cdd:PLN03073 509 ISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAVFS--------- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 lnilaqQHHIFDGTLSEN-LAYAA---PDATSQQMIAALTQAELGGWFSelKQGLKTrlgtggrnVSQGQSRRIALAQAL 494
Cdd:PLN03073 579 ------QHHVDGLDLSSNpLLYMMrcfPGVPEQKLRAHLGSFGVTGNLA--LQPMYT--------LSGGQKSRVAFAKIT 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 495 LQKPAILVLDEPTEGLDNISKQAVMNSVLQLKehASVLTITHDPALLSQMDSVIWLDS 552
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ--GGVLMVSHDEHLISGSVDELWVVS 698
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
339-542 |
9.02e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsdkeiislhdlnneSRAKT 418
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------------SENAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQH-HIFDG--TLSENLAYAAPDATSQQMIaaltQAELGGW-FS--ELKQGLKtrlgtggrNVSQGQSRRIALAQ 492
Cdd:PRK15064 384 IGYYAQDHaYDFENdlTLFDWMSQWRQEGDDEQAV----RGTLGRLlFSqdDIKKSVK--------VLSGGEKGRMLFGK 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAvMNSVLQLKEhASVLTITHDPALLS 542
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIES-LNMALEKYE-GTLIFVSHDREFVS 499
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
340-567 |
1.15e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGtiNLQSDKEIISLhdlnnesraktL 419
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--ERQSQFSHITR-----------L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHIFDGTLSENLAYAAPDA-----TSQQMI------AALTQaELGGWFselkqGLKTRLGTGGRNVSQGQSRRI 488
Cdd:PRK10938 71 SFEQLQKLVSDEWQRNNTDMLSPGEddtgrTTAEIIqdevkdPARCE-QLAQQF-----GITALLDRRFKYLSTGETRKT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 489 ALAQALLQKPAILVLDEPTEGLDNISKQAVMN--SVLQLKEHASVLTITHDPALLSQMDSVIWLDSGQIIAQGSHQQLLN 566
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAEllASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
.
gi 1949233634 567 E 567
Cdd:PRK10938 225 Q 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
353-574 |
1.26e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.02 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 353 QALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGtinlqsdkEIISL-HDLNNESRAKTLNILAQQHHIFdg 431
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDG--------EVAWLgKDLLGMKDDEWRAVRSDIQMIF-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 432 tlSENLAYAAPDATSQQMIAAltqaELGGWFSEL-KQGLKTRLGTGGRNV--------------SQGQSRRIALAQALLQ 496
Cdd:PRK15079 105 --QDPLASLNPRMTIGEIIAE----PLRTYHPKLsRQEVKDRVKAMMLKVgllpnlinryphefSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 497 KPAILVLDEPTEGLDnISKQA-VMNSVLQL-KEHA-SVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLLN--EHPD 570
Cdd:PRK15079 179 EPKLIICDEPVSALD-VSIQAqVVNLLQQLqREMGlSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHnpLHPY 257
|
....
gi 1949233634 571 YVAL 574
Cdd:PRK15079 258 TKAL 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
354-569 |
1.59e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 354 ALNNVSFELPAKQKVAIVGRSGSGKT----TLVNLLSSlwplqQGTIN---LQSDKEIISL--HDLNnESRAKTLNILAQ 424
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIGgsaTFNGREILNLpeKELN-KLRAEQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 425 qhhifDGTLSEN------------------LAYAAPDATSQQMIAALTQAELggwfselkqglKTRLGTGGRNVSQGQSR 486
Cdd:PRK09473 105 -----DPMTSLNpymrvgeqlmevlmlhkgMSKAEAFEESVRMLDAVKMPEA-----------RKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 487 RIALAQALLQKPAILVLDEPTEGLDnISKQA-VMNSVLQLKE--HASVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQ 562
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALD-VTVQAqIMTLLNELKRefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNAR 247
|
....*....
gi 1949233634 563 QLLNE--HP 569
Cdd:PRK09473 248 DVFYQpsHP 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
340-561 |
1.85e-08 |
|
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: 57.14 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPlqQGTIN---LQSDKEIISLHDLNNEsrA 416
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP--HGTWDgeiYWSGSPLKASNIRDTE--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 417 KTLNILAQQHHIF-DGTLSENLaYAAPDATSQQMIAAltQAELGGWFSELKQGLKTRLGTGGRNVSQ---GQSRRIALAQ 492
Cdd:TIGR02633 78 AGIVIIHQELTLVpELSVAENI-FLGNEITLPGGRMA--YNAMYLRAKNLLRELQLDADNVTRPVGDyggGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 493 ALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDpalLSQMDSVIwlDSGQIIAQGSH 561
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGvACVYISHK---LNEVKAVC--DTICVIRDGQH 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
339-536 |
2.11e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsDKEIISLHDlNNESRAKT 418
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL--DGEPVRFRS-PRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNILAQQHHIFDgTLS--ENLAYAAPDATS-----QQMIAALTQAelggwFSELkqGLKTRLGTGGRNVSQGQSRRIALA 491
Cdd:COG1129 81 IAIIHQELNLVP-NLSvaENIFLGREPRRGglidwRAMRRRAREL-----LARL--GLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1949233634 492 QALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH-ASVLTITH 536
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISH 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-559 |
2.27e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 351 QKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSlwPLQ----QGTInLQSDKEIislhdlnNESRAKTLNILAQQH 426
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQgnnfTGTI-LANNRKP-------TKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 427 HIFDG-TLSENLAYAA----PDATSQQ---MIAALTQAELGgwfseLKQGLKTRLG-TGGRNVSQGQSRRIALAQALLQK 497
Cdd:PLN03211 150 ILYPHlTVRETLVFCSllrlPKSLTKQekiLVAESVISELG-----LTKCENTIIGnSFIRGISGGERKRVSIAHEMLIN 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 498 PAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDP-ALLSQM-DSVIWLDSGQIIAQG 559
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGkTIVTSMHQPsSRVYQMfDSVLVLSEGRCLFFG 289
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
340-569 |
2.29e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ----KQALNNVSFELPAKQKVAIVGRSGSGKTtlVNLLSSLWPLQ-------QGTINLQSDKeiiSLH 408
Cdd:PRK15134 6 LAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSILRLLPsppvvypSGDIRFHGES---LLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 409 DLNNESRAKTLNILA---QQH-------HIFDGTLSENLAY---AAPDATSQQMIAALTQAELggwfselkQGLKTRLGT 475
Cdd:PRK15134 81 ASEQTLRGVRGNKIAmifQEPmvslnplHTLEKQLYEVLSLhrgMRREAARGEILNCLDRVGI--------RQAAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 476 GGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDnISKQAVMNSVL-QLKE--HASVLTITHDPALLSQM-DSVIWLD 551
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD-VSVQAQILQLLrELQQelNMGLLFITHNLSIVRKLaDRVAVMQ 231
|
250 260
....*....|....*....|
gi 1949233634 552 SGQIIAQGSHQQLLN--EHP 569
Cdd:PRK15134 232 NGRCVEQNRAATLFSapTHP 251
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
23-275 |
3.36e-08 |
|
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: 55.25 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 23 FLASLTVLANVGLLAISGWFLASMAAAGIASVHMNY-FTPAGTIRFLAIVRTASRYAERLVTHNATFLLLSEIRVNMFAT 101
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLlLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 102 LSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALICFVGIIIIGVIIpAILS 181
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL-RYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 182 KQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQArnqqltkcdllsEQYNQQLF------IRHKALGNADGLSLLIVQ 255
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAA------------EEREIERFreanrdLRDANLRAARLSALFSPL 228
|
250 260
....*....|....*....|
gi 1949233634 256 LAMLSSIVTIVPLVFSGAMV 275
Cdd:cd07346 229 IGLLTALGTALVLLYGGYLV 248
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-572 |
4.08e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.81 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 350 GQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQS-DKEIISLHDLNNESRAKTLNILAQQHHI 428
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvDIAKISDAELREVRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 429 FDGTLSENLAYAAPDATsqqmIAALTQAELGgwFSELKQ-GLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPT 507
Cdd:PRK10070 119 PHMTVLDNTAFGMELAG----INAEERREKA--LDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 508 EGLDNISKQAVMNSV--LQLKEHASVLTITHD-PALLSQMDSVIWLDSGQIIAQGSHQQLLNEHP-DYV 572
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAnDYV 261
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
339-536 |
2.17e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEIislhDLNNESRAKT 418
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID-GKPV----RIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 LNI-LAQQH-HIFDG-TLSENLAYAAPD--------ATSQQMIAALTQaelggwfselKQGLKTRLgtgGRNVSQ---GQ 484
Cdd:COG3845 80 LGIgMVHQHfMLVPNlTVAENIVLGLEPtkggrldrKAARARIRELSE----------RYGLDVDP---DAKVEDlsvGE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 485 SRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITH 536
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITH 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
355-565 |
2.71e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdKEII--SLHD-LNN------ESRAKtlnilaqq 425
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-HEVVtrSPQDgLANgivyisEDRKR-------- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 426 hhifDG-----TLSENLAYAAPDATSQQMIAALTQAE--LGGWFSELKQgLKT-----RLGtggrNVSQGQSRRIALAQA 493
Cdd:PRK10762 339 ----DGlvlgmSVKENMSLTALRYFSRAGGSLKHADEqqAVSDFIRLFN-IKTpsmeqAIG----LLSGGNQQKVAIARG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 494 LLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITHD-PALLSQMDSVIWLDSGQI-----IAQGSHQQLL 565
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEmPEVLGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
355-578 |
5.54e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEII----SLHDLNNESRAKTLNILAQQHHifd 430
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTlngePLAAIDAPRLARLRAVLPQAAQ--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 431 gtlsENLAYAAPDATS------QQMIAALTQAELG-GWFSELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQ------- 496
Cdd:PRK13547 94 ----PAFAFSAREIVLlgryphARRAGALTHRDGEiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 497 --KPAILVLDEPTEGLDNISKQAVMNSVLQLKE--HASVLTITHDPALLSQ-MDSVIWLDSGQIIAQGSHQQLLNehPDY 571
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLT--PAH 247
|
....*..
gi 1949233634 572 VALTTRF 578
Cdd:PRK13547 248 IARCYGF 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
356-568 |
6.17e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 356 NNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQ-QGTINLQSdKEIislhDLNNESRAKTLNILA-----QQHHIF 429
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDG-KPV----KIRNPQQAIAQGIAMvpedrKRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 430 -DGTLSENLAYAAPDATSQQMI--AALTQAELGGWFSELKqgLKT---RLGTGgrNVSQGQSRRIALAQALLQKPAILVL 503
Cdd:PRK13549 354 pVMGVGKNITLAALDRFTGGSRidDAAELKTILESIQRLK--VKTaspELAIA--RLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949233634 504 DEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHD-PALLSQMDSVIWLDSGQIIAQGSHQQLLNEH 568
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
352-563 |
6.78e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 352 KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLHDLNNESRAKTLNILAQQHHIFDG 431
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 432 TLSENLAYAA--------PDATSQQM----IAALTQAELGgwfseLKQGLKTRLGTGG-RNVSQGQSRRIALAQALLQKP 498
Cdd:TIGR00956 154 TVGETLDFAArcktpqnrPDGVSREEyakhIADVYMATYG-----LSHTRNTKVGNDFvRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 499 AILVLDEPTEGLDNISKQAVMNSvlqLKEHASVLTITHDPALL--SQ-----MDSVIWLDSGQIIAQGSHQQ 563
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRA---LKTSANILDTTPLVAIYqcSQdayelFDKVIVLYEGYQIYFGPADK 297
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
340-559 |
6.89e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.95 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQ----KQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGtinlqsdkeiislhdLNNESR 415
Cdd:cd03233 4 LSWRNISFTTGKgrskIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS---------------VEGDIH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 416 AKTLNIlAQQHHIFDGTLSENlayaapdatSQQ--MIAALTqaelggwfseLKQGLKTRLGTGG----RNVSQGQSRRIA 489
Cdd:cd03233 69 YNGIPY-KEFAEKYPGEIIYV---------SEEdvHFPTLT----------VRETLDFALRCKGnefvRGISGGERKRVS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949233634 490 LAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLTITHDPA--LLSQMDSVIWLDSGQIIAQG 559
Cdd:cd03233 129 IAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMadVLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
474-564 |
8.15e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 474 GTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHDPALLSQM-DSVIWLD 551
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLaHELTVID 218
|
90
....*....|...
gi 1949233634 552 SGQIIAQGSHQQL 564
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
337-528 |
9.04e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 337 HWALSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPlqQGTInlqsDKEII----SLHDLN- 411
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HGTY----EGEIIfegeELQASNi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 412 NESRAKTLNILAQQ----------HHIFDG---TLSENLAYAAPDATSQQMIAALtqaelggwfselkqGLKTRLGTGGR 478
Cdd:PRK13549 77 RDTERAGIAIIHQElalvkelsvlENIFLGneiTPGGIMDYDAMYLRAQKLLAQL--------------KLDINPATPVG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1949233634 479 NVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH 528
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
355-567 |
9.33e-07 |
|
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: 51.75 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQ-QGTInlqsdkeIISLHDLNNESRAKTLN---ILAQQHHIFD 430
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNV-------FINGKPVDIRNPAQAIRagiAMVPEDRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 431 GTLS-----ENLAYAAPDATSQQMIAAlTQAELGGWFSELKQgLKTR-----LGTGGrnVSQGQSRRIALAQALLQKPAI 500
Cdd:TIGR02633 349 GIVPilgvgKNITLSVLKSFCFKMRID-AAAELQIIGSAIQR-LKVKtaspfLPIGR--LSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949233634 501 LVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHD-PALLSQMDSVIWLDSGQIIAQGSHQQLLNE 567
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGDFVNHALTQE 493
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
340-567 |
1.00e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSyhygQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPlQQGTINLQSDkeiiSLHDLNNESRAKTL 419
Cdd:PRK03695 1 MQLNDVA----VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQ----PLEAWSAAELARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQH---------HIFDGTLSENLAYAAPDATSQQMIAALtqaelggwfselkqGLKTRLGTGGRNVSQGQSRRIAL 490
Cdd:PRK03695 72 AYLSQQQtppfampvfQYLTLHQPDKTRTEAVASALNEVAEAL--------------GLDDKLGRSVNQLSGGEWQRVRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 491 AQALLQ-KPAI------LVLDEPTEGLDnISKQAVMNSVlqLKEHA----SVLTITHDpaL---LSQMDSVIWLDSGQII 556
Cdd:PRK03695 138 AAVVLQvWPDInpagqlLLLDEPMNSLD-VAQQAALDRL--LSELCqqgiAVVMSSHD--LnhtLRHADRVWLLKQGKLL 212
|
250
....*....|.
gi 1949233634 557 AQGSHQQLLNE 567
Cdd:PRK03695 213 ASGRRDEVLTP 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
340-536 |
1.85e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKeiislHDLNN--ESRAK 417
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFASttAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHIF-DGTLSENLayaapdatsqqMIAALTQAelGGWF--SELKQGLKTRLGTGGRNV---------SQGQS 485
Cdd:PRK11288 80 GVAIIYQELHLVpEMTVAENL-----------YLGQLPHK--GGIVnrRLLNYEAREQLEHLGVDIdpdtplkylSIGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITH 536
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRaEGRVILYVSH 198
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
355-540 |
2.69e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIIslhdlnnesraktlnILAQQHHIFDGTLS 434
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLF---------------YVPQRPYMTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 435 ENLAYaaPDATSQQMIAALTQAELGGWFSELKQGLKTRLGTGGRNV-------SQGQSRRIALAQALLQKPAILVLDEPT 507
Cdd:TIGR00954 533 DQIIY--PDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVqdwmdvlSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|...
gi 1949233634 508 EGLdNISKQAVMNSVLQlKEHASVLTITHDPAL 540
Cdd:TIGR00954 611 SAV-SVDVEGYMYRLCR-EFGITLFSVSHRKSL 641
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-559 |
2.79e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.11 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 345 VSYHYGQKqALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLqsdkeiisLHDLNNESRAKTLNILAQ 424
Cdd:PRK15056 14 VTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI--------LGQPTRQALQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 425 QHHIFDGT---LSENLAYAA----------PDATSQQMI-AALTQAELggwfSELKQglkTRLGtggrNVSQGQSRRIAL 490
Cdd:PRK15056 85 QSEEVDWSfpvLVEDVVMMGryghmgwlrrAKKRDRQIVtAALARVDM----VEFRH---RQIG----ELSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLK-EHASVLTITHDPALLSQMDSVIWLDSGQIIAQG 559
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-569 |
5.40e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 354 ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdKEIISLHDLNNESRAKTLNILAQQHHI-FDGT 432
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-QRIDTLSPGKLQALRRDIQFIFQDPYAsLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 433 LSENLAYAAPdATSQQMIAALTQAELGGWFSElKQGLKTRLG-TGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLD 511
Cdd:PRK10261 418 QTVGDSIMEP-LRVHGLLPGKAAAARVAWLLE-RVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 512 NISKQAVMNSVLQLKEHASV--LTITHDPAL---LSQMDSVIWLdsGQIIAQGSHQQLLN--EHP 569
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIayLFISHDMAVverISHRVAVMYL--GQIVEIGPRRAVFEnpQHP 558
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
340-565 |
8.19e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.30 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDkeiiSLHDLNNESRAKTL 419
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD----DVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQqhhifDGTLSENLAYAapdaTSQQMIAALTQAELGGWFSELKQGLKTRLGTGG---------RNVSQGQSRRIAL 490
Cdd:PRK09536 80 ASVPQ-----DTSLSFEFDVR----QVVEMGRTPHRSRFDTWTETDRAAVERAMERTGvaqfadrpvTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 491 AQALLQKPAILVLDEPTEGLDnISKQA-VMNSVLQLKEHA-SVLTITHDPALLSQM-DSVIWLDSGQIIAQGSHQQLL 565
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD-INHQVrTLELVRRLVDDGkTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
355-559 |
8.25e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNllsslwplqqGTINLQSDKEIIslhdlnnesraKTLNILAQQhhiFDGTLS 434
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAF----------DTIYAEGQRRYV-----------ESLSAYARQ---FLGQMD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 435 -------ENLAYAApdATSQQMIAALTQAELGGwFSEL---------KQGLKTRLG----------TGGRNV---SQGQS 485
Cdd:cd03270 67 kpdvdsiEGLSPAI--AIDQKTTSRNPRSTVGT-VTEIydylrllfaRVGIRERLGflvdvglgylTLSRSAptlSGGEA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 486 RRIALAQALLQK--PAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQMDSVIWL------DSGQII 556
Cdd:cd03270 144 QRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGnTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIV 223
|
...
gi 1949233634 557 AQG 559
Cdd:cd03270 224 AQG 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
472-564 |
8.92e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 472 RLGTGGRNVSQGQSRRIALAQALLQK---PAILVLDEPTEGL--DNISKqaVMNSVLQLKEHA-SVLTITHDPALLSQMD 545
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfDDIKK--LLEVLQRLVDKGnTVVVIEHNLDVIKTAD 899
|
90 100
....*....|....*....|....*
gi 1949233634 546 SVIWL------DSGQIIAQGSHQQL 564
Cdd:TIGR00630 900 YIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
340-560 |
2.19e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.17 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSS--LWPLQQGTINLQSdkeiISLHDLNNESRAK 417
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKG----ESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 TLNILAQQHHI-FDGTLSEN---LAYaapdaTSQQMIAALTQAELGGWFSELKQGLK------TRLGtggRNV----SQG 483
Cdd:CHL00131 84 LGIFLAFQYPIeIPGVSNADflrLAY-----NSKRKFQGLPELDPLEFLEIINEKLKlvgmdpSFLS---RNVnegfSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 484 QSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQM--DSVIWLDSGQIIAQGS 560
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEnSIILITHYQRLLDYIkpDYVHVMQNGKIIKTGD 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
342-511 |
2.28e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNL-LSSLWPlQQGTINLQSDKEiISLHDlnnesraktln 420
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHCGTKLE-VAYFD----------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 421 ilaqQHHIF---DGTLSENLAyaapDATSQQMIAALTQAELGgwfsELKQGL--KTRLGTGGRNVSQGQSRRIALAQALL 495
Cdd:PRK11147 389 ----QHRAEldpEKTVMDNLA----EGKQEVMVNGRPRHVLG----YLQDFLfhPKRAMTPVKALSGGERNRLLLARLFL 456
|
170
....*....|....*..
gi 1949233634 496 qKPA-ILVLDEPTEGLD 511
Cdd:PRK11147 457 -KPSnLLILDEPTNDLD 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
343-537 |
2.39e-05 |
|
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: 47.24 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 343 NNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSDKEIISLhdlnNESRaktlnil 422
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYV----DQSR------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 423 aqqhhifdgtlsENLayaAPDATSQQMIA-ALTQAELG----------GWFSELKQGLKTRLGtggrNVSQGQSRRIALA 491
Cdd:TIGR03719 395 ------------DAL---DPNKTVWEEISgGLDIIKLGkreipsrayvGRFNFKGSDQQKKVG----QLSGGERNRVHLA 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1949233634 492 QALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKehASVLTITHD 537
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVVISHD 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
357-555 |
3.21e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 357 NVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiislHDLNNESrakTLNILA----------QQH 426
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG-------KEINALS---TAQRLArglvylpedrQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 427 HIF-DGTLSENlayaapdatsqqmIAALTQAELGGW--------------------FSELKQGLKTrlgtggrnVSQGQS 485
Cdd:PRK15439 351 GLYlDAPLAWN-------------VCALTHNRRGFWikparenavleryrralnikFNHAEQAART--------LSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 486 RRIALAQALLQKPAILVLDEPTEGLDniskQAVMNSVLQL-----KEHASVLTITHDPALLSQM-DSVIWLDSGQI 555
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVD----VSARNDIYQLirsiaAQNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-275 |
3.33e-05 |
|
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: 45.88 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 18 MLLGTFLASLTVLANVGLLAISGWFLASMAAAGiaSVHMNYFTPAGTIrFLAIVRTASRYAERLVTHNATFLLLSEIRVN 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEK--DLEALLLVPLAII-GLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 98 MFAtlsKLNNLDLA---MSRSADLVNRLQNDVDALDK-----------------------FYLNVLLpMLVALLTVPIIM 151
Cdd:cd18552 78 LFD---KLLRLPLSffdRNSSGDLISRITNDVNQVQNaltsaltvlvrdpltvigllgvlFYLDWKL-TLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 152 LFMSaynvnvalicfvgiiiigviipaILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKcdllSEQ 231
Cdd:cd18552 154 LPIR-----------------------RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKR----FRK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1949233634 232 YNQQLFIRHKALGNADGLSLLIVQlaMLSSIVTIVPLVFSGAMV 275
Cdd:cd18552 207 ANERLRRLSMKIARARALSSPLME--LLGAIAIALVLWYGGYQV 248
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
23-166 |
3.92e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU 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 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: 349986 [Multi-domain] Cd Length: 292 Bit Score: 45.89 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 23 FLASLTVLANVGLLAISGWFLASMAAAGIASVHMNYFTP-AGTIRFLAIVRTASRYAERLVTHNATFLLLSEIRVNMFat 101
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLlALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY-- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 102 lSKLNNLDLA---MSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALICF 166
Cdd:cd18542 80 -DHLQRLSFSfhdKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISL 146
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
357-560 |
4.13e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.46 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 357 NVSFELPAKQKVAIVGRSGSGKT-TLVNLLSSLWP-LQQGTINLQSDKEIISLHDLnnesRAKTLNILAQQH-------H 427
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgVRQTAGRVLLDGKPVAPCAL----RGRKIATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 428 IFDGTLSENLAYAAPDATSQQMIAALTQAELGGwfselkqgLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPT 507
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAALEAVGLEN--------AARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 508 EGLDNISKQAVMNSVLQL-KEHA-SVLTITHDPALLSQM-DSVIWLDSGQIIAQGS 560
Cdd:PRK10418 169 TDLDVVAQARILDLLESIvQKRAlGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGD 224
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
340-548 |
5.51e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNV-SYHYGQKqalnnVSFELPAkqkVAIVGRSGSGKTTLVN-LLSSLWPLQ-QGTINLQSDKEIISLH------DL 410
Cdd:cd03240 4 LSIRNIrSFHERSE-----IEFFSPL---TLIVGQNGAGKTTIIEaLKYALTGELpPNSKGGAHDPKLIREGevraqvKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 411 NNESRAKTLNILAQQHHIFdgtlsENLAYaapdaTSQQMIAALTQAELGgwfselkqglktRLgTGGRNVSQGQSRRIAL 490
Cdd:cd03240 76 AFENANGKKYTITRSLAIL-----ENVIF-----CHQGESNWPLLDMRG------------RC-SGGEKVLASLIIRLAL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 491 AQALLQKPAILVLDEPTEGLD--NISKQAV--MNSVLQLKeHASVLTITHDPALLSQMDSVI 548
Cdd:cd03240 133 AETFGSNCGILALDEPTTNLDeeNIEESLAeiIEERKSQK-NFQLIVITHDEELVDAADHIY 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
340-510 |
5.93e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINlqsdkeiISLHDLNNESRAKT- 418
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE-------IGGNPCARLTPAKAh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 419 ---LNILAQQHHIFDG-TLSENLAY--AAPDATSQQMIAALTQaelggwfseLKQGLKTRLGTGGRNVSQGQSRRIalAQ 492
Cdd:PRK15439 85 qlgIYLVPQEPLLFPNlSVKENILFglPKRQASMQKMKQLLAA---------LGCQLDLDSSAGSLEVADRQIVEI--LR 153
|
170
....*....|....*...
gi 1949233634 493 ALLQKPAILVLDEPTEGL 510
Cdd:PRK15439 154 GLMRDSRILILDEPTASL 171
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
17-297 |
7.52e-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: 44.94 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 17 AMLLGTFLASLTVLANVGLLAISGWFLASMAAAGIASVhmnyftpAGTIRFLAIVRTASRyaerlvthnatflLLSEIRV 96
Cdd:pfam00664 19 PLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFI-------LSFLQSYLLNHTGER-------------LSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 97 NMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALICFVGIIIIGVII 176
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 177 pAILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELNIYQARNQQLTKCDLLSEQYNQQLFIRHKALGnadglsLLIVQL 256
Cdd:pfam00664 159 -AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANG------LSFGIT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1949233634 257 AMLSSIVTIVPLVFSGAMVNV-ELAMLSLFVLASFESVLLLP 297
Cdd:pfam00664 232 QFIGYLSYALALWFGAYLVISgELSVGDLVAFLSLFAQLFGP 273
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
355-560 |
8.09e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPAKQKVAIVGRSGSGKTTLVNllSSLWPLQQGTINLQSD-----KEIISLHDLN------------------ 411
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEqpgnhDRIEGLEHIDkvividqspigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 412 ---------------NESRAK-----TLNILAQQHHIFD---GTLSENLAYAAPDATSQQMIAALTQAELGgwfselkqg 468
Cdd:cd03271 89 atytgvfdeirelfcEVCKGKrynreTLEVRYKGKSIADvldMTVEEALEFFENIPKIARKLQTLCDVGLG--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 469 lKTRLGTGGRNVSQGQSRRIALAQALLQK---PAILVLDEPTEGL--DNISKqavMNSVLQ--LKEHASVLTITHDPALL 541
Cdd:cd03271 160 -YIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfHDVKK---LLEVLQrlVDKGNTVVVIEHNLDVI 235
|
250 260
....*....|....*....|....*
gi 1949233634 542 SQMDSVIWL------DSGQIIAQGS 560
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGT 260
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
365-551 |
1.21e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 365 KQKVAIVGRSGSGKTTLVNLLsslwplqqgtinlqsdkeiislhdlnnesraktLNILAQQHHIFdgtlsenlAYAAPDA 444
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL---------------------------------ARELGPPGGGV--------IYIDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 445 TSQQmiaaltqaelggwfsELKQGLKTRLGTGGRNVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSV-- 522
Cdd:smart00382 41 ILEE---------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEel 105
|
170 180 190
....*....|....*....|....*....|....
gi 1949233634 523 -----LQLKEHASVLTITHDPALLSQMDSVIWLD 551
Cdd:smart00382 106 rllllLKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
342-511 |
1.54e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 342 LNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLS-----------SLWPLQQGTIN---------LQSD 401
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncQILHVEQEVVGddttalqcvLNTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 402 KEIISLhdLNNESRaktlnILAQQHHI------------FDGTLSENLAYA----------APDATSQQMIAALTQAELG 459
Cdd:PLN03073 260 IERTQL--LEEEAQ-----LVAQQRELefetetgkgkgaNKDGVDKDAVSQrleeiykrleLIDAYTAEARAASILAGLS 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 460 gwFSELKQGLKTRLGTGGRNVsqgqsrRIALAQALLQKPAILVLDEPTEGLD 511
Cdd:PLN03073 333 --FTPEMQVKATKTFSGGWRM------RIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
439-511 |
1.59e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 439 YAAPDATSQQ-MIAALTQ---AELGGWFSELKQGlKTRLGTG-------G--RNVSQGQSRRIALAQALLQKPAILVLDE 505
Cdd:PRK15064 103 YALPEMSEEDgMKVADLEvkfAEMDGYTAEARAG-ELLLGVGipeeqhyGlmSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
....*.
gi 1949233634 506 PTEGLD 511
Cdd:PRK15064 182 PTNNLD 187
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
17-164 |
1.68e-04 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 43.94 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 17 AMLLGTFLASLTVLANVGL-LAISGWFLASMAAAGIAsvhmnyfTPAGTIRFLAIVRTASRYAERLVTHNATFLLLSEIR 95
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLaRIIAGVFLEGAGLAALL-------PLLLLLLAALLLRALLAWAQERLAARAAARVKAELR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 96 VNMFATLSKLNNLDLAMSRSADLVNRLQNDVDALDKFYLNVlLPMLVALLTVPIIML-FMSAYNVNVALI 164
Cdd:cd18584 74 RRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARY-LPQLVLAAIVPLLILvAVFPLDWVSALI 142
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
354-555 |
2.51e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 354 ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQsDKEI---ISLHDLNN------ESRAKTlNILAQ 424
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLH-GKKInnhNANEAINHgfalvtEERRST-GIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 425 QHHIFDGTLSENLAYAAP-DATSQQMIAALTQaelggWFSELKQ----GLKTRLGTggrnVSQGQSRRIALAQALLQKPA 499
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKvGLLDNSRMKSDTQ-----WVIDSMRvktpGHRTQIGS----LSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949233634 500 ILVLDEPTEGLDNISKQAVMNSVLQL-KEHASVLTITHD-PALLSQMDSVIWLDSGQI 555
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEmPELLGITDRILVMSNGLV 469
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
366-548 |
2.67e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.12 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 366 QKVAIVGRSGSGKTTLVNLLSSlwplqQGTINLQSDKEIISLHDLNNESRAKTLNILAQQhhIFDGTLSENLA--YA--A 441
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAG-----KLKPNLGKFDDPPDWDEILDEFRGSELQNYFTK--LLEGDVKVIVKpqYVdlI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 442 PDATSQQMIAALTQAELGGWFSELKQGLKTRlGTGGRNVSQ---GQSRRIALAQALLQKPAILVLDEPTEGLDnISKQAV 518
Cdd:cd03236 100 PKAVKGKVGELLKKKDERGKLDELVDQLELR-HVLDRNIDQlsgGELQRVAIAAALARDADFYFFDEPSSYLD-IKQRLN 177
|
170 180 190
....*....|....*....|....*....|..
gi 1949233634 519 MNSVLQ--LKEHASVLTITHDPALLSQMDSVI 548
Cdd:cd03236 178 AARLIRelAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
481-548 |
3.37e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 3.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 481 SQGQSRRIALAQAL---LQKPAILV-LDEPTEGLDNISKQAVMNSVL-QLKEHASVLTITHDPALLSQMDSVI 548
Cdd:cd03227 79 SGGEKELSALALILalaSLKPRPLYiLDEIDRGLDPRDGQALAEAILeHLVKGAQVIVITHLPELAELADKLI 151
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
369-559 |
3.43e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 369 AIVGRSGSGKTTLVNLLSSlwPLQQGTInlqsDKEI-ISLHDLNNESRAKTLNILAQQH-HIFDGTLSENLAYAA----P 442
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGGYI----EGDIrISGFPKKQETFARISGYCEQNDiHSPQVTVRESLIYSAflrlP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 443 DATSQQ--MIAALTQAELGGwFSELKQGLKTRLGTGGrnVSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMN 520
Cdd:PLN03140 984 KEVSKEekMMFVDEVMELVE-LDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1949233634 521 SVLQLKEHA-SVLTITHDPA--LLSQMDSVIWLD-SGQIIAQG 559
Cdd:PLN03140 1061 TVRNTVDTGrTVVCTIHQPSidIFEAFDELLLMKrGGQVIYSG 1103
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
339-511 |
3.68e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.09 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 339 ALSLNNVSYH-YGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINLQSdkeiislHDLNNESRAK 417
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG-------EDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 418 tlnilAQQHHIF-------------DGTLSENLA----------------YAAPDATSQQMIAAltqaelggwFSELKQG 468
Cdd:COG3845 330 -----RRRLGVAyipedrlgrglvpDMSVAENLIlgryrrppfsrggfldRKAIRAFAEELIEE---------FDVRTPG 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1949233634 469 LKTRLGT--GGrNVsQgqsrRIALAQALLQKPAILVLDEPTEGLD 511
Cdd:COG3845 396 PDTPARSlsGG-NQ-Q----KVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
367-435 |
3.75e-04 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 41.63 E-value: 3.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949233634 367 KVAIVGRSGSGKTTLVNLLS---SLWPLQQGTINLQSDKEIISLHDLNNESRaktlNILAQQHHIFDGTLSE 435
Cdd:PRK07261 2 KIAIIGYSGSGKSTLARKLSqhyNCPVLHLDTLHFQPNWQERDDDDMIADIS----NFLLKHDWIIDGNYSW 69
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
340-511 |
4.65e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 41.76 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 340 LSLNNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINlqsdkeiISLHDLNNESRAKTL 419
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQ-------IDGKTATRGDRSRFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 420 NILAQQHHI-FDGTLSENLAY--AAPDATSQQMIA-ALTQAELGGWFSELKqglktrlgtggRNVSQGQSRRIALAQALL 495
Cdd:PRK13543 85 AYLGHLPGLkADLSTLENLHFlcGLHGRRAKQMPGsALAIVGLAGYEDTLV-----------RQLSAGQKKRLALARLWL 153
|
170
....*....|....*.
gi 1949233634 496 QKPAILVLDEPTEGLD 511
Cdd:PRK13543 154 SPAPLWLLDEPYANLD 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
343-398 |
5.70e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 5.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949233634 343 NNVSYHYGQKQALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPLQQGTINL 398
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
480-574 |
1.33e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 480 VSQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLTITHDPALLSQM-DSVIWLDSGQII 556
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWaDKINVLYCGQTV 238
|
90 100
....*....|....*....|
gi 1949233634 557 AQGSHQQLLN--EHPDYVAL 574
Cdd:PRK15093 239 ETAPSKELVTtpHHPYTQAL 258
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
21-274 |
1.64e-03 |
|
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: 40.62 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 21 GTFLASLTVLANVGLLAISGWFLASMAAAGIASVHMNYFTPAGTIRFLAIVRTASRY------AERLVTHnatflllseI 94
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYylfniaGERIVAR---------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 95 RVNMFatlSKLNNLDLAM---SRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTV--PIIMLFMSAYNVNVALICFVGI 169
Cdd:cd18557 72 RRDLF---SSLLRQEIAFfdkHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVigGLIILFILSWKLTLVLLLVIPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 170 IIIGViipAILSKQLDKNSHQETLLSAQLRAELSDTLTGLRELniyQARNQQLTKCDLLSEQYNQQLFI-RHKALGNA-- 246
Cdd:cd18557 149 LLIAS---KIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTV---RSFSAEEKEIRRYSEALDRSYRLaRKKALANAlf 222
|
250 260
....*....|....*....|....*...
gi 1949233634 247 DGLSLLIVQLAMLSSIVTIVPLVFSGAM 274
Cdd:cd18557 223 QGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
481-533 |
2.24e-03 |
|
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: 41.15 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 481 SQGQSRRIALAQALLQKPAILVLDEPTEGLDNISKQAVMNSVLQL--KEHASVLT 533
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIirEGRAVVLT 2126
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
67-166 |
2.25e-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: 40.45 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 67 FLAIVRTASRYAERLVTHNATFLLLSEIRVNMFATLsklnnLDLAMS-----RSADLVNRLQNDVDALDKFYLNVLLPML 141
Cdd:cd18544 49 GLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHI-----QRLPLSffdrtPVGRLVTRVTNDTEALNELFTSGLVTLI 123
|
90 100
....*....|....*....|....*
gi 1949233634 142 VALLTVPIIMLFMSAYNVNVALICF 166
Cdd:cd18544 124 GDLLLLIGILIAMFLLNWRLALISL 148
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
473-574 |
2.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 473 LGTGGRNVSQGQSRRIALAQALL---QKPAILVLDEPTEGLDNISKQAVMNSVLQLKEHA-SVLTITHDPALLSQMDSVI 548
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGhTVVIIEHNMHVVKVADYVL 882
|
90 100 110
....*....|....*....|....*....|...
gi 1949233634 549 WLD------SGQIIAQGSHQQLLNEH-PDYVAL 574
Cdd:PRK00635 883 ELGpeggnlGGYLLASCSPEELIHLHtPTAKAL 915
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
354-536 |
3.11e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 354 ALNNVSFELPAKQKVAIVGRSGSGKTTLVNLLSSLWPL--QQGTINLqsDKEIISLHDLnNESRAKTLNILAQQhhifdg 431
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILF--DGEVCRFKDI-RDSEALGIVIIHQE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 432 tlsenLAyaapdatsqqMIAALTQAE---LG------GWFS---------EL--KQGLKTRLGTGGRNVSQGQSRRIALA 491
Cdd:NF040905 87 -----LA----------LIPYLSIAEnifLGnerakrGVIDwnetnrrarELlaKVGLDESPDTLVTDIGVGKQQLVEIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1949233634 492 QALLQKPAILVLDEPTEGLDNISKQAVMNSVLQLKEH--ASVLtITH 536
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgiTSII-ISH 197
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
35-166 |
4.05e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis 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 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: 349990 [Multi-domain] Cd Length: 292 Bit Score: 39.39 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 35 LLAISGWFLASMAAAGIASVhmnyftpagtirflAIVRTASRYAERLvthnatfllLSEIRVNMFAtlsKLNNLDLAM-- 112
Cdd:cd18546 38 LLLAAAAYLAVVLAGWVAQR--------------AQTRLTGRTGERL---------LYDLRLRVFA---HLQRLSLDFhe 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1949233634 113 -SRSADLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALICF 166
Cdd:cd18546 92 rETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVAL 146
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
355-553 |
4.36e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 355 LNNVSFELPaKQKVAIVGRSGSGKTTLVNLLSSLwplqqgtinLQSDKEI-ISLHDLNNESRAKTLNIlaqqhHI---FD 430
Cdd:COG3593 14 IKDLSIELS-DDLTVLVGENNSGKSSILEALRLL---------LGPSSSRkFDEEDFYLGDDPDLPEI-----EIeltFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 431 GTLSENLAYAAPDATSQQMIAALT--QAELGGWFSELKQGLKTRLGTGGRNV---------------------------- 480
Cdd:COG3593 79 SLLSRLLRLLLKEEDKEELEEALEelNEELKEALKALNELLSEYLKELLDGLdlelelsldeledllkslslriedgkel 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 481 -----SQGQSRRI--ALAQALLQ-----KPAILVLDEPteglDN---ISKQAVMNSVLQ--LKEHASVLTITHDPALLSQ 543
Cdd:COG3593 159 pldrlGSGFQRLIllALLSALAElkrapANPILLIEEP----EAhlhPQAQRRLLKLLKelSEKPNQVIITTHSPHLLSE 234
|
250
....*....|..
gi 1949233634 544 M--DSVIWLDSG 553
Cdd:COG3593 235 VplENIRRLRRD 246
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
18-164 |
4.49e-03 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) 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: 349991 [Multi-domain] Cd Length: 298 Bit Score: 39.31 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 18 MLLGTFLASLTVLANVGLLAISGWFLASMAAAGIASVHMNYFTPAGTIRFLAIV---RTASRYAERLVTHNATFLLLSEI 94
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLyllSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949233634 95 RVNMFAtlsKLNNLDLAM--SRSA-DLVNRLQNDVDALDKFYLNVLLPMLVALLTVPIIMLFMSAYNVNVALI 164
Cdd:cd18547 81 RKDLFE---KLQRLPLSYfdTHSHgDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLI 150
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
483-511 |
6.33e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 6.33e-03
10 20
....*....|....*....|....*....
gi 1949233634 483 GQSRRIALAQALLQKPAILVLDEPTEGLD 511
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
478-565 |
9.22e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949233634 478 RNVSQGQSRRIALAQALLQKPAILVLDEPTEGLD-NISKQAV--MNSVLQLKEhASVLTITHDPA--LLSQMDSVIWLDS 552
Cdd:PLN03140 335 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDsSTTYQIVkcLQQIVHLTE-ATVLMSLLQPApeTFDLFDDIILLSE 413
|
90
....*....|...
gi 1949233634 553 GQIIAQGSHQQLL 565
Cdd:PLN03140 414 GQIVYQGPRDHIL 426
|
|
| |
