|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
616-1180 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 551.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 616 LRRLLREFRGPLALSLLLVAVQTCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQ 695
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 696 VLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTM 775
Cdd:COG1132 92 VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 776 PVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFV 855
Cdd:COG1132 172 PLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 856 ALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRT--PSSPAAR 933
Cdd:COG1132 252 ELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeiPDPPGAV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 934 PVGTLRGEVVFDAVHYSYRTrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVD 1013
Cdd:COG1132 332 PLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1014 GYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARA 1093
Cdd:COG1132 411 SLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARA 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1094 RLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSR 1173
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYAR 570
|
....*..
gi 1108176189 1174 LWAAHTR 1180
Cdd:COG1132 571 LYRLQFG 577
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-565 |
5.00e-172 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 520.11 E-value: 5.00e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 6 WWRLSGYVMRHRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRI 84
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGgDLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 85 AHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAV 163
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 164 LLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFG 243
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 244 PLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTLVDGT 323
Cdd:COG1132 249 PLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 324 KPLS-PEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT 402
Cdd:COG1132 329 GAVPlPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 403 LDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALA 482
Cdd:COG1132 409 LESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRY 562
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLY 568
|
...
gi 1108176189 563 REL 565
Cdd:COG1132 569 ARL 571
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
641-1176 |
2.97e-128 |
|
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: 409.99 E-value: 2.97e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 641 GLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDG 720
Cdd:COG2274 172 ALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 721 DAQIVTAVTaDVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRL 800
Cdd:COG2274 252 VGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEAS 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 801 GTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVIS 880
Cdd:COG2274 331 AKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 881 VGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRT--PSSPAARPVGTLRGEVVFDAVHYSYRTREVPA 958
Cdd:COG2274 411 LGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPerEEGRSKLSLPRLKGDIELENVSFRYPGDSPPV 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIA 1038
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENIT 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1039 YGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVV 1118
Cdd:COG2274 571 LGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1119 QRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLWA 1176
Cdd:COG2274 651 LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-567 |
8.56e-115 |
|
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: 373.79 E-value: 8.56e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 6 WWRLSGYVMRHRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAI-AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRI 84
Cdd:COG2274 144 LRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLpNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 85 AHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTtNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAV 163
Cdd:COG2274 224 GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGsLLTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 164 LLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFG 243
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 244 PLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTLVDGT 323
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGR 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 324 KPLS-PEARLSLEFQRVSFGY-VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVREL 401
Cdd:COG2274 463 SKLSlPRLKGDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 402 TLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIAL 481
Cdd:COG2274 543 DPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAI 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPR 561
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
....*.
gi 1108176189 562 YRELLS 567
Cdd:COG2274 703 YAELVQ 708
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
637-918 |
3.04e-97 |
|
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: 311.73 E-value: 3.04e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 637 QTCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAF 716
Cdd:cd18546 11 DTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 717 EDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRA 796
Cdd:cd18546 91 ERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 797 RHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRA 876
Cdd:cd18546 171 RERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAA 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1108176189 877 GVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18546 251 GTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-558 |
9.13e-97 |
|
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: 320.51 E-value: 9.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 6 WWRLSGYVMRHRRDLLLG----FGAALAGTVIAVLVplvtKRVIDDA-IAADHRPLAPWAVVLVAAAGATYLLTYVRRYY 80
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAgvamILVAATESTLAALL----KPLLDDGfGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 81 GGRIAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVL-RHVLTLLLGVAVMTWLSVPLA 159
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLvRETLTVIGLFIVLLYYSWQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 160 LLAVLLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLN 239
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 240 AHFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTL 319
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 320 VDGTKPLsPEARLSLEFQRVSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV 398
Cdd:TIGR02203 318 DTGTRAI-ERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 399 RELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATP-EQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQ 477
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADrAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 478 RIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
.
gi 1108176189 558 R 558
Cdd:TIGR02203 557 R 557
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
208-565 |
1.63e-93 |
|
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: 312.52 E-value: 1.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 208 VKAFGQEERETVKLVTASRALYAAQLR----VARLNAhfgpllqtlpalGQMAVFALG----GWMAAQ----GSITVGTF 275
Cdd:COG5265 231 VKYFGNEAREARRYDEALARYERAAVKsqtsLALLNF------------GQALIIALGltamMLMAAQgvvaGTMTVGDF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 276 VAFWACLTLLARPaCDLAGML--TIaQQARAGAVRVLELIDSRPTLVD--GTKPLSPeARLSLEFQRVSFGYVADRPVLR 351
Cdd:COG5265 299 VLVNAYLIQLYIP-LNFLGFVyrEI-RQALADMERMFDLLDQPPEVADapDAPPLVV-GGGEVRFENVSFGYDPERPILK 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 352 EISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYG 431
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 432 RPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQE 511
Cdd:COG5265 456 RPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 512 VLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:COG5265 536 ALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
638-1176 |
2.29e-93 |
|
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: 311.27 E-value: 2.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLirhgiDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:TIGR02203 32 TLAALLKPLL-----DDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRAR 797
Cdd:TIGR02203 107 RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 798 HRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAG 877
Cdd:TIGR02203 187 NSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 878 VISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGTLRGEVVFDAVHYSYRTREVP 957
Cdd:TIGR02203 267 SLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIERARGDVEFRNVTFRYPGRDRP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAI 1037
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYGRP-DATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEA 1116
Cdd:TIGR02203 427 AYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1117 VVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLWA 1176
Cdd:TIGR02203 507 LVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
334-565 |
2.74e-90 |
|
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: 290.29 E-value: 2.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLI 493
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 494 MDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
91-567 |
4.03e-89 |
|
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: 299.37 E-value: 4.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 91 DLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDV--PnVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPV 168
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVllP-LLVALLVILAAVAFLAFFSPALALVLALGLLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 169 IGLI-----AHRSRRLLAAATHCAQEHKAAVTGVVDaavcGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFG 243
Cdd:COG4987 168 AGLLlpllaARLGRRAGRRLAAARAALRARLTDLLQ----GAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 244 PLLQTLPALGQMAVFALGGWMAAQGSITVgtfvAFWACLTLLARPACDLAGMLTIA----QQARAGAVRVLELIDSRPTL 319
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPLVAAGALSG----PLLALLVLAALALFEALAPLPAAaqhlGRVRAAARRLNELLDAPPAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 320 VDGTKPLSPEARLSLEFQRVSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV 398
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSFRYPgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 399 RELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQR 478
Cdd:COG4987 400 RDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 479 IALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
....*....
gi 1108176189 559 CPRYRELLS 567
Cdd:COG4987 560 NGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
616-1169 |
5.17e-89 |
|
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: 298.98 E-value: 5.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 616 LRRLLREFRGPLALSLLLVAVQTCAGLLPPLLIRHGIDVGIRRHV-LSALWWAALAGTATVVIRWVVQWGSAMVAGYTGE 694
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGApLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 695 QVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAI--RARLVLLIf 772
Cdd:COG4988 88 RVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLdwLSGLILLV- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 773 tTMPVL----ALATWQFRRAS--NWtyrRARHRLGtvtATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRR--LGV-R 843
Cdd:COG4988 167 -TAPLIplfmILVGKGAAKASrrQW---RALARLS---GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKrtMKVlR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 844 GQRLLALYYPFVAllcSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLS 923
Cdd:COG4988 240 VAFLSSAVLEFFA---SLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 924 TRTPSSPAARPVGTLRG--EVVFDAVHYSYRTREvPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVR 1001
Cdd:COG4988 317 APEPAAPAGTAPLPAAGppSIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1002 VDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLS 1081
Cdd:COG4988 396 INGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1082 AGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAH 1161
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTH 555
|
....*...
gi 1108176189 1162 TELLAAGG 1169
Cdd:COG4988 556 EELLAKNG 563
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
20-309 |
9.77e-87 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) 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: 349987 [Multi-domain] Cd Length: 291 Bit Score: 282.83 E-value: 9.77e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIA-ADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQ 98
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAhGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 99 ALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRR 178
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 179 LLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVF 258
Cdd:cd18543 161 RYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 259 ALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18543 241 ALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
696-1176 |
1.00e-86 |
|
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: 292.83 E-value: 1.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 696 VLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIV-AFLRT--GLVVAVISVVtLVGILVALLAIRARLVLLIF 772
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnLYLRVllPLLVALLVIL-AAVAFLAFFSPALALVLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 773 TTMPVLALATWQFRRASNWTYRRARHRlGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYY 852
Cdd:COG4987 165 LLLAGLLLPLLAARLGRRAGRRLAAAR-AALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 853 PFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTP-SSPA 931
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAvTEPA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 932 ARPVGTLRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFD 1011
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1012 VDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALA 1091
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1092 RARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHY 1171
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
....*
gi 1108176189 1172 SRLWA 1176
Cdd:COG4987 564 RQLYQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
942-1175 |
2.47e-86 |
|
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: 279.50 E-value: 2.47e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGI 1021
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDIL 1101
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1102 LLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLW 1175
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
9-565 |
7.91e-86 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 290.45 E-value: 7.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 9 LSGYVMRHRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAADH-RPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHL 87
Cdd:TIGR02204 9 LWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSsGLLNRYFAFLLVVALVLALGTAARFYLVTWLGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 88 VQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALL-FDVPNVLRHVLTLLLGVAVMTW----LSVPLALLA 162
Cdd:TIGR02204 89 VVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIgSSLSMALRNALMCIGGLIMMFItspkLTSLVLLAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 163 VLLVPVIGLIAHRSRRLlaaaTHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHF 242
Cdd:TIGR02204 169 PLVLLPILLFGRRVRKL----SRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 243 GPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTLVDG 322
Cdd:TIGR02204 245 TAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 323 TKPLSPEARLS--LEFQRVSFGYVA--DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV 398
Cdd:TIGR02204 325 AHPKTLPVPLRgeIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 399 RELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQR 478
Cdd:TIGR02204 405 RQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 479 IALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
....*..
gi 1108176189 559 CPRYREL 565
Cdd:TIGR02204 565 GGLYARL 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
942-1175 |
1.86e-85 |
|
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: 277.11 E-value: 1.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTR-EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLG 1020
Cdd:cd03249 1 IEFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1021 IVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDI 1100
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1101 LLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLW 1175
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
940-1169 |
7.77e-85 |
|
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: 275.26 E-value: 7.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 940 GEVVFDAVHYSYRtREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRL 1019
Cdd:cd03254 1 GEIEFENVNFSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPD 1099
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1100 ILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGG 1169
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
334-565 |
2.91e-84 |
|
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: 273.72 E-value: 2.91e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVAD-RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLL 492
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-565 |
8.37e-81 |
|
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: 264.40 E-value: 8.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGYVA--DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:cd03249 2 EFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLL 492
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
704-1176 |
6.52e-79 |
|
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: 272.08 E-value: 6.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 704 VFAHAQRLGLDaFEDD---GdaqivtAVTADVE----AIVAFLRTGLVVAVISVVTLVGILVALLAI-RARLVLLIFTTm 775
Cdd:COG5265 117 VFRHLHALSLR-FHLErqtG------GLSRDIErgtkGIEFLLRFLLFNILPTLLEIALVAGILLVKyDWWFALITLVT- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 776 pvLALATWQFRRASNW--TYRRARHRLGTVTAT-----LREYaaglRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLL 848
Cdd:COG5265 189 --VVLYIAFTVVVTEWrtKFRREMNEADSEANTravdsLLNY----ETVKYFGNEAREARRYDEALARYERAAVKSQTSL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 849 ALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALV---TYLLYielLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTR 925
Cdd:COG5265 263 ALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVlvnAYLIQ---LYIPLNFLGFVYREIRQALADMERMFDLLDQP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 926 T--PSSPAARPVGTLRGEVVFDAVHYSYRTREvPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVD 1003
Cdd:COG5265 340 PevADAPDAPPLVVGGGEVRFENVSFGYDPER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1004 GCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAG 1083
Cdd:COG5265 419 GQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGG 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1084 QLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTE 1163
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAE 578
|
490
....*....|...
gi 1108176189 1164 LLAAGGHYSRLWA 1176
Cdd:COG5265 579 LLAQGGLYAQMWA 591
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
942-1175 |
1.01e-78 |
|
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: 258.70 E-value: 1.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGI 1021
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDIL 1101
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1102 LLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLW 1175
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-554 |
5.15e-77 |
|
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: 265.47 E-value: 5.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 8 RLSGYVMRHRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAADHRP--LAPWAVVLVAAAGATYLLTYVRRYYGGRIA 85
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLsaLLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 86 HLVQHDLRMDAFQALLRWDGRQQDRWSSG---QLIVRTTNDL---------QLVQALLfdVPnvlrhvLTLLLGVAVMTW 153
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGelaTLLTEGVEALdgyfarylpQLFLAAL--VP------LLILVAVFPLDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 154 LSvplallavllvpviGLIahrsrrLLA--------------AATHCAQEHKAAVT----GVVDAaVCGIRVVKAFGQEE 215
Cdd:COG4988 159 LS--------------GLI------LLVtapliplfmilvgkGAAKASRRQWRALArlsgHFLDR-LRGLTTLKLFGRAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 216 RETVKLVTASRALYAA---QLRVArLNAHFgpLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWacltLLA----RP 288
Cdd:COG4988 218 AEAERIAEASEDFRKRtmkVLRVA-FLSSA--VLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVL----LLApeffLP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 289 ACDLAGMLTIAQQARAGAVRVLELIDS-RPTLVDGTKPLSPEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVG 367
Cdd:COG4988 291 LRDLGSFYHARANGIAAAEKIFALLDApEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 368 APGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAA 447
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 448 HIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTR 527
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH 530
|
570 580
....*....|....*....|....*..
gi 1108176189 528 RRSMLTLADRVAVLDSGRLLDVGTPDE 554
Cdd:COG4988 531 RLALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-565 |
3.25e-76 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 263.50 E-value: 3.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 32 VIAVL--VPLVTKRVIDDAIAADH---RPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQALLRWDGR 106
Cdd:PRK10789 6 IIAMLqlIPPKVVGIIVDGVTEQHmttGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 107 QQDRWSSGQLIVRTTNDlqlVQALLFDV-PNVLRHVLTLLLGVAVM----TWLSVPLALLAVLLVPVIGLIAHRSRRLLA 181
Cdd:PRK10789 86 FYLRHRTGDLMARATND---VDRVVFAAgEGVLTLVDSLVMGCAVLivmsTQISWQLTLLALLPMPVMAIMIKRYGDQLH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 182 AATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTlpALGQMAVFALG 261
Cdd:PRK10789 163 ERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYI--AIGMANLLAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 262 G--WMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTLVDGTKPLsPEARLSLEFQRV 339
Cdd:PRK10789 241 GgsWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPV-PEGRGELDVNIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGY-VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAV 418
Cdd:PRK10789 320 QFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 419 LFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 499 SAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
335-558 |
3.62e-76 |
|
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: 250.99 E-value: 3.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVP 414
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 EDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIM 494
Cdd:cd03254 84 QDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 495 DDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
684-1174 |
9.94e-73 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 257.34 E-value: 9.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 684 GSAMVAG-------YTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGI 756
Cdd:TIGR00958 213 ASSVSAGlrggsfnYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 757 LVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDD 836
Cdd:TIGR00958 293 LGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 837 YRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAG 916
Cdd:TIGR00958 373 TLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 917 RIRSLLStRTPSSPaarPVGTL-----RGEVVFDAVHYSYRTR-EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVA 990
Cdd:TIGR00958 453 KVFEYLD-RKPNIP---LTGTLaplnlEGLIEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 991 RFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYL 1070
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1071 HQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQraTLTLAARRTTLIVAHGLAIAEHADRIVVL 1150
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ--ESRSRASRTVLLIAHRLSTVERADQILVL 686
|
490 500
....*....|....*....|....
gi 1108176189 1151 EHGTVVEDGAHTELLAAGGHYSRL 1174
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
642-1174 |
2.06e-72 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 253.02 E-value: 2.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 642 LLPPLLirhgiDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGD 721
Cdd:PRK11176 47 LLKPLL-----DDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQST 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 722 AQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALA----TWQFRRASnwtyRRAR 797
Cdd:PRK11176 122 GTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAirvvSKRFRNIS----KNMQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 798 HRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVL----LDGARE 873
Cdd:PRK11176 198 NTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLyaasFPSVMD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 874 -VRAGVISV--GALVTyllyielLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGTLRGEVVFDAVHYS 950
Cdd:PRK11176 278 tLTAGTITVvfSSMIA-------LMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERAKGDIEFRNVTFT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 951 YRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFA 1030
Cdd:PRK11176 351 YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRDAIAYGRPDA-TDAQVERAAREvgAHPM--ITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:PRK11176 431 DTIANNIAYARTEQySREQIEEAARM--AYAMdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1108 VALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRL 1174
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-566 |
9.69e-70 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 248.48 E-value: 9.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 7 WRLSGYVMRHRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDaIAADHRP--LAPWAVVLVAAAGATYLLTYVRryyGG-- 82
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDT-LGGDKGPpaLASAIFFMCLLSIASSVSAGLR---GGsf 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 83 RIAH-LVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLG-VAVMTWLSVPLAL 160
Cdd:TIGR00958 226 NYTMaRINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGlLGFMLWLSPRLTM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 161 LAVLLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNA 240
Cdd:TIGR00958 306 VTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 241 HFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTL- 319
Cdd:TIGR00958 386 GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIp 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 320 VDGT-KPLSPEARLslEFQRVSFGYVA--DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQ 396
Cdd:TIGR00958 466 LTGTlAPLNLEGLI--EFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 397 DVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQR 476
Cdd:TIGR00958 544 PLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 477 QRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEvLREAiADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVW 556
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSR-ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
570
....*....|
gi 1108176189 557 ERCPRYRELL 566
Cdd:TIGR00958 702 EDQGCYKHLV 711
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
188-566 |
1.58e-68 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 241.79 E-value: 1.58e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 188 QEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQ 267
Cdd:PRK13657 188 EEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTITMLAILVLGAALVQK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 268 GSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTLVD--GTKPLSpeaRLS--LEFQRVSFGY 343
Cdd:PRK13657 268 GQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDppGAIDLG---RVKgaVEFDDVSFSY 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 344 VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGT 423
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRS 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 424 IGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA 503
Cdd:PRK13657 425 IEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 504 VIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYRELL 566
Cdd:PRK13657 505 ETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
845-1177 |
5.75e-68 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 240.25 E-value: 5.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 845 QRLLALYYP------FVALLCSLATTL----VLLDGAREVRAGVISVGALVTYLLYIELLytpIGELAQMFDDYQRAAVA 914
Cdd:PRK13657 226 DNLLAAQMPvlswwaLASVLNRAASTItmlaILVLGAALVQKGQLRVGEVVAFVGFATLL---IGRLDQVVAFINQVFMA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 915 AGRIR---SLLSTrTPSS---PAARPVGTLRGEVVFDAVHYSYRTREvPALAGINLRIPAGQTVVFVGSTGSGKSTLIKL 988
Cdd:PRK13657 303 APKLEeffEVEDA-VPDVrdpPGAIDLGRVKGAVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 989 VARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNG 1068
Cdd:PRK13657 381 LQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDG 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1069 YLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIV 1148
Cdd:PRK13657 461 YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRIL 540
|
330 340
....*....|....*....|....*....
gi 1108176189 1149 VLEHGTVVEDGAHTELLAAGGHYSRLWAA 1177
Cdd:PRK13657 541 VFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
72-555 |
5.42e-67 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 236.57 E-value: 5.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 72 LLTYVRRYYGGRIAHLVQHDLRMDAFQALLRwDGRQQDRWSSGQLIvrttNDLQLVQALL--------FDVPNVLRHVLT 143
Cdd:COG4618 75 LLDAVRSRILVRVGARLDRRLGPRVFDAAFR-AALRGGGGAAAQAL----RDLDTLRQFLtgpglfalFDLPWAPIFLAV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 144 L-----------LLGVAVMTWLsvplallavllvpviGLIAHR-SRRLLAAAthcaQEHKAAVTGVVDAAVCGIRVVKAF 211
Cdd:COG4618 150 LflfhpllgllaLVGALVLVAL---------------ALLNERlTRKPLKEA----NEAAIRANAFAEAALRNAEVIEAM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 212 GQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAfwaCLTLLAR---P 288
Cdd:COG4618 211 GMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIA---ASILMGRalaP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 289 ACDLAGMLTIAQQARAGAVRVLELIDSRPTLVDGTKPLSPEARLSLEfqRVSFGY-VADRPVLREISLSVRAGETLAVVG 367
Cdd:COG4618 288 IEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRPKGRLSVE--NLTVVPpGSKRPILRGVSFSLEPGEVLGVIG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 368 APGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAygR-PDATPEQIATAARA 446
Cdd:COG4618 366 PSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA--RfGDADPEKVVAAAKL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 447 AHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIEcgiqEVLREAIAD-----RT 521
Cdd:COG4618 444 AGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE----AALAAAIRAlkargAT 519
|
490 500 510
....*....|....*....|....*....|....
gi 1108176189 522 AVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:COG4618 520 VVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
109-565 |
1.84e-66 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 235.68 E-value: 1.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 109 DRWSSGQLIVRTTNDLQLV-----QALLfdvpNVLRHVLTLLLGVAVMTW----LSVPLALLAVLLVPVIGLIAHRSRRL 179
Cdd:PRK11176 117 DKQSTGTLLSRITYDSEQVassssGALI----TVVREGASIIGLFIMMFYyswqLSLILIVIAPIVSIAIRVVSKRFRNI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 180 laaaTHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFA 259
Cdd:PRK11176 193 ----SKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 260 LGGWMAAQGSITVGTF-VAFWACLTLLaRPACDLAGMLTIAQQARAGAVRVLELIDSRPTLVDGTKPLSPeARLSLEFQR 338
Cdd:PRK11176 269 AASFPSVMDTLTAGTItVVFSSMIALM-RPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIER-AKGDIEFRN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 339 VSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDA 417
Cdd:PRK11176 347 VTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNV 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 418 VLFSGTIGANIAYGRPDA-TPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDD 496
Cdd:PRK11176 427 HLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 497 PTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-546 |
5.31e-66 |
|
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: 222.08 E-value: 5.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYVAD-RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:cd03245 2 RIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRL 491
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 492 LIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
653-1150 |
1.35e-65 |
|
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: 231.79 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 653 DVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADV 732
Cdd:TIGR02857 32 GLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 733 EAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAA 812
Cdd:TIGR02857 112 EALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 813 GLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLD-GAREVRAGVISVGALVTYLLYI 891
Cdd:TIGR02857 192 GLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVYiGFRLLAGDLDLATGLFVLLLAP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 892 ELlYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGTLR-GEVVFDAVHYSYRTREvPALAGINLRIPAGQ 970
Cdd:TIGR02857 272 EF-YLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPaSSLEFSGVSVAYPGRR-PALRPVSFTVPPGE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 971 TVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVE 1050
Cdd:TIGR02857 350 RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIR 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1051 RAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRT 1130
Cdd:TIGR02857 430 EALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRT 509
|
490 500
....*....|....*....|
gi 1108176189 1131 TLIVAHGLAIAEHADRIVVL 1150
Cdd:TIGR02857 510 VLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
638-918 |
4.25e-65 |
|
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: 222.43 E-value: 4.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:cd07346 12 TALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRAR 797
Cdd:cd07346 92 RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 798 HRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAG 877
Cdd:cd07346 172 ESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1108176189 878 VISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd07346 252 SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
616-1171 |
3.62e-64 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 229.60 E-value: 3.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 616 LRRLL---REFRGPLALSLLLVAVQTCAGLLPPLLIRHGIDVGIRRHVLSalwWAALAGTATV-----VIRWVVQWGSAM 687
Cdd:PRK10790 11 LKRLLaygSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLP---LGLVAGLAAAyvglqLLAAGLHYAQSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 688 VAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEaIVAFLRTGLVVAVISVVTLVG-ILVALLAIRAR 766
Cdd:PRK10790 88 LFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTE-VIRDLYVTVVATVLRSAALIGaMLVAMFSLDWR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 767 LVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYR-----GLQS---YFAHSDDYR 838
Cdd:PRK10790 167 MALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARfgermGEASrshYMARMQTLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 839 RLGVRGQRLLALYYPFValLCSLattlVLLDGAREVraGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:PRK10790 247 LDGFLLRPLLSLFSALI--LCGL----LMLFGFSAS--GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 919 RSLL-STRTPSSPAARPVGTlrGEVVFDAVHYSYRTREvPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTH 997
Cdd:PRK10790 319 FELMdGPRQQYGNDDRPLQS--GRIDIDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 998 GTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRpDATDAQVERAAREVGAHPMITALDNGYLHQVTAGG 1077
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1078 RNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRAtLTLAARRTTLIV-AHGLAIAEHADRIVVLEHGTVV 1156
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA-LAAVREHTTLVViAHRLSTIVEADTILVLHRGQAV 553
|
570
....*....|....*
gi 1108176189 1157 EDGAHTELLAAGGHY 1171
Cdd:PRK10790 554 EQGTHQQLLAAQGRY 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
942-1153 |
8.18e-64 |
|
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: 213.78 E-value: 8.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGI 1021
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAGTVRDAIaygrpdatdaqveraarevgahpmitaldngylhqvtaggrnLSAGQLQLLALARARLVDPDIL 1101
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1102 LLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHG 1153
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
334-545 |
1.28e-63 |
|
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: 213.40 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGY-VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSGTIGANIaygrpdatpeqiataaraahieefvntlpdgyqtavgargltLSGGQRQRIALARALLHQPRLL 492
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGR 545
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
942-1176 |
2.71e-62 |
|
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: 212.35 E-value: 2.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGI 1021
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDIL 1101
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1102 LLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLWA 1176
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
78-1166 |
1.12e-61 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 231.79 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 78 RYYG--GRIAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQ---LIVRTTNDLQLVQALL---FDVPNVLRHVLTLL---L 146
Cdd:PLN03232 360 QYFQnvGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKvtnMITTDANALQQIAEQLhglWSAPFRIIVSMVLLyqqL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 147 GVAvmtwlSVPLALLAVLLVPVIGLIAHRSRRLLAAATHCAQEHkaavTGVVDAAVCGIRVVKAFGQEERETVKlVTASR 226
Cdd:PLN03232 440 GVA-----SLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKR----VGIINEILASMDTVKCYAWEKSFESR-IQGIR 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 227 ALYAAQLRVARLNAHFGP-LLQTLPALgqMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAG 305
Cdd:PLN03232 510 NEELSWFRKAQLLSAFNSfILNSIPVV--VTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVS 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 306 AVRVLELIDSRPTLVDGTKPLSPEA-RLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASlatrcy 384
Cdd:PLN03232 588 LQRIEELLLSEERILAQNPPLQPGApAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS------ 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 385 dvtqgaVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRpDATPEQIATAARAAHIEEFVNTLPDGYQTAV 464
Cdd:PLN03232 662 ------AMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEI 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 465 GARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA-VIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDS 543
Cdd:PLN03232 735 GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSE 814
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 544 GRLLDVGTPDEVWERCPRYRELLSPAPDLADDLVVAERSpvcRPVAGLGTKAAqhTNVHNPGPHDHPPGPDPLRRLLREF 623
Cdd:PLN03232 815 GMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTND---ENILKLGPTVT--IDVSERNLGSTKQGKRGRSVLVKQE 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 624 ---RGPLALSLLLVAVQTCAGL--LPPLLIRHGIDVGIRrhVLSALWWAALAGTAT---------VVIRWVVQWGSAMVA 689
Cdd:PLN03232 890 ereTGIISWNVLMRYNKAVGGLwvVMILLVCYLTTEVLR--VSSSTWLSIWTDQSTpksyspgfyIVVYALLGFGQVAVT 967
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 690 gYTGEQVLF--------RLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAI---VAFLRT---GLVVAVISVVTLVG 755
Cdd:PLN03232 968 -FTNSFWLIssslhaakRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIdrnVANLMNmfmNQLWQLLSTFALIG 1046
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 756 IL--VALLAIrarlvllifttMPVLAL--ATWQFRRAsnwTYRRARhRLGTVT-----ATLREYAAGLRIAQAFRAEYR- 825
Cdd:PLN03232 1047 TVstISLWAI-----------MPLLILfyAAYLYYQS---TSREVR-RLDSVTrspiyAQFGEALNGLSSIRAYKAYDRm 1111
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 826 ----------GLQSYFAHSDDYRRLGVRGQRLLALyypfvaLLCSLATTLVLLDGAREVRAGVISV-GALVTYLLYIELL 894
Cdd:PLN03232 1112 akingksmdnNIRFTLANTSSNRWLTIRLETLGGV------MIWLTATFAVLRNGNAENQAGFASTmGLLLSYTLNITTL 1185
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 895 YTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGT--LRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTV 972
Cdd:PLN03232 1186 LSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGwpSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKV 1265
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 973 VFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIaygRP--DATDAQVE 1050
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPfsEHNDADLW 1342
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1051 RAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRT 1130
Cdd:PLN03232 1343 EALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCT 1422
|
1130 1140 1150
....*....|....*....|....*....|....*.
gi 1108176189 1131 TLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PLN03232 1423 MLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
334-565 |
6.56e-61 |
|
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: 208.49 E-value: 6.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLL 492
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
638-918 |
8.27e-61 |
|
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: 210.32 E-value: 8.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGI--RRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDA 715
Cdd:cd18544 12 TALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 716 FeddgDAQ----IVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNW 791
Cdd:cd18544 92 F----DRTpvgrLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 792 TYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGA 871
Cdd:cd18544 168 AYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1108176189 872 REVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18544 248 GQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
940-1159 |
1.13e-60 |
|
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: 207.06 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 940 GEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRL 1019
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPD 1099
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1100 ILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
642-1177 |
1.40e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 218.43 E-value: 1.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 642 LLPPLLIrhGIDV-GIRRHVLSA----LWWAALAGTATVV--IRWVvqWGSAMV-AGYtgeQVLFRLRSVVFAHAQRLGL 713
Cdd:PRK10789 12 LIPPKVV--GIIVdGVTEQHMTTgqilMWIGTMVLIAVVVylLRYV--WRVLLFgASY---QLAVELREDFYRQLSRQHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 714 DAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVAL-LAIRARLVLLIFTTMPVLALATWQFRRASNWT 792
Cdd:PRK10789 85 EFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYGDQLHER 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 793 YRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAR 872
Cdd:PRK10789 165 FKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 873 EVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGTLRGEVVFDAVHYSYR 952
Cdd:PRK10789 245 MVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQFTYP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 953 TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGT 1032
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1033 VRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDP 1112
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1113 ATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGG------HYSRLWAA 1177
Cdd:PRK10789 485 RTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGwyrdmyRYQQLEAA 555
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
198-555 |
2.87e-60 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 216.83 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 198 VDAAVCGIRVVKAFGQEeRETVKLVTASRALYAAQLRVAR-LNAHFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFV 276
Cdd:TIGR01842 183 ADSALRNAEVIEAMGMM-GNLTKRWGRFHSKYLSAQSAASdRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 277 AfwaCLTLLARPACDLAGMLTIAQQ---ARAGAVRVLELIDSRPTLVDGTKPLSPEARLSLEfqRVSFGY-VADRPVLRE 352
Cdd:TIGR01842 262 A---GSILVGRALAPIDGAIGGWKQfsgARQAYKRLNELLANYPSRDPAMPLPEPEGHLSVE--NVTIVPpGGKKPTLRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGR 432
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 433 PDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEV 512
Cdd:TIGR01842 417 ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1108176189 513 LREAIADR-TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:TIGR01842 497 IKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-562 |
5.97e-60 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 217.28 E-value: 5.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 8 RLSGYVMRHRRDLLLG----FGAALAgtviAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATYL---LTYVRRYY 80
Cdd:PRK10790 13 RLLAYGSPWRKPLGLAvlmlWVAAAA----EVSGPLLISYFIDNMVAKGNLPLGLVAGLAAAYVGLQLLaagLHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 81 GGRIAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDV-PNVLRH---VLTLLLGVAVMTWLSV 156
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVvATVLRSaalIGAMLVAMFSLDWRMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 157 PLALLAVLLVPVIGLIAHR-----SRRLLAaathcaqeHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAA 231
Cdd:PRK10790 169 LVAIMIFPAVLVVMVIYQRystpiVRRVRA--------YLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 232 QLRVARLNAHF-GPLLQTLPAL---GQMAVFALGGwmaaQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAV 307
Cdd:PRK10790 241 RMQTLRLDGFLlRPLLSLFSALilcGLLMLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 308 RVLELIDS-RPTLVDGTKPLSPEarlSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDV 386
Cdd:PRK10790 317 RVFELMDGpRQQYGNDDRPLQSG---RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 387 TQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRpDATPEQIATAARAAHIEEFVNTLPDGYQTAVGA 466
Cdd:PRK10790 394 TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 467 RGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
570
....*....|....*.
gi 1108176189 547 LDVGTPDEVWERCPRY 562
Cdd:PRK10790 553 VEQGTHQQLLAAQGRY 568
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
13-565 |
8.65e-59 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 216.15 E-value: 8.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 13 VMRHRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAadHR---PLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQ 89
Cdd:TIGR01846 134 IIRYRKQFREVLLISLALQLFALVTPLLFQVVIDKVLV--HRglsTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRID 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 90 HDLRMDAFQALLR-----WDGRQqdrwsSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVL 164
Cdd:TIGR01846 212 VELGARLYRHLLGlplgyFESRR-----VGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 165 LVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLnahfGP 244
Cdd:TIGR01846 287 SLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNL----GN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 245 LLQTLPALGQMAVFALGGWMAAQ----GSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTLV 320
Cdd:TIGR01846 363 IAGQAIELIQKLTFAILLWFGAHlvigGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPR 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 321 DGTKPLSPEARLSLEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVR 399
Cdd:TIGR01846 443 SAGLAALPELRGAITFENIRFRYAPDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 400 ELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRI 479
Cdd:TIGR01846 523 IADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRI 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERC 559
Cdd:TIGR01846 603 AIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
....*.
gi 1108176189 560 PRYREL 565
Cdd:TIGR01846 683 GLYARL 688
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
20-309 |
1.99e-58 |
|
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: 203.17 E-value: 1.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQ 98
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAgDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 99 ALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSR 177
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 178 RLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAV 257
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 258 FALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
940-1160 |
7.95e-55 |
|
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: 190.40 E-value: 7.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 940 GEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRL 1019
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEQYVFAGTVRDAIA-YGRpdATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDP 1098
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGA 1160
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
638-918 |
1.11e-54 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV 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: 349989 [Multi-domain] Cd Length: 293 Bit Score: 192.68 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:cd18545 13 TAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRAR 797
Cdd:cd18545 93 SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 798 HRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAG 877
Cdd:cd18545 173 KKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1108176189 878 VISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18545 253 AITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
324-1169 |
1.93e-54 |
|
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: 208.65 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 324 KPLSPEARLSLEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGqdvrelt 402
Cdd:TIGR00957 627 RTIKPGEGNSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 403 ldslrsAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEfVNTLPDGYQTAVGARGLTLSGGQRQRIALA 482
Cdd:TIGR00957 700 ------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVL---REAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERC 559
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRD 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 560 PRYRELLSPAPDLADDLVVAERSpvcrpVAGLGTKAAQHTNVHNPGPHDHPPGPDPLRRL---------LREFRGPLALS 630
Cdd:TIGR00957 853 GAFAEFLRTYAPDEQQGHLEDSW-----TALVSGEGKEAKLIENGMLVTDVVGKQLQRQLsasssdsgdQSRHHGSSAEL 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 631 LLLVAVQTCAGLLPPLLIRHGI-----------DVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFR 699
Cdd:TIGR00957 928 QKAEAKEETWKLMEADKAQTGQvelsvywdymkAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLR 1007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 700 LR----------SVVFAHA-----------QRLGLDA-----------FEDDGDAQIVTAVTADVEAIVAFLRTGLVVAV 747
Cdd:TIGR00957 1008 LSvygalgilqgFAVFGYSmavsiggiqasRVLHQDLlhnklrspmsfFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 748 ISVVTLVGILVALLAiRARLVLLIFTTMPVLALATWQFRRASNwtyrRARHRLGTVTAT-----LREYAAGLRIAQAFRA 822
Cdd:TIGR00957 1088 GSLFNVIGALIVILL-ATPIAAVIIPPLGLLYFFVQRFYVASS----RQLKRLESVSRSpvyshFNETLLGVSVIRAFEE 1162
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 823 EYRglqsyFAHSDDYR--------RLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVisVGALVTYLLYIEll 894
Cdd:TIGR00957 1163 QER-----FIHQSDLKvdenqkayYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGL--VGLSVSYSLQVT-- 1233
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 895 yTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSS---PAARPVGTL--RGEVVFDavHYSYRTREVP--ALAGINLRIP 967
Cdd:TIGR00957 1234 -FYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiQETAPPSGWppRGRVEFR--NYCLRYREDLdlVLRHINVTIH 1310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 968 AGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAI-AYGRpdATD 1046
Cdd:TIGR00957 1311 GGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSD 1388
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1047 AQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLA 1126
Cdd:TIGR00957 1389 EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF 1468
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1108176189 1127 ARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGG 1169
Cdd:TIGR00957 1469 EDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
204-541 |
3.78e-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: 198.28 E-value: 3.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 204 GIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGqMAVFA-------LGGWMAAQGSITVgtfv 276
Cdd:TIGR02857 192 GLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLS-VALVAvyigfrlLAGDLDLATGLFV---- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 277 afwacltLLARPAC-----DLAGMLTIAQQARAGAVRVLELIDSRPTLVDGTKPLSPEARLSLEFQRVSFGYVADRPVLR 351
Cdd:TIGR02857 267 -------LLLAPEFylplrQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 352 EISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYG 431
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 432 RPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQE 511
Cdd:TIGR02857 420 RPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
330 340 350
....*....|....*....|....*....|
gi 1108176189 512 VLREAIADRTAVIFTRRRSMLTLADRVAVL 541
Cdd:TIGR02857 500 ALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
113-567 |
6.83e-54 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 201.71 E-value: 6.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 113 SGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRRLLAAATHCAQEHKA 192
Cdd:TIGR03796 250 AGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 193 AVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQGSITV 272
Cdd:TIGR03796 330 KLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTI 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 273 GTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV-------LELIDSRPTLVDGTKPlsPEARLS--LEFQRVSFGY 343
Cdd:TIGR03796 410 GMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLddvlrnpVDPLLEEPEGSAATSE--PPRRLSgyVELRNITFGY 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 344 VA-DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSG 422
Cdd:TIGR03796 488 SPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEG 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:TIGR03796 568 TVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 503 AVIECGIQEVLREaiadR--TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYRELLS 567
Cdd:TIGR03796 648 PETEKIIDDNLRR----RgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
334-546 |
3.20e-53 |
|
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: 185.75 E-value: 3.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYV--ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:cd03248 12 VKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRL 491
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 492 LIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-552 |
5.54e-53 |
|
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: 185.00 E-value: 5.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYVAD-RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:cd03244 2 DIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSGTIGANIA-YGRpdATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPR 490
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 491 LLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTP 552
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
75-528 |
3.66e-52 |
|
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: 192.58 E-value: 3.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 75 YVRRYYGGRIAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVpnVLRHVLTLLLG---VAVM 151
Cdd:TIGR02868 71 YLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRV--IVPAGVALVVGaaaVAAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 152 TWLSVPLALLAVLLVPVIGLIAHRSRRLLAAATHCAQEH-KAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYA 230
Cdd:TIGR02868 149 AVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARlRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 231 AQLRVARLNAhfgpLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIA----QQARAGA 306
Cdd:TIGR02868 229 AERRAAAATA----LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAaqqlTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 307 VRVLELIDSRPTLVDGTKPL---SPEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRC 383
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPAagaVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 384 YDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTA 463
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 464 VGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRR 528
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
211-565 |
5.48e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 190.04 E-value: 5.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 211 FGQEERETVKLVTASRALYAAQLRVARLNAhFGPLLQTLpALGQMAVFALggWMAAQGsitVGTFV---AFWACLTLLAR 287
Cdd:PRK11160 216 FGAEDRYRQQLEQTEQQWLAAQRRQANLTG-LSQALMIL-ANGLTVVLML--WLAAGG---VGGNAqpgALIALFVFAAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 288 PACDLAGMLTIA----QQARAGAVRVLELIDSRPTLVDGTKPLSPEARLSLEFQRVSFGYV-ADRPVLREISLSVRAGET 362
Cdd:PRK11160 289 AAFEALMPVAGAfqhlGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPdQPQPVLKGLSLQIKAGEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 363 LAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIAT 442
Cdd:PRK11160 369 VALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 443 AARAAHIEEFVNTlPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTA 522
Cdd:PRK11160 449 VLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV 527
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1108176189 523 VIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:PRK11160 528 LMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
349-1164 |
6.97e-51 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 197.31 E-value: 6.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRiggqdvreltldSLRSaIGLVPEDAVLFSGTIGANI 428
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------------AERS-IAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 429 AYGRPDaTPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA-VIEC 507
Cdd:PTZ00243 742 LFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGER 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 508 GIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTpDEVWERCPRYREL---LSPAPDLADDLVVAERSPV 584
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS-SADFMRTSLYATLaaeLKENKDSKEGDADAEVAEV 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 585 ---CRPVAGLGTKAAQHTNVhNPGPHDHPPGPDPLRRLLREFR--GPLALSLLLVAVQTCAGLLPPLLIRHGIDVGIRRH 659
Cdd:PTZ00243 900 daaPGGAVDHEPPVAKQEGN-AEGGDGAALDAAAGRLMTREEKasGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVT 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 660 VLSALW---WAA------------------LAGTATVVIRWVVQWGSAMVAGYTGEQVLfrLRSVVFAHaqrlgLDAFED 718
Cdd:PTZ00243 979 VSSGVWlsmWSTrsfklsaatylyvylgivLLGTFSVPLRFFLSYEAMRRGSRNMHRDL--LRSVSRGT-----MSFFDT 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 719 DGDAQIVTAVTADVEAivafLRTGLVVAVISVVT-LVGILVALLAIRARLVLLIFTTMPV--LALATWQFRRASNWTYRR 795
Cdd:PTZ00243 1052 TPLGRILNRFSRDIDI----LDNTLPMSYLYLLQcLFSICSSILVTSASQPFVLVALVPCgyLYYRLMQFYNSANREIRR 1127
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 796 ARHRLGT-VTATLREYAAGLRIAQAFRAEYRGLQSYFA-----HSDDY------RRLGVRGQRLLALYYPFVAL------ 857
Cdd:PTZ00243 1128 IKSVAKSpVFTLLEEALQGSATITAYGKAHLVMQEALRrldvvYSCSYlenvanRWLGVRVEFLSNIVVTVIALigvigt 1207
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 858 ----------LCSLATTLV---------LLDGAREVRAGVISVGALVTYLLYIELLYTPigELAQMFDDYQRAAVAAGRI 918
Cdd:PTZ00243 1208 mlratsqeigLVSLSLTMAmqttatlnwLVRQVATVEADMNSVERLLYYTDEVPHEDMP--ELDEEVDALERRTGMAADV 1285
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 919 RSLLSTRTPSSPAARPVGTLRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHG 998
Cdd:PTZ00243 1286 TGTVVIEPASPTSAAPHPVQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGG 1365
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 999 TVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIaygRP--DATDAQVERAAREVGAHPMITALDNGYLHQVTAG 1076
Cdd:PTZ00243 1366 EIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEG 1442
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1077 GRNLSAGQLQLLALARARLV-DPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTV 1155
Cdd:PTZ00243 1443 GSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
....*....
gi 1108176189 1156 VEDGAHTEL 1164
Cdd:PTZ00243 1523 AEMGSPREL 1531
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
937-1155 |
4.47e-50 |
|
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: 176.89 E-value: 4.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 937 TLRGEVVFDAVHYSYRTR-EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGY 1015
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1016 RNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARL 1095
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1096 VDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTV 1155
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
311-1167 |
7.96e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 193.71 E-value: 7.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 311 ELIDSRPTLVDGTKPLSPEARLSLEFQRVSFGYVA--DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQ 388
Cdd:PTZ00265 360 EIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 389 GAVRIG-GQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYG--------------RPDATPEQ-------------- 439
Cdd:PTZ00265 440 GDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGNDSQenknkrnscrakca 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 440 -----------------------------IATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPR 490
Cdd:PTZ00265 520 gdlndmsnttdsneliemrknyqtikdseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 491 LLIMDDPTSAVDAVIECGIQEVLR--EAIADRTAVIFTRRRSMLTLADRVAVL---DSGRLLDV---------------- 549
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLsnrERGSTVDVdiigedptkdnkennn 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 550 ----------------------------GTPDEVWE-RCPRYRELLSPA------------------------------- 569
Cdd:PTZ00265 680 knnkddnnnnnnnnnnkinnagsyiieqGTHDALMKnKNGIYYTMINNQkvsskkssnndndkdsdmkssaykdsergyd 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 570 PDLADDLVVAERSPVcrpvaglGTKAAQHTNVHNPGPHDHPPGPDPLRRLLRE---------------FRGPLALSLLLV 634
Cdd:PTZ00265 760 PDEMNGNSKHENESA-------SNKKSCKMSDENASENNAGGKLPFLRNLFKRkpkapnnlrivyreiFSYKKDVTIIAL 832
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 635 AVQTCAGLLPPLLIRHGidvgirRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYT---------GEQVLFRLRSVVF 705
Cdd:PTZ00265 833 SILVAGGLYPVFALLYA------KYVSTLFDFANLEANSNKYSLYILVIAIAMFISETlknyynnviGEKVEKTMKRRLF 906
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 706 AHAQRLGLDAFEDDGDAQIVtaVTADVEAIVAFLRTGLVVAVIS-----VVTLVGILVALL---AIRARLVLLIFTTMPV 777
Cdd:PTZ00265 907 ENILYQEISFFDQDKHAPGL--LSAHINRDVHLLKTGLVNNIVIfthfiVLFLVSMVMSFYfcpIVAAVLTGTYFIFMRV 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 778 LALatwQFRRASNWTYRRAR-HRLGTVTATLRE----YAAGLRIAQAFRAEYR----GLQSYFAH----SDDYRRLGVRG 844
Cdd:PTZ00265 985 FAI---RARLTANKDVEKKEiNQPGTVFAYNSDdeifKDPSFLIQEAFYNMNTviiyGLEDYFCNliekAIDYSNKGQKR 1061
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 845 QRLL-ALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI----- 918
Cdd:PTZ00265 1062 KTLVnSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYyplii 1141
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 919 -RSLLSTRTPSSPAARPVGTLRGEVVFDAVHYSYRTR-EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYD-- 994
Cdd:PTZ00265 1142 rKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlk 1221
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 995 ----------------------------------------------------PTHGTVRVDGCDLREFDVDGYRNRLGIV 1022
Cdd:PTZ00265 1222 ndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIV 1301
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 TQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILL 1102
Cdd:PTZ00265 1302 SQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILL 1381
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1103 LDEATVALDPATEAVVQRATLTL--AARRTTLIVAHGLAIAEHADRIVVLEH----GTVVE-DGAHTELLAA 1167
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSV 1453
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
939-1175 |
4.30e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 184.64 E-value: 4.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 939 RGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNR 1018
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITAlDNGYLHQVTAGGRNLSAGQLQLLALARARLVDP 1098
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLW 1175
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
638-918 |
7.04e-49 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 175.80 E-value: 7.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGID-VGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAF 716
Cdd:cd18778 12 TLLGLVPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 717 EDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRA 796
Cdd:cd18778 92 DDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 797 RHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRA 876
Cdd:cd18778 172 REALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1108176189 877 GVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18778 252 GELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
696-1138 |
7.42e-49 |
|
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: 182.95 E-value: 7.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 696 VLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVA-FLRT------GLVVAVISVVTLVGILVALLAIRARLV 768
Cdd:TIGR02868 84 SLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlYVRVivpagvALVVGAAAVAAIAVLSVPAALILAAGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 769 LLIFTTMPVLALATwqfRRASNWTYRRARHRLGTVTATLREYAAGLRIA---QAFRAEYRglqsyfAHSDDYRRLGVRGQ 845
Cdd:TIGR02868 164 LLAGFVAPLVSLRA---ARAAEQALARLRGELAAQLTDALDGAAELVASgalPAALAQVE------EADRELTRAERRAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 846 RLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTR 925
Cdd:TIGR02868 235 AATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 926 ----TPSSPAARPVGTLRGEVVFDAVHYSYRTREvPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVR 1001
Cdd:TIGR02868 315 gpvaEGSAPAAGAVGLGKPTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1002 VDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLS 1081
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1082 AGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGL 1138
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-558 |
8.41e-49 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 185.93 E-value: 8.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 6 WWRLSGYVMR-HRRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIA-ADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGR 83
Cdd:TIGR03797 123 LRDLLRFALRgARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPdADRSLLVQIALALLAAAVGAAAFQLAQSLAVLR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 84 IAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAV 163
Cdd:TIGR03797 203 LETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 164 LLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEER---ETVKLVTASRALYAAQLRVARLNA 240
Cdd:TIGR03797 283 ALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRafaRWAKLFSRQRKLELSAQRIENLLT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 241 HFGpllQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRVLELIDSRPTlV 320
Cdd:TIGR03797 363 VFN---AVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPE-V 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 321 DGTKPLSPEARLSLEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVR 399
Cdd:TIGR03797 439 DEAKTDPGKLSGAIEVDRVTFRYRPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 400 ELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPdATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRI 479
Cdd:TIGR03797 519 GLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDAViecgIQEVLREAIA--DRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDNR----TQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
.
gi 1108176189 558 R 558
Cdd:TIGR03797 674 R 674
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-1169 |
9.93e-49 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 190.33 E-value: 9.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 345 ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLAtrcydvtqgavrIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTI 424
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM------------LGELPPRSDASVVIRGTVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANIAYGRPdATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAV 504
Cdd:PLN03130 696 RDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 505 IEcgiQEV----LREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYRELLSPAPDLAD------ 574
Cdd:PLN03130 775 VG---RQVfdkcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEyveeng 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 575 --DLVVAERSPVCRPVAGLGTKAAQHTNvhnpgpHDHPPGPDPLRRLLREfrgplalslllvavqtcAGLLP-PLLIRHg 651
Cdd:PLN03130 852 eeEDDQTSSKPVANGNANNLKKDSSSKK------KSKEGKSVLIKQEERE-----------------TGVVSwKVLERY- 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 652 idvgirRHVLSALWWAA---LAGTATVVIR-----WVVQWGSA-------------MVAGYTGEQVLFRL---------- 700
Cdd:PLN03130 908 ------KNALGGAWVVMilfLCYVLTEVFRvssstWLSEWTDQgtpkthgplfynlIYALLSFGQVLVTLlnsywlimss 981
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 701 ------------RSV-----VFAHAQRLG--LDAFEDD-GDAQIVTAVTADVeaivaFLrtGLVVAVISVVTLVGIL--V 758
Cdd:PLN03130 982 lyaakrlhdamlGSIlrapmSFFHTNPLGriINRFAKDlGDIDRNVAVFVNM-----FL--GQIFQLLSTFVLIGIVstI 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 759 ALLAIrarlvllifttMPVLALatwqFRRASNWTYRRARH--RLGTVT-----ATLREYAAGLRIAQAFRAeYRGLQSYF 831
Cdd:PLN03130 1055 SLWAI-----------MPLLVL----FYGAYLYYQSTAREvkRLDSITrspvyAQFGEALNGLSTIRAYKA-YDRMAEIN 1118
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 832 AHSDD----YRRLGVRGQRLLALYYPFV-ALLCSLATTLVLLDGAR-EVRAGVIS-VGALVTYLLYIELLYTPIGELAQM 904
Cdd:PLN03130 1119 GRSMDnnirFTLVNMSSNRWLAIRLETLgGLMIWLTASFAVMQNGRaENQAAFAStMGLLLSYALNITSLLTAVLRLASL 1198
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 905 FDDYQRAAVAAGRIRSLLSTRTPSSPAARPVG--TLRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGK 982
Cdd:PLN03130 1199 AENSLNAVERVGTYIDLPSEAPLVIENNRPPPgwPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGK 1278
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 983 STLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVR---DAIAygrpDATDAQVERAAREVGAH 1059
Cdd:PLN03130 1279 SSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRfnlDPFN----EHNDADLWESLERAHLK 1354
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1060 PMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLA 1139
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLN 1434
|
890 900 910
....*....|....*....|....*....|
gi 1108176189 1140 IAEHADRIVVLEHGTVVEDGAHTELLAAGG 1169
Cdd:PLN03130 1435 TIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
942-1166 |
4.83e-48 |
|
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: 170.98 E-value: 4.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRtREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGI 1021
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQ--EQYVFAGTVRDAIAYG------RPDATDAQVERAAREVGAHpmitaldnGYLHQVTAggrNLSAGQLQLLALARA 1093
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLE--------HLADRPPH---ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1094 RLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVA-HGLA-IAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDlVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
638-918 |
7.74e-48 |
|
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: 172.62 E-value: 7.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLdAFE 717
Cdd:cd18542 12 TALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSF-SFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DD---GDaqIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYR 794
Cdd:cd18542 91 DKartGD--LMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 795 RARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREV 874
Cdd:cd18542 169 EIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1108176189 875 RAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18542 249 INGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
908-1167 |
1.10e-47 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 179.94 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 908 YQRAAVAAGRIRSLLSTRtPSSPAARPVGTLRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIK 987
Cdd:COG4618 298 FVSARQAYRRLNELLAAV-PAEPERMPLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 988 LVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAygR-PDATDAQVERAAREVGAHPMITALD 1066
Cdd:COG4618 377 LLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA--RfGDADPEKVVAAAKLAGVHEMILRLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1067 NGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTT-LIVAHGLAIAEHAD 1145
Cdd:COG4618 455 DGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAVD 534
|
250 260
....*....|....*....|..
gi 1108176189 1146 RIVVLEHGTVVEDGAHTELLAA 1167
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVLAR 556
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
202-565 |
1.44e-46 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 179.55 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 202 VCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAhfgpLLQTLPALGQMAVFALGGWMAAQ----GSITVGTFVA 277
Cdd:TIGR01193 341 LNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQ----GQQAIKAVTKLILNVVILWTGAYlvmrGKLTLGQLIT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 278 FWACLTLLARPACDLAGMLTIAQQARAGAVRVLE--LIDSRptLVDGTKPLSPEARL-SLEFQRVSFGYVADRPVLREIS 354
Cdd:TIGR01193 417 FNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSE--FINKKKRTELNNLNgDIVINDVSYSYGYGSNILSDIS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 355 LSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYG-RP 433
Cdd:TIGR01193 495 LTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKE 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 434 DATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVL 513
Cdd:TIGR01193 575 NVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL 654
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 514 REaIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYREL 565
Cdd:TIGR01193 655 LN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
638-918 |
6.04e-46 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 167.30 E-value: 6.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGID----VGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGL 713
Cdd:cd18563 12 TALGLVPPYLTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 714 DAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTY 793
Cdd:cd18563 92 SFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 794 RRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGARE 873
Cdd:cd18563 172 HRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQ 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1108176189 874 VRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18563 252 VLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
300-554 |
5.12e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 169.64 E-value: 5.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 300 QQARAGAVRVLELIDSR-PTLVDGTKPLSPEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTL-- 376
Cdd:PRK11174 315 AQAVGAAESLVTFLETPlAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLln 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 377 ASLATRCYdvtQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTL 456
Cdd:PRK11174 395 ALLGFLPY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 457 PDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLAD 536
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWD 551
|
250
....*....|....*...
gi 1108176189 537 RVAVLDSGRLLDVGTPDE 554
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAE 569
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
334-555 |
3.01e-43 |
|
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: 157.49 E-value: 3.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 ---PEDAvLFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARA 484
Cdd:COG1122 81 fqnPDDQ-LFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAViecGIQEVLrEAIAD-----RTAVIFTRRRSMLT-LADRVAVLDSGRLLDVGTPDEV 555
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPR---GRRELL-ELLKRlnkegKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREV 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
958-1177 |
3.99e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 166.94 E-value: 3.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAG-INLRIPAGQTVVFVGSTGSGKSTLIKLVARFYdPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDA 1036
Cdd:PRK11174 364 TLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1037 IAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEA 1116
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1117 VVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLWAA 1177
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
943-1154 |
5.50e-42 |
|
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: 153.01 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 943 VFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIV 1022
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 TQ--EQYVFAGTVRDAIAYG------RPDATDAQVERAAREVGahpmitalDNGYLHQVTAggrNLSAGQLQLLALARAR 1094
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVG--------LEGLRDRSPF---TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1095 LVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVA-HGLA-IAEHADRIVVLEHGT 1154
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
958-1159 |
9.33e-42 |
|
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: 153.11 E-value: 9.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYD-----PTHGTVRVDGCDLREFDVD--GYRNRLGIVTQEQYVFA 1030
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRDAIAYG-------RPDATDAQVERAAREVGAHPmiTALDNgylhqvtAGGRNLSAGQLQLLALARARLVDPDILLL 1103
Cdd:cd03260 95 GSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD--EVKDR-------LHALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
334-546 |
5.03e-41 |
|
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: 148.90 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSGTIGANIaygrpdatpeqiataaraahieefvntlpdgyqtavgargltLSGGQRQRIALARALLHQPRLL 492
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREA-IADRTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-552 |
7.58e-41 |
|
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: 149.48 E-value: 7.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:cd03369 6 EIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSGTIGANI-AYGRpdATPEQIATAARaahieefvntlpdgyqtaVGARGLTLSGGQRQRIALARALLHQPR 490
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 491 LLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTP 552
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
645-918 |
5.46e-40 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 150.74 E-value: 5.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 645 PLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQI 724
Cdd:cd18564 34 PLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 725 VTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVT 804
Cdd:cd18564 114 LSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 805 ATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGAL 884
Cdd:cd18564 194 SVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL 273
|
250 260 270
....*....|....*....|....*....|....
gi 1108176189 885 VTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18564 274 LVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
899-1181 |
6.84e-40 |
|
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: 155.83 E-value: 6.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 899 GELAQMFDDYQRAAvAAGRIRSLLSTRTPSSPAARPVgtlrgeVVFDAVHYSYRTR---EVPALAGINLRIPAGQTVVFV 975
Cdd:COG1123 225 GPPEEILAAPQALA-AVPRLGAARGRAAPAAAAAEPL------LEVRNLSKRYPVRgkgGVRAVDDVSLTLRRGETLGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 976 GSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVtqeQYVF---------AGTVRDAIAYG------ 1040
Cdd:COG1123 298 GESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRV---QMVFqdpysslnpRMTVGDIIAEPlrlhgl 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1041 -RPDATDAQVERAAREVGahpmitaLDNGYL----HQvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVALDPATE 1115
Cdd:COG1123 375 lSRAERRERVAELLERVG-------LPPDLAdrypHE-------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQ 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1116 AVVQRATLTLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGGH-YSR-LWAAHTRL 1181
Cdd:COG1123 441 AQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANPQHpYTRaLLAAVPSL 511
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
940-1157 |
6.91e-40 |
|
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: 146.79 E-value: 6.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 940 GEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRL 1019
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEQYVFAGTVRDAI-AYGRpdATDAQVERAARevgahpmitaldngylhqVTAGGRNLSAGQLQLLALARARLVDP 1098
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVE 1157
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-545 |
1.55e-39 |
|
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: 145.69 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADR----PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvreltldslrsa 409
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPEDAVLFSGTIGANIAYGRP-DatPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQ 488
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfD--EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 489 PRLLIMDDPTSAVDAVIECGI-QEVLREAIAD-RTAVIFTRRRSMLTLADRVAVLDSGR 545
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIfENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
20-309 |
1.92e-39 |
|
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: 148.35 E-value: 1.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAI-AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQ 98
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIgGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 99 ALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALL-FDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSR 177
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLaFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 178 RLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAV 257
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 258 FALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
334-558 |
1.95e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.75 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTlDSLRSAIGLV 413
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANI-----AYGRPDATPEQiataaRAAHIEEFVNtLPDGYQTAVGarglTLSGGQRQRIALARALLH 487
Cdd:COG1131 79 PQEPALYPDlTVRENLrffarLYGLPRKEARE-----RIDELLELFG-LTDAADRKVG----TLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTrrrsmlT--------LADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLS------ThyleeaerLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
314-572 |
3.83e-39 |
|
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: 153.52 E-value: 3.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 314 DSRPTLVDGTKPLSPEARLS---LEFQRVSFGYVADRP----VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDV 386
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 387 TQGAVRIGGQDVRELT---LDSLRSAIGLVPED--AVLFSG-TIGANIAYG---RPDATPEQIatAARAAHIEEFVNtLP 457
Cdd:COG1123 318 TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDpySSLNPRmTVGDIIAEPlrlHGLLSRAER--RERVAELLERVG-LP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 458 DGYqtaVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREaIADRT--AVIF-------TRR 528
Cdd:COG1123 395 PDL---ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRD-LQRELglTYLFishdlavVRY 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1108176189 529 rsmltLADRVAVLDSGRLLDVGTPDEVWERcPRY---RELLSPAPDL 572
Cdd:COG1123 471 -----IADRVAVMYDGRIVEDGPTEEVFAN-PQHpytRALLAAVPSL 511
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
20-309 |
6.55e-39 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) 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: 349985 [Multi-domain] Cd Length: 293 Bit Score: 147.17 E-value: 6.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDD--AIAADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAF 97
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDAltAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 98 QALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALL-FDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRS 176
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALgPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 177 RRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMA 256
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 257 VFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18541 241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
334-582 |
7.44e-39 |
|
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: 145.14 E-value: 7.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAY-----GRPdatPEQIatAARAAHIEEFVNTLPDGYqtaVGARGLTLSGGQRQRIALARALLH 487
Cdd:cd03295 81 IQQIGLFPHmTVEENIALvpkllKWP---KEKI--RERADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEV---LREAIAdRTAVIFTRR-RSMLTLADRVAVLDSGRLLDVGTPDEVwercpryr 563
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEfkrLQQELG-KTIVFVTHDiDEAFRLADRIAIMKNGEIVQVGTPDEI-------- 223
|
250
....*....|....*....
gi 1108176189 564 eLLSPAPDLADDLVVAERS 582
Cdd:cd03295 224 -LRSPANDFVAEFVGADRL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
942-1167 |
3.13e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 143.28 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRtrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGI 1021
Cdd:COG1131 1 IEVRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAG-TVRD-----AIAYGRPDAT-DAQVERAAREVGahpmitaLDnGYLHQVTaggRNLSAGQLQLLALARAR 1094
Cdd:COG1131 78 VPQEPALYPDlTVREnlrffARLYGLPRKEaRERIDELLELFG-------LT-DAADRKV---GTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1095 LVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVA-HGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
947-1173 |
5.83e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 142.63 E-value: 5.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQ 1026
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 YVFA---GTVRDAIA-----YGRPDaTDAQVERAAREVGahpmitaLDNGYL----HQvtaggrnLSAGQLQLLALARAR 1094
Cdd:COG1124 89 YASLhprHTVDRILAeplriHGLPD-REERIAELLEQVG-------LPPSFLdrypHQ-------LSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1095 LVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGGH- 1170
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGPKHp 233
|
...
gi 1108176189 1171 YSR 1173
Cdd:COG1124 234 YTR 236
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
645-918 |
1.38e-37 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 143.39 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 645 PLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQI 724
Cdd:cd18540 22 PLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 725 VTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVT 804
Cdd:cd18540 102 MARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRIT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 805 ATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGAL 884
Cdd:cd18540 182 GAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTL 261
|
250 260 270
....*....|....*....|....*....|....
gi 1108176189 885 VTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18540 262 VAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-499 |
2.98e-37 |
|
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: 137.01 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSG-TIGANI 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 429 AYGRPDATPEQIATAARAAHIEEFVNtLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTS 499
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
945-1165 |
1.02e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 139.41 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 945 DAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQ 1024
Cdd:COG1120 5 ENLSVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQYV-FAGTVRDAIAYGR---------PDATD-AQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARA 1093
Cdd:COG1120 83 EPPApFGLTVRELVALGRyphlglfgrPSAEDrEAVEEALERTG----LEHLADRPVDE-------LSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1094 RLVDPDILLLDEATVALDPATeavvQRATLTLAAR------RTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELL 1165
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAH----QLEVLELLRRlarergRTVVMVLHDLNLAaRYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
334-555 |
1.48e-36 |
|
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: 138.08 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDV-----TQGAVRIGGQDVRELTLD--SL 406
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 407 RSAIGLVPEDAVLFSGTIGANIAYG------RPDATPEQIATAA--RAAHIEEFVNTLpdgyqtavgaRGLTLSGGQRQR 478
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlrKAALWDEVKDRL----------HALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 479 IALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTrrRSM---LTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVT--HNMqqaARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
72-309 |
1.89e-36 |
|
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: 139.86 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 72 LLTYVRRYYGGRIAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVL-RHVLTLLLGVAV 150
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLvRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 151 MTWLSVPLALLAVLLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYA 230
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 231 AQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
333-558 |
1.98e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLAslatRC----YDVTQGAVRIGGQDV-------REl 401
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLL----RMiagfETPDSGRILLDGRDVtglppekRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 402 tldslrsaIGLVPEDAVLFSG-TIGANIAYG--RPDATPEQIATAARAA----HIEEFVNTLPDgyqtavgarglTLSGG 474
Cdd:COG3842 79 --------VGMVFQDYALFPHlTVAENVAFGlrMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 475 QRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFTRRRS-MLTLADRVAVLDSGRLLDVGT 551
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEeALALADRIAVMNDGRIEQVGT 219
|
....*..
gi 1108176189 552 PDEVWER 558
Cdd:COG3842 220 PEEIYER 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
948-1155 |
2.77e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 948 HYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQY 1027
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 VFAGTVRDAIA----YGRPDATDAQVERAAREVGahpmitaLDNGYLHQVTaggRNLSAGQLQLLALARARLVDPDILLL 1103
Cdd:COG4619 85 LWGGTVRDNLPfpfqLRERKFDRERALELLERLG-------LPPDILDKPV---ERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAAR--RTTLIVAHGLA-IAEHADRIVVLEHGTV 1155
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEegRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
640-918 |
3.88e-36 |
|
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: 139.09 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 640 AGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDD 719
Cdd:cd18552 14 TTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 720 GDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQF----RRASnwtyRR 795
Cdd:cd18552 94 SSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIgkrlRKIS----RR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 796 ARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVR 875
Cdd:cd18552 170 SQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1108176189 876 AGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18552 250 SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
942-1159 |
4.62e-36 |
|
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: 134.75 E-value: 4.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDvDGYRNRLGI 1021
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAGTVRDAIaygrpdatdaqveraarevgahpmitaldngylhqvtagGRNLSAGQLQLLALARARLVDPDIL 1101
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1102 LLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
947-1159 |
1.02e-35 |
|
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: 135.71 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---YRNRLGIVT 1023
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiRRKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1024 QEQY-----VFagTVRDAIA-----YGRPDATDAQVERAAREVGAHPMITALDNGYLHQvtaggrnLSAGQLQLLALARA 1093
Cdd:cd03257 89 QDPMsslnpRM--TIGEQIAeplriHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE-------LSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1094 RLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
335-545 |
1.44e-35 |
|
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: 134.52 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGY-VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 ---PEDAvLFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARA 484
Cdd:cd03225 81 fqnPDDQ-FFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAViecGIQEVLrEAIAD-----RTAVIFTRRRSML-TLADRVAVLDSGR 545
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPA---GRRELL-ELLKKlkaegKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
945-1155 |
1.58e-35 |
|
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: 133.11 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 945 DAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQ 1024
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQYVFAGTVRDAIaygrpdatdaqveraarevgahpmitaldngylhqvtaggrnLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:cd03246 84 DDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1105 EATVALDPATEAVVQRATLTLAARRTTLI-VAHGLAIAEHADRIVVLEHGTV 1155
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIvIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-583 |
1.84e-35 |
|
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: 142.35 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVA-DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVT---QGAVRIGGQDVRELTLDSLRSA 409
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPED--AVLFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIAL 481
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR-TAVIFTRRRS--MLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLgvVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260
....*....|....*....|....*
gi 1108176189 559 cpryRELLSPAPDLADDLVVAERSP 583
Cdd:COG1123 234 ----PQALAAVPRLGAARGRAAPAA 254
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-309 |
2.53e-35 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 136.51 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAI--AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAF 97
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTigSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 98 QALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRS 176
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADgIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 177 RRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMA 256
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 257 VFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
347-550 |
2.90e-35 |
|
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: 134.17 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAIGLVPEDAvlFSG- 422
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP--MSSl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 ----TIGANIA------YGRPDATPEQIATAARAAHI---EEFVNTLPdgYQtavgargltLSGGQRQRIALARALLHQP 489
Cdd:cd03257 96 nprmTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVglpEEVLNRYP--HE---------LSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 490 RLLIMDDPTSAVDAVIECGIQEVLREAIADR-TAVIF-TRRRSML-TLADRVAVLDSGRLLDVG 550
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLFiTHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
616-1167 |
3.47e-35 |
|
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: 142.24 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 616 LRRLLREFRGPLALSlllvavqTCAGLLPPL-------LIRHGIdVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAmv 688
Cdd:COG4615 4 LRLLLRESRWLLLLA-------LLLGLLSGLanagliaLINQAL-NATGAALARLLLLFAGLLVLLLLSRLASQLLLT-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 689 agYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTgLVVAVISVVTLVGILV--ALLAIRAR 766
Cdd:COG4615 74 --RLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAylAWLSPPLF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 767 LVLLIFttmpvLALATWQFRRASNWTYR---RAR-------HRLGTVTATLREyaagLRIAQAFRAEYRGLQsYFAHSDD 836
Cdd:COG4615 151 LLTLVL-----LGLGVAGYRLLVRRARRhlrRAReaedrlfKHFRALLEGFKE----LKLNRRRRRAFFDED-LQPTAER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 837 YRRLGVRGQRLLALYYPF--VALLCSLATTLVLLdgareVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVA 914
Cdd:COG4615 221 YRDLRIRADTIFALANNWgnLLFFALIGLILFLL-----PALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 915 AGRIRSL---LSTRTPSSPAARPVGTLRG--EVVFDAVHYSYRTREVP---ALAGINLRIPAGQTVVFVGSTGSGKSTLI 986
Cdd:COG4615 296 LRKIEELelaLAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 987 KLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFagtvrDAIAYGRPDATDAQVERAAREVG-AHpmITAL 1065
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLERLElDH--KVSV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1066 DNGYLHQvtaggRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATL-TLAAR-RTTLIVAHGLAIAEH 1143
Cdd:COG4615 449 EDGRFST-----TDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELLpELKARgKTVIAISHDDRYFDL 523
|
570 580
....*....|....*....|....
gi 1108176189 1144 ADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:COG4615 524 ADRVLKMDYGKLVELTGPAALAAS 547
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-309 |
5.79e-35 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 135.72 E-value: 5.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAI-----AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRM 94
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLiqlgpGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 95 DAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIA 173
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDgLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 174 HRSRRLLAAATHcAQEHK-AAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPAL 252
Cdd:cd18563 161 YFFWKKIRRLFH-RQWRRwSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 253 GQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18563 240 GTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
944-1158 |
8.30e-35 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 132.60 E-value: 8.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRT--REVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCdlrefDVDGYRNRLGI 1021
Cdd:cd03293 3 VRNVSKTYGGggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFA-GTVRDAIAYG------RPDATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARAR 1094
Cdd:cd03293 78 VFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVG----LSGFENAYPHQ-------LSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1095 LVDPDILLLDEATVALDPATEAVVQRATLTL--AARRTTLIVAHGLAIAEH-ADRIVVLE--HGTVVED 1158
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFlADRVVVLSarPGRIVAE 215
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
638-918 |
1.04e-34 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 134.53 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:cd18576 9 SAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALAT----WQFRRASnwty 793
Cdd:cd18576 89 ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAvlfgRRIRKLS---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 794 RRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGARE 873
Cdd:cd18576 165 KKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1108176189 874 VRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18576 245 VLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
81-555 |
1.48e-34 |
|
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: 144.32 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 81 GGRIAHLVQHdlrMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLAL 160
Cdd:TIGR00957 1032 GGIQASRVLH---QDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAA 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 161 LAVLLvpvIGLIAHRSRRLLAAATHCAQE----HKAAVTGVVDAAVCGIRVVKAFGQEER----ETVKLVTASRALY--- 229
Cdd:TIGR00957 1109 VIIPP---LGLLYFFVQRFYVASSRQLKRlesvSRSPVYSHFNETLLGVSVIRAFEEQERfihqSDLKVDENQKAYYpsi 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 230 -AAQLRVARLNAhFGPLLQTLPALgqMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAvr 308
Cdd:TIGR00957 1186 vANRWLAVRLEC-VGNCIVLFAAL--FAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYS-- 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 309 vlELIDSRPTLVDGTKPlsPEA---RLSLEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCY 384
Cdd:TIGR00957 1261 --ETEKEAPWQIQETAP--PSGwppRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 385 DVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANI-AYGRpdATPEQIATAARAAHIEEFVNTLPDGYQTA 463
Cdd:TIGR00957 1337 ESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHE 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 464 VGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDS 543
Cdd:TIGR00957 1415 CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDK 1494
|
490
....*....|..
gi 1108176189 544 GRLLDVGTPDEV 555
Cdd:TIGR00957 1495 GEVAEFGAPSNL 1506
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
942-1163 |
2.19e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRtREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD---LREFDVDGYRNR 1018
Cdd:COG2884 2 IRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LGIVTQEQYVFAG-TVRDAIAY-----GRPdatDAQVERAAREVgahpmitaLDN-GYLHQVTAGGRNLSAGQLQLLALA 1091
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALplrvtGKS---RKEIRRRVREV--------LDLvGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1092 RARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVA-HGLAIAEHAD-RIVVLEHGTVVEDGAHTE 1163
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
20-309 |
2.65e-34 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 133.71 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAadHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQA 99
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSA--GGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 100 LLRWDGRQQDRWSSGQLIVRTTNDLQLVQALL-FDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRR 178
Cdd:cd18551 79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELItSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 179 LLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVF 258
Cdd:cd18551 159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 259 ALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18551 239 GVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
334-546 |
3.94e-34 |
|
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: 129.36 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTlDSLRSAIGL 412
Cdd:cd03247 1 LSINNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSGTIGANIaygrpdatpeqiataaraahieefvntlpdgyqtavgarGLTLSGGQRQRIALARALLHQPRLL 492
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
334-550 |
6.47e-34 |
|
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: 129.95 E-value: 6.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslRSAIGLV 413
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALL 486
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFTRRRS-MLTLADRVAVLDSGRLLDVG 550
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-555 |
7.91e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 130.93 E-value: 7.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVL-FSGTIGANIAYGR---------PDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALA 482
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEAlERTGLEHLADRPVD-----------ELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVLRE--AIADRTAVIftrrrSM--LTLA----DRVAVLDSGRLLDVGTPDE 554
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVM-----VLhdLNLAaryaDRLVLLKDGRIVAQGPPEE 224
|
.
gi 1108176189 555 V 555
Cdd:COG1120 225 V 225
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
640-918 |
1.13e-33 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 131.79 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 640 AGLLPPLLIRHGIDVGIRRHVLsalWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDD 719
Cdd:cd18551 14 ASLAQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 720 GDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHR 799
Cdd:cd18551 91 RSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 800 LGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVI 879
Cdd:cd18551 171 LGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGAL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1108176189 880 SVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18551 251 TVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-557 |
1.20e-33 |
|
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: 130.10 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAI 410
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-TIGANIAYG---RPDATPEQIATAAR----AAHIEEFVNTLPDGyqtavgargltLSGGQRQRIALA 482
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLekleLVGLPGAADKMPSE-----------LSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVLREaIADR---TAVIFTRR-RSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRE-LRDElglTSVVVTHDlDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-558 |
1.36e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.27 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLatrcYDVTQGAVRIGGQDVreLTLDSLRS 408
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiAGL----EDPTSGEILIGGRDV--TDLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 409 AIGLVPEDAVLF-SGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIAL 481
Cdd:COG3839 76 NIAMVFQSYALYpHMTVYENIAFPlklrkvPKAEIDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAviecgiqeVLREAIADRTAVIFTRRRS-----------MLTLADRVAVLDSGRLLDVG 550
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDA--------KLRVEMRAEIKRLHRRLGTttiyvthdqveAMTLADRIAVMNDGRIQQVG 216
|
....*...
gi 1108176189 551 TPDEVWER 558
Cdd:COG3839 217 TPEELYDR 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
944-1167 |
1.48e-33 |
|
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: 136.96 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPT---HGTVRVDGCDLREFDVDGYRNRLG 1020
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1021 IVTQE--QYVFAGTVRDAIAYG------RPDATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALAR 1092
Cdd:COG1123 87 MVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVG----LERRLDRYPHQ-------LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1093 ARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGvVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
944-1190 |
1.58e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 130.63 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFD-VDGYRNRLGIV 1022
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 TQE---QYVfAGTVRDAIAYG------RPDATDAQVERAAREVGahpMitaldNGYLHQVTAggrNLSAGQLQLLALARA 1093
Cdd:TIGR04520 83 FQNpdnQFV-GATVEDDVAFGlenlgvPREEMRKRVDEALKLVG---M-----EDFRDREPH---LLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1094 RLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEHADRIVVLEHGTVVEDG------AHTELL 1165
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVELL 230
|
250 260
....*....|....*....|....*
gi 1108176189 1166 AAGGhysrlwaahtrLCSPEITQLQ 1190
Cdd:TIGR04520 231 KEIG-----------LDVPFITELA 244
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
942-1166 |
2.43e-33 |
|
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: 129.34 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREvPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGI 1021
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAG-TVRDAIA-------YGRPdatdaQVERAARE----VGAHPmiTALDNGYLHQvtaggrnLSAGQLQLLA 1089
Cdd:cd03295 80 VIQQIGLFPHmTVEENIAlvpkllkWPKE-----KIRERADEllalVGLDP--AEFADRYPHE-------LSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1090 LARARLVDPDILLLDEATVALDPATEAVVQRATLTL--AARRTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
334-546 |
3.35e-33 |
|
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: 126.36 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDsLRSAIGLV 413
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFsgtiganiaygrPDATPEQIataaraahieefvntlpdgyqtavgargLTLSGGQRQRIALARALLHQPRLLI 493
Cdd:cd03230 79 PEEPSLY------------ENLTVREN----------------------------LKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 494 MDDPTSAVDAVIECGIQEVLREAIADRTAVIFTrrrS-----MLTLADRVAVLDSGRL 546
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLS---ShileeAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
950-1155 |
3.87e-33 |
|
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: 126.36 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTRevPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgYRNRLGIVTQEQYVF 1029
Cdd:cd03230 9 RYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AG-TVRDaiaygrpdatdaqveraarevgahpmitaldngYLHqvtaggrnLSAGQLQLLALARARLVDPDILLLDEATV 1108
Cdd:cd03230 86 ENlTVRE---------------------------------NLK--------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1108176189 1109 ALDPATEAVVQRATLTLAARRTTLIVA-HGLAIAEH-ADRIVVLEHGTV 1155
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-558 |
8.55e-33 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 127.45 E-value: 8.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslRSAIGLVPEDAVLFSG-TIGAN 427
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 428 IAYG-----RPDAT-PEQIATAARAAHIEEFVNTLPdgyqtavgargLTLSGGQRQRIALARALLHQPRLLIMDDPTSAV 501
Cdd:cd03299 92 IAYGlkkrkVDKKEiERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 502 DAVIECGIQEVLREAI--ADRTAVIFTRRRS-MLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:cd03299 161 DVRTKEKLREELKKIRkeFGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
347-555 |
8.96e-33 |
|
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: 128.10 E-value: 8.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGA 426
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYGRpDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIE 506
Cdd:cd03288 114 NLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1108176189 507 CGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENL 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
942-1159 |
1.08e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.42 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL--REFDVDGYRNRL 1019
Cdd:COG1126 2 IEIENLHKSFGDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEQYVFAG-TVRDAIAY------GRPDAtdaQVERAARE----VG------AHPmitaldngylhqvtaggRNLSA 1082
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLapikvkKMSKA---EAEERAMEllerVGladkadAYP-----------------AQLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1083 GQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTT-LIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTmVVVTHEMGFAREvADRVVFMDGGRIVEEG 218
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
20-309 |
1.08e-32 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV 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: 349989 [Multi-domain] Cd Length: 293 Bit Score: 129.12 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQ 98
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNgDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 99 ALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVM----TWLSVPLALLAVLLVPVIGLIA 173
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNgLINLIPDLLTLVGIVIIMfslnVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 174 HRSRRllaaATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALG 253
Cdd:cd18545 162 RRARK----AWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 254 QMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18545 238 TALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
334-546 |
1.25e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.08 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSGTIGANIAYgrPDATPEQIATAARAAHIEEFVNtLPDGY-QTAVGarglTLSGGQRQRIALARALLHQPRLL 492
Cdd:COG4619 80 PQEPALWGGTVRDNLPF--PFQLRERKFDRERALELLERLG-LPPDIlDKPVE----RLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 493 IMDDPTSAVD-----AVIECgIQEVLREaiADRTAVIFT-----RRRsmltLADRVAVLDSGRL 546
Cdd:COG4619 153 LLDEPTSALDpentrRVEEL-LREYLAE--EGRAVLWVShdpeqIER----VADRVLTLEAGRL 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
942-1159 |
1.29e-32 |
|
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: 126.09 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRtrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLreFDVDGYRNRLGI 1021
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAG-TVRDAIAYG--RPDATDAQVERAAREVGAHPMITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDP 1098
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTL--AARRTTLIVAHGLAIA-EHADRIVVLEHGTVVEDG 1159
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEAlALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-549 |
1.87e-32 |
|
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: 126.05 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGY---VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELtldslRSAI 410
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFS-GTIGANIAYG-----RPDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALAR 483
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgVPKAEARERAEELlELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIA-DRTAVIftrrrsMLT--------LADRVAVLDS--GRLLDV 549
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVL------LVThdideavfLADRVVVLSArpGRIVAE 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
334-555 |
2.30e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 127.16 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVR-ELTLDSLRSAIG 411
Cdd:TIGR04520 1 IEVENVSFSYPeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LV---PEDAvLFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPdgyqtavgargLTLSGGQRQRIALA 482
Cdd:TIGR04520 81 MVfqnPDNQ-FVGATVEDDVAFGlenlgvPREEMRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAViecGIQEVL-------REaiADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPK---GRKEVLetirklnKE--EGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-555 |
2.68e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 126.46 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 339 VSFGYVADR-PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV---P 414
Cdd:COG1124 9 VSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVfqdP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 EDAVLFSGTIGANIA-----YGRPDaTPEQIATAARAAHI-EEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQ 488
Cdd:COG1124 89 YASLHPRHTVDRILAeplriHGLPD-REERIAELLEQVGLpPSFLDRYPH-----------QLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 489 PRLLIMDDPTSAVDAVIECGIQEVLREAIADR-TAVIFTR--RRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREERgLTYLFVShdLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
334-558 |
3.40e-32 |
|
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: 125.43 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVreLTLDSLRSAIGLV 413
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALL 486
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLREaIADR---TAVIFTRRRS-MLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKR-LQKElgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
638-918 |
4.15e-32 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) 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: 349987 [Multi-domain] Cd Length: 291 Bit Score: 127.21 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:cd18543 12 TLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DDGDAQIVTAVTADVEAIVAFLRTGLVVAViSVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRAR 797
Cdd:cd18543 92 RWQSGQLLSRATSDLSLVQRFLAFGPFLLG-NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 798 HRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAG 877
Cdd:cd18543 171 DQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1108176189 878 VISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18543 251 SLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
949-1167 |
4.31e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 125.39 E-value: 4.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 949 YSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD---LREFDVDGYRNRLGIVTQE 1025
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1026 QYVFAG-TVRDAIAYGRPDATDAQVERAARevgAHPMITALdnGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:cd03258 91 FNLLSSrTVFENVALPLEIAGVPKAEIEER---VLELLELV--GLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1105 EATVALDPATEAVVQRATLTLAARR--TTLIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELglTIVLITHEMeVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
928-1166 |
4.52e-32 |
|
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: 126.18 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 928 SSPAARPVGtLRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL 1007
Cdd:cd03288 7 GSSNSGLVG-LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1008 REFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRpDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQL 1087
Cdd:cd03288 86 SKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1088 LALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-309 |
5.12e-32 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 127.24 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATYL----------------LTYVRRYYGGR 83
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLllaaaalvgiallrglASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 84 IAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVP-NVLRHVLTLLLGVAVMTWLSVPLALLA 162
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVlPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 163 VLLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHF 242
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 243 GPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
335-545 |
5.54e-32 |
|
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: 122.35 E-value: 5.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVP 414
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 EdavlfsgtiganiaygrpdatpeqiataaraahieefvntlpdgyqtavgargltLSGGQRQRIALARALLHQPRLLIM 494
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 495 DDPTSAVDAVIECGIQEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSGR 545
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVthDPELAELAADRVIVLKDGK 157
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
292-558 |
9.09e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 135.49 E-value: 9.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 292 LAGMLTIAQQARAG---AVRVLELID---SRPTLVDGTKPLSP-EARLSLEFQRVSFGYVAD-RPVLREISLSVRAGETL 363
Cdd:PLN03232 1186 LSGVLRQASKAENSlnsVERVGNYIDlpsEATAIIENNRPVSGwPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKV 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 364 AVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIaygrpDATPEQ---- 439
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPFSEHndad 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 440 IATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIAD 519
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
250 260 270
....*....|....*....|....*....|....*....
gi 1108176189 520 RTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
942-1158 |
9.29e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 124.00 E-value: 9.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRT--REVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---YR 1016
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElarLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1017 NR-LGIVTQEQYVFAG-TVRDAIAY-----GRPDATD-AQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLL 1088
Cdd:COG1136 85 RRhIGFVFQFFNLLPElTALENVALplllaGVSRKERrERARELLERVG----LGDRLDHRPSQ-------LSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1089 ALARArLV-DPDILLLDEATVALDPATEAVVQRATLTLAAR--RTTLIVAHGLAIAEHADRIVVLEHGTVVED 1158
Cdd:COG1136 154 AIARA-LVnRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
942-1178 |
1.02e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTRevPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfdvdgYRNRLGI 1021
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYV---FAGTVRDAIAYG---------RPDATD-AQVERAAREVGahpmITALDNgylHQVtaggRNLSAGQLQLL 1088
Cdd:COG1121 80 VPQRAEVdwdFPITVRDVVLMGrygrrglfrRPSRADrEAVDEALERVG----LEDLAD---RPI----GELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTT-LIVAHGL-AIAEHADRIVVLE-----HGTVVEDGAH 1161
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTiLVVTHDLgAVREYFDRVLLLNrglvaHGPPEEVLTP 228
|
250
....*....|....*..
gi 1108176189 1162 TELLAAGGHYSRLWAAH 1178
Cdd:COG1121 229 ENLSRAYGGPVALLAHG 245
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
338-555 |
1.02e-31 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 124.15 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAIGLVP 414
Cdd:cd03261 7 TKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 EDAVLFSG-TIGANIAY------GRPDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALL 486
Cdd:cd03261 84 QSGALFDSlTVFENVAFplrehtRLSEEEIREIVLEKlEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 487 HQPRLLIMDDPTSAVD----AVIECGIQEvLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:cd03261 153 LDPELLLYDEPTAGLDpiasGVIDDLIRS-LKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
942-1158 |
1.03e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.20 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTR--EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDlrefdVDGYRNRL 1019
Cdd:COG1116 8 LELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEQYVFA-GTVRDAIAYG------RPDATDAQVERAAREVG------AHPmitaldngylHQvtaggrnLSAGQLQ 1086
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGlagfedAYP----------HQ-------LSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1087 LLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAA--RRTTLIVAHGL--AIAeHADRIVVLEH--GTVVED 1158
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHDVdeAVF-LADRVVVLSArpGRIVEE 222
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
638-918 |
1.19e-31 |
|
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: 125.98 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGID------VGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRL 711
Cdd:cd18547 12 TLLSVLGPYLLGKAIDliieglGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 712 GLDAFED--DGDaqIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRAS 789
Cdd:cd18547 92 PLSYFDThsHGD--IMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 790 NWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLD 869
Cdd:cd18547 170 QKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1108176189 870 GAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18547 250 GGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
334-545 |
1.35e-31 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 121.91 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDS--LRSAIG 411
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSG-TIGANIAYGrpdatpeqiataaraahieefvntlpdgyqtavgargltLSGGQRQRIALARALLHQPR 490
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 491 LLIMDDPTSAVDAVIECGIQEVLREaIADR--TAVIFTRR--RSMLTLADRVAVLDSGR 545
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKS-LQAQlgITVVLVTHdlDEAARLADRVVVLRDGK 178
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
20-309 |
1.41e-31 |
|
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: 125.68 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQ 98
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAgDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 99 ALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSR 177
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTgLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 178 RLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAV 257
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 258 FALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18546 241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
20-309 |
1.79e-31 |
|
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: 125.58 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA---DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDA 96
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPgqgDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 97 FQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDV-PNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIA-- 173
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGlVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATyl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 174 ---------HRSRRLLAAATHCAQEHkaavtgvvdaaVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGP 244
Cdd:cd18544 161 frkksrkayREVREKLSRLNAFLQES-----------ISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRP 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 245 LLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18544 230 LVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
959-1108 |
2.11e-31 |
|
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: 120.45 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAG-TVRDAI 1037
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1038 AYGRP------DATDAQVERAAREVGahpmitalDNGYLHQ-VTAGGRNLSAGQLQLLALARARLVDPDILLLDEATV 1108
Cdd:pfam00005 81 RLGLLlkglskREKDARAEEALEKLG--------LGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
950-1154 |
2.53e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 120.43 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQeqyvf 1029
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 agtvrdaiaygrpdatdaqveraarevgahpmitaldngylhqvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVA 1109
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1108176189 1110 LDPATEAVVQRATLTLAAR-RTTLIVAHGLAIAEHA-DRIVVLEHGT 1154
Cdd:cd00267 111 LDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
944-1165 |
5.40e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.56 E-value: 5.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVT 1023
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1024 Q---EQYVFAgTVRDAIAYG------RPDATDAQVERAAREVGahpMITALDNGYLhqvtaggrNLSAGQLQLLALARAR 1094
Cdd:PRK13632 90 QnpdNQFIGA-TVEDDIAFGlenkkvPPKKMKDIIDDLAKKVG---MEDYLDKEPQ--------NLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1095 LVDPDILLLDEATVALDPATEAVVQRATLTLAARRT-TLI-VAHGLAIAEHADRIVVLEHGTVVEDGAHTELL 1165
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
955-1166 |
6.74e-31 |
|
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: 121.39 E-value: 6.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgYRNRLGI--VTQEQYVFAG- 1031
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRD----AIAYGRPDATDAQVERaarevgAHPMITALDNgYLHQVtagGRNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:cd03224 91 TVEEnlllGAYARRRAKRKARLER------VYELFPRLKE-RRKQL---AGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1108 VALDPATEAVVQRATLTLAARRTT-LIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTiLLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-555 |
8.38e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 8.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELtldslRSAIGLV 413
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 P-------------EDAVLfSGTIGANIAYGRPDATPEQIATAA-RAAHIEEFVNTLpdgyqtaVGarglTLSGGQRQRI 479
Cdd:COG1121 81 PqraevdwdfpitvRDVVL-MGRYGRRGLFRRPSRADREAVDEAlERVGLEDLADRP-------IG----ELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTrrrS-----MLTLADRVAVLDsGRLLDVGTPDE 554
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVV---ThdlgaVREYFDRVLLLN-RGLVAHGPPEE 224
|
.
gi 1108176189 555 V 555
Cdd:COG1121 225 V 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
942-1155 |
8.80e-31 |
|
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: 121.06 E-value: 8.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRT--REVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---YR 1016
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1017 NR-LGIVTQEQYVFAG-TVRDAIAYGRPDATDAQVERAARevgAHPMITALdnGYLHQVTAGGRNLSAGQLQLLALARAR 1094
Cdd:cd03255 81 RRhIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRER---AEELLERV--GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1095 LVDPDILLLDEATVALDPATEAVVQRATLTLA--ARRTTLIVAHGLAIAEHADRIVVLEHGTV 1155
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
334-550 |
2.16e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.16 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAI 410
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-TIGANIAY-----GRPdatPEQIATAARAA----HIEEFVNTLPDgyqtavgarglTLSGGQRQRIA 480
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtGKS---RKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIF-TRRRSML-TLADRVAVLDSGRLLDVG 550
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIaTHDLELVdRMPKRVLELEDGRLVRDE 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
333-558 |
2.18e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLATrcydVTQGAVRIGGQDVrELTLDSLRS 408
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLlriiAGLET----PDSGRIVLNGRDL-FTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 409 AIGLVPEDAVLFSG-TIGANIAYGRPDATPEQIATAARAA------HIEEFVNTLPDgyqtavgarglTLSGGQRQRIAL 481
Cdd:COG1118 76 RVGFVFQHYALFPHmTVAENIAFGLRVRPPSKAEIRARVEellelvQLEGLADRYPS-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIAD--RTAVIFTR-RRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
640-918 |
2.80e-30 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) 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: 349985 [Multi-domain] Cd Length: 293 Bit Score: 122.13 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 640 AGLLPPLLIRHGIDvGIRRHVL--SALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:cd18541 14 LQLLIPRIIGRAID-ALTAGTLtaSQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DD--GDaqIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRR 795
Cdd:cd18541 93 KNrtGD--LMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 796 ARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVR 875
Cdd:cd18541 171 VQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVI 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1108176189 876 AGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18541 251 RGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
944-1154 |
3.24e-30 |
|
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: 118.06 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRtrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLR--EFDVDGYRNRLGI 1021
Cdd:cd03229 3 LKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAG-TVRDAIAYGrpdatdaqveraarevgahpmitaldngylhqvtaggrnLSAGQLQLLALARARLVDPDI 1100
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1101 LLLDEATVALDPATEAVVQRATLTLAAR--RTTLIVAHGLAIAEH-ADRIVVLEHGT 1154
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
334-567 |
4.14e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.71 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRV--SFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLasLatRCY----DVTQGAVRIGGQDV--RELTLDS 405
Cdd:COG1126 2 IEIENLhkSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTL--L--RCInlleEPDSGTITVDGEDLtdSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 406 LRSAIGLVPEDAVLFSG-TIGANIAY------GRPDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQ 477
Cdd:COG1126 75 LRRKVGMVFQQFNLFPHlTVLENVTLapikvkKMSKAEAEERAMELlERVGLADKADAYPA-----------QLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 478 RIALARALLHQPRLLIMDDPTSAVDAVIecgIQEVLR--EAIADR--TAVI------FTRRrsmltLADRVAVLDSGRLL 547
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPEL---VGEVLDvmRDLAKEgmTMVVvthemgFARE-----VADRVVFMDGGRIV 215
|
250 260
....*....|....*....|..
gi 1108176189 548 DVGTPDEVWE--RCPRYRELLS 567
Cdd:COG1126 216 EEGPPEEFFEnpQHERTRAFLS 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-565 |
5.87e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 5.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYV---ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslrsaI 410
Cdd:COG1116 8 LELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFs-gTIGANIAYGRPDATPEQIATAARAAHI------EEFVNTLPDgyqtavgarglTLSGGQRQRIALAR 483
Cdd:COG1116 83 GVVFQEPALLpwlTVLDNVALGLELRGVPKAERRERARELlelvglAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIAD-RTAVIFTrrrsmlT--------LADRVAVLDS--GRL---LDV 549
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFV------ThdvdeavfLADRVVVLSArpGRIveeIDV 225
|
250
....*....|....*....
gi 1108176189 550 GTP---DEVWERCPRYREL 565
Cdd:COG1116 226 DLPrprDRELRTSPEFAAL 244
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-575 |
7.70e-30 |
|
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: 121.31 E-value: 7.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFgYVADRPV--LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYD---VTQGAVRIGGQDVRELTLDSLRSA--- 409
Cdd:COG0444 8 KVYF-PTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIrgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 -IGLVPEDA------VLfsgTIGANIA--------YGRPDATpEQIATAARAAHI---EEFVNTLPdgYQtavgargltL 471
Cdd:COG0444 87 eIQMIFQDPmtslnpVM---TVGDQIAeplrihggLSKAEAR-ERAIELLERVGLpdpERRLDRYP--HE---------L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 472 SGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR-TAVIFtrrrsmLT--------LADRVAVLD 542
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILF------IThdlgvvaeIADRVAVMY 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1108176189 543 SGRLLDVGTPDEVWERcPR--Y-RELLSPAPDLADD 575
Cdd:COG0444 226 AGRIVEEGPVEELFEN-PRhpYtRALLSSIPRLDPD 260
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
334-546 |
1.02e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGY---VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATrCYDV-TQGAVRIGGQDVRELT---LDSL 406
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG-GLDRpTSGEVLIDGQDISSLSereLARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 407 R-SAIGLVPEDAVLFSG-TIGANIAY-----GRPDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQR 478
Cdd:COG1136 84 RrRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRERARELlERVGLGDRLDHRPS-----------QLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 479 IALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIAD--RTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
333-554 |
1.22e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 128.32 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYVAD-RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:PLN03130 1237 SIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSGTIGANIaygrpDATPEQ----IATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLH 487
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNL-----DPFNEHndadLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDE 554
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPEN 1458
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-546 |
1.50e-29 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 117.59 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADR---PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLR 407
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 408 SA-IGLVPEDAVLFSG-TIGANIAY-----GRPDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRI 479
Cdd:cd03255 81 RRhIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELlERVGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLRE--AIADRTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-558 |
1.96e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.96 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:PRK13635 6 IRVEHISFRYPdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 V---PEDAvlFSG-TIGANIAYG-------RPDATpEQIATAARAAHIEEFVNTLPdgyqtavgARgltLSGGQRQRIAL 481
Cdd:PRK13635 86 VfqnPDNQ--FVGaTVQDDVAFGlenigvpREEMV-ERVDQALRQVGMEDFLNREP--------HR---LSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAViecGIQEVLrEAIADrtavifTRRRSMLTL------------ADRVAVLDSGRLLDV 549
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPR---GRREVL-ETVRQ------LKEQKGITVlsithdldeaaqADRVIVMNKGEILEE 221
|
....*....
gi 1108176189 550 GTPDEVWER 558
Cdd:PRK13635 222 GTPEEIFKS 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-571 |
1.97e-29 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 118.90 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSL----RSAIGLVPEDAVLFSG-TI 424
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANIAY-----GRPDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:cd03294 120 LENVAFglevqGVPRAEREERAAEAlELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 499 SAVDAVIECGIQEVLREAIAD--RTAVIFTRR-RSMLTLADRVAVLDSGRLLDVGTPDEVwercpryreLLSPAPD 571
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDlDEALRLGDRIAIMKDGRLVQVGTPEEI---------LTNPAND 255
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
332-557 |
3.21e-29 |
|
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: 117.44 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVS--FGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslRSA 409
Cdd:cd03296 1 MSIEVRNVSkrFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPEDAVLFSG-TIGANIAYG---RPDAT-PEQIATAARAAHIEEFVNTlpDGYQTAVGARgltLSGGQRQRIALARA 484
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVAFGlrvKPRSErPPEAEIRAKVHELLKLVQL--DWLADRYPAQ---LSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAVIECGIQEVLREaIADR---TAVIFTRRRS-MLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRR-LHDElhvTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
947-1155 |
3.57e-29 |
|
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: 116.09 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL--REFDVDGYRNRLGIVTQ 1024
Cdd:cd03262 6 LHKSFGDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQYVFAG-TVRDAIAY------GRPdatDAQVERAAREvgahpmitALDN-GYLHQVTAGGRNLSAGQLQLLALARARLV 1096
Cdd:cd03262 84 QFNLFPHlTVLENITLapikvkGMS---KAEAEERALE--------LLEKvGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLAARRTT-LIVAHGLAIAEH-ADRIVVLEHGTV 1155
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTmVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
334-555 |
5.61e-29 |
|
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: 116.53 E-value: 5.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVS--FGYVADR-PVLREISLSVRAGETLAVVGAPGSGKSTLaslaTRCYDV----TQGAVRIGGQDVRELTLDSL 406
Cdd:cd03258 2 IELKNVSkvFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerpTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 407 RSA---IGLVPEDAVLFSG-TIGANIAYgrpdatPEQIATAARAaHIEEFVNTLPD--GYQTAVGARGLTLSGGQRQRIA 480
Cdd:cd03258 78 RKArrrIGMIFQHFNLLSSrTVFENVAL------PLEIAGVPKA-EIEERVLELLElvGLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFT------RRrsmltLADRVAVLDSGRLLDVGTP 552
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLIThemevvKR-----ICDRVAVMEKGEVVEEGTV 225
|
...
gi 1108176189 553 DEV 555
Cdd:cd03258 226 EEV 228
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
640-918 |
6.81e-29 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 118.44 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 640 AGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTAT-----------VVIRWVV----QWGSAMVAGYTGEQVLFRLRSVV 704
Cdd:cd18565 14 FDLAPPLLIGVAIDAVFNGEASFLPLVPASLGPADprgqlwllgglTVAAFLLeslfQYLSGVLWRRFAQRVQHDLRTDT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 705 FAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQ 784
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 785 FRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATT 864
Cdd:cd18565 174 FQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFV 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 865 LVLLDGAREVRAGV------ISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18565 254 ATFVVGGYWVLDGPplftgtLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-555 |
7.81e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.01 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGY-VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:PRK13632 9 KVENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 ---PEDAvlFSG-TIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPdgyqtavgargLTLSGGQRQRIALAR 483
Cdd:PRK13632 89 fqnPDNQ--FIGaTVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSM--LTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdeAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
642-910 |
8.81e-29 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 117.55 E-value: 8.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 642 LLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIR----WVVQ-WGSAMvagytGEQVLFRLRSVVFAHAQRLGLDAF 716
Cdd:cd18549 19 LVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRtllnYFVTyWGHVM-----GARIETDMRRDLFEHLQKLSFSFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 717 EDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRA 796
Cdd:cd18549 94 DNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 797 RHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRA 876
Cdd:cd18549 174 REKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIK 253
|
250 260 270
....*....|....*....|....*....|....
gi 1108176189 877 GVISVGALVTYLLYIELLYTPIGELAQMFDDYQR 910
Cdd:cd18549 254 GEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
947-1192 |
1.46e-28 |
|
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: 117.85 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDP---THGTVRVDGCDLREFDVDGYR----NRL 1019
Cdd:COG0444 9 VYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEQY-----VFagTVRDAIA--------YGRPDAtDAQVERAAREVGAHPMITALDNgYLHQvtaggrnLSAGQLQ 1086
Cdd:COG0444 89 QMIFQDPMtslnpVM--TVGDQIAeplrihggLSKAEA-RERAIELLERVGLPDPERRLDR-YPHE-------LSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1087 LLALARARLVDPDILLLDEATVALDpateAVVQRATLTL-----AARRTTLI-VAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALD----VTIQAQILNLlkdlqRELGLAILfITHDLGvVAEIADRVAVMYAGRIVEEG 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1108176189 1160 AHTELLAAGGH-YSR-LWAAHTRLcSPEITQLQCI 1192
Cdd:COG0444 234 PVEELFENPRHpYTRaLLSSIPRL-DPDGRRLIPI 267
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
952-1166 |
1.49e-28 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 116.20 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRN----RLGIVTQEqy 1027
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 vFA----GTVRDAIAYGRPDATDAQVERAAREVGAhpmitaldngyLHQVTAGG------RNLSAGQLQLLALARARLVD 1097
Cdd:cd03294 111 -FAllphRTVLENVAFGLEVQGVPRAEREERAAEA-----------LELVGLEGwehkypDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1098 PDILLLDEATVALDPATEAVVQRATLTLAA--RRTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEAlRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
942-1167 |
1.89e-28 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 115.08 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGY---RNR 1018
Cdd:COG1127 6 IEVRNLTKSFGDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LGIVTQEqyvfaG------TVRDAIAYG---RPDATDAQVERAAREVgahpmitaldngyLHQV---TAGGRN---LSAG 1083
Cdd:COG1127 84 IGMLFQG-----GalfdslTVFENVAFPlreHTDLSEAEIRELVLEK-------------LELVglpGAADKMpseLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1084 QLQLLALARArLV-DPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:COG1127 146 MRKRVALARA-LAlDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*...
gi 1108176189 1160 AHTELLAA 1167
Cdd:COG1127 225 TPEELLAS 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
957-1154 |
2.00e-28 |
|
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: 113.72 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyrnRLGIVTQEQYVFAGTVRDA 1036
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1037 IAYGRP-DAtdaqvERAAREVGA---HPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDP 1112
Cdd:cd03250 86 ILFGKPfDE-----ERYEKVIKAcalEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1108176189 1113 ATEA-VVQRATL-TLAARRTTLIVAHGLAIAEHADRIVVLEHGT 1154
Cdd:cd03250 161 HVGRhIFENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
950-1159 |
3.10e-28 |
|
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: 113.40 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFdvdgyRNRLGIVTQEQYV- 1028
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 --FAGTVRDAIAYGR---------PDATDAQ-VERAAREVGahpmITALDNgylHQVTaggrNLSAGQLQLLALARARLV 1096
Cdd:cd03235 81 rdFPISVRDVVLMGLyghkglfrrLSKADKAkVDEALERVG----LSELAD---RQIG----ELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGL-AIAEHADRIVVLEHgTVVEDG 1159
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLgLVLEYFDRVLLLNR-TVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
944-1166 |
3.47e-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: 114.14 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG---CDLREFDVDGYRNRLG 1020
Cdd:cd03261 3 LRGLTKSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1021 IVTQEQYVFAG-TVRDAIAYG---RPDATDAQVERAARE----VGAHpmitaldnGYLHQVTAggrNLSAGQLQLLALAR 1092
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLR--------GAEDLYPA---ELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1093 ARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
348-557 |
5.15e-28 |
|
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: 113.30 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDS-LRSAIGLVPEDAVLFSG-TIG 425
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 426 ANI---AYGRPDATPEQIataaraahIEEFVNTLPDGYQTAvGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:cd03224 94 ENLllgAYARRRAKRKAR--------LERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 503 AVIECGIQEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTILLVeqNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
327-555 |
5.86e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.98 E-value: 5.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 327 SPEARLSLEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLasLatRC----YDVTQGA-----VRIGGQD 397
Cdd:COG1117 5 ASTLEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTL--L--RClnrmNDLIPGArvegeILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 398 VRELTLD--SLRSAIGLVPEDAVLFSGTIGANIAYG------RPDATPEQIA-TAARAAHI-EEFVNTLpdgyqtavGAR 467
Cdd:COG1117 80 IYDPDVDvvELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVeESLRKAALwDEVKDRL--------KKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 468 GLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD----AVIECGIQEvLREaiaDRTAVIFT------RRrsmltLADR 537
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILE-LKK---DYTIVIVThnmqqaAR-----VSDY 222
|
250
....*....|....*...
gi 1108176189 538 VAVLDSGRLLDVGTPDEV 555
Cdd:COG1117 223 TAFFYLGELVEFGPTEQI 240
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
637-918 |
7.96e-28 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 114.80 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 637 QTCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAF 716
Cdd:cd18548 11 EVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 717 EDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRA 796
Cdd:cd18548 91 DKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 797 RHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRA 876
Cdd:cd18548 171 QKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINA 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1108176189 877 GVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18548 251 GSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
947-1168 |
1.09e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.96 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQ-- 1024
Cdd:PRK13635 11 ISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQnp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 -EQYVFAgTVRDAIAYG-------RPDATDaQVERAAREVGAHPmitaldngYLHQVTAggrNLSAGQLQLLALARARLV 1096
Cdd:PRK13635 91 dNQFVGA-TVQDDVAFGlenigvpREEMVE-RVDQALRQVGMED--------FLNREPH---RLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAG 1168
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
17-308 |
3.25e-27 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 112.93 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 17 RRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAI-AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMD 95
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLpSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 96 AFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVP-NVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAH 174
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPeDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 175 RSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQ 254
Cdd:cd18549 161 YFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 255 MAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVR 308
Cdd:cd18549 241 LVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
955-1158 |
6.21e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 111.33 E-value: 6.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD---LREFDvdgyRNRL-GIVTQEqyVFA 1030
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK----RAKYiGRVFQD--PMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRD-------AIAYGRPD------ATDAQVERAAREvgahpMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVD 1097
Cdd:COG1101 92 GTAPSmtieenlALAYRRGKrrglrrGLTKKRRELFRE-----LLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1098 PDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGL--AIaEHADRIVVLEHGTVVED 1158
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMeqAL-DYGNRLIMMHEGRIILD 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
955-1165 |
7.48e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.57 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLR--EFDVDGYRNRLGIVTQEQYVFAG- 1031
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRDAIAYGrP----DATDAQVERAAREVGAHPMITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:PRK09493 93 TALENVMFG-PlrvrGASKEEAEKQARELLAKVGLAERAHHYPSE-------LSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1108 VALDPATEAVVQRATLTLAARRTTL-IVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELL 1165
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMvIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
956-1155 |
8.47e-27 |
|
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: 109.42 E-value: 8.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG---CDLREFDVDGYRNRLGIVTQE-QYVFAG 1031
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvSDLRGRAIPYLRRKIGVVFQDfRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRDAIAYGRpDATDAQVERAAREVGAhpmitALDN-GYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVAL 1110
Cdd:cd03292 94 NVYENVAFAL-EVTGVPPREIRKRVPA-----ALELvGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1108176189 1111 DPATEAVVQRATLTLAARRTTLIVA-HGLAIAE-HADRIVVLEHGTV 1155
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDtTRHRVIALERGKL 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
947-1159 |
1.28e-26 |
|
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: 107.91 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQeq 1026
Cdd:cd03214 5 LSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 yvfagtvrdaiaygrpdatdaqverAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEA 1106
Cdd:cd03214 81 -------------------------ALELLG----LAHLADRPFNE-------LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1107 TVALDPATeavvQRATLTLAAR------RTTLIVAHGLAIA-EHADRIVVLEHGTVVEDG 1159
Cdd:cd03214 125 TSHLDIAH----QIELLELLRRlarergKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
349-577 |
1.55e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLAslatRCYD----VTQGAVRIGGQDVRELTLDSLRSA---IGLVPEDAVLFS 421
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINllerPTSGSVLVDGVDLTALSERELRAArrkIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 422 G-TIGANIAY-----GRPdatPEQIAtaARAAHIEEFVntlpdgyqtavgarGLT---------LSGGQRQRIALARALL 486
Cdd:COG1135 96 SrTVAENVALpleiaGVP---KAEIR--KRVAELLELV--------------GLSdkadaypsqLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLREaIADR---TAVIFT------RRrsmltLADRVAVLDSGRLLDVGTPDEVwe 557
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKD-INRElglTIVLIThemdvvRR-----ICDRVAVLENGRIVEQGPVLDV-- 228
|
250 260
....*....|....*....|
gi 1108176189 558 rcpryreLLSPAPDLADDLV 577
Cdd:COG1135 229 -------FANPQSELTRRFL 241
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
945-1159 |
2.54e-26 |
|
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: 108.05 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 945 DAVHYSYRTREvpALAGINLRIPAGQTVVfVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGIVTQ 1024
Cdd:cd03264 4 ENLTKRYGKKR--ALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQYVFAG-TVRDAIAY-----GRPDAT-DAQVERAAREVGahpmitaldngyLHQVtAGGR--NLSAGQLQLLALARARL 1095
Cdd:cd03264 80 EFGVYPNfTVREFLDYiawlkGIPSKEvKARVDEVLELVN------------LGDR-AKKKigSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1096 VDPDILLLDEATVALDPAtEAVVQRATLT-LAARRTTLIVAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03264 147 GDPSILIVDEPTAGLDPE-ERIRFRNLLSeLGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
311-573 |
3.13e-26 |
|
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: 114.78 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 311 ELIDSRPTLVDGTKPLSPEARLSLEFQRVSF--------GYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATR 382
Cdd:COG4172 255 KLLAAEPRGDPRPVPPDAPPLLEARDLKVWFpikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 383 CYDvTQGAVRIGGQDVRELT---LDSLRSAIGLVPEDAvlFSG-----TIGANIAYG----RPDATPEQIATAARAAHIE 450
Cdd:COG4172 335 LIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEALEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 451 -------------EFvntlpdgyqtavgargltlSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAI 517
Cdd:COG4172 412 vgldpaarhryphEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQ 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 518 ADRT----------AVIftrrRSMltlADRVAVLDSGRLLDVGTPDEVWERcPR--Y-RELLSPAPDLA 573
Cdd:COG4172 473 REHGlaylfishdlAVV----RAL---AHRVMVMKDGKVVEQGPTEQVFDA-PQhpYtRALLAAAPLLE 533
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-571 |
3.45e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.98 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV---RELTLDSLRSAIGLVPEDAvlFSG-----TI 424
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELRPLRRRMQMVFQDP--YASlnprmTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANIaygrpdATPEQIATAARAAHIEEFVNTLPDgyqtAVGARGLTL-------SGGQRQRIALARALLHQPRLLIMDDP 497
Cdd:COG4608 115 GDII------AEPLRIHGLASKAERRERVAELLE----LVGLRPEHAdryphefSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 498 TSAVDAVIECGIQEVLREaiadrtavifTRRRSMLT-------------LADRVAVLDSGRLLDVGTPDEVWERcPR--Y 562
Cdd:COG4608 185 VSALDVSIQAQVLNLLED----------LQDELGLTylfishdlsvvrhISDRVAVMYLGKIVEIAPRDELYAR-PLhpY 253
|
250
....*....|..
gi 1108176189 563 -RELLS--PAPD 571
Cdd:COG4608 254 tQALLSavPVPD 265
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
958-1159 |
3.52e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.97 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYD--P---THGTVRVDGCDL--REFDVDGYRNRLGIVTQEQYVFA 1030
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRDAIAYG-------RPDATDAQVERAAREVgahpmitAL-----DNgyLHQvtaGGRNLSAGQLQLLALARARLVDP 1098
Cdd:COG1117 106 KSIYDNVAYGlrlhgikSKSELDEIVEESLRKA-------ALwdevkDR--LKK---SALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFG 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
346-550 |
4.84e-26 |
|
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: 107.34 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELtlDSLRSAIGLVPEDAVLFSG-TI 424
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMVFQNYALYPHmTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:cd03301 90 YDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 499 SAVDAViecgIQEVLREAIA------DRTAVIFTRRRS-MLTLADRVAVLDSGRLLDVG 550
Cdd:cd03301 159 SNLDAK----LRVQMRAELKrlqqrlGTTTIYVTHDQVeAMTMADRIAVMNDGQIQQIG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
334-566 |
5.69e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.87 E-value: 5.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVS--FGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLaslaTRCYD----VTQGAVRIGGQDVRELTLD--S 405
Cdd:PRK09493 2 IEFKNVSkhFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTL----LRCINkleeITSGDLIVDGLKVNDPKVDerL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 406 LRSAIGLVPEDAVLFSG-TIGANIAYGrpdatPEQIATAARAAhIEEFVNTLpdgyqtaVGARGLT---------LSGGQ 475
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHlTALENVMFG-----PLRVRGASKEE-AEKQAREL-------LAKVGLAerahhypseLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 476 RQRIALARALLHQPRLLIMDDPTSAVDAVIEcgiQEVLR--EAIADR--TAVIFTRRrsmLTLADRVA----VLDSGRLL 547
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELR---HEVLKvmQDLAEEgmTMVIVTHE---IGFAEKVAsrliFIDKGRIA 215
|
250 260
....*....|....*....|.
gi 1108176189 548 DVGTPDEVWERCP--RYRELL 566
Cdd:PRK09493 216 EDGDPQVLIKNPPsqRLQEFL 236
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
637-918 |
1.03e-25 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 108.72 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 637 QTCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAF 716
Cdd:cd18550 11 SALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 717 EDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATwqfRRASN--WTYR 794
Cdd:cd18550 91 TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPT---RRVGRrrRKLT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 795 RAR-HRLGTVTATLREY--AAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGA 871
Cdd:cd18550 168 REQqEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1108176189 872 REVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18550 248 LLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
350-554 |
1.08e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 106.30 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTlDSLRSAIGLVPEDAVLFSGTIG-ANI 428
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 429 A-----YGRPDATPEQiataaRAAHIEEFVNtLPDGYQTAVGarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA 503
Cdd:cd03265 95 YiharlYGVPGAERRE-----RIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 504 VIECGIQEVLREAIADRTAVIFTRRRSML---TLADRVAVLDSGRLLDVGTPDE 554
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEeaeQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-304 |
1.16e-25 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 108.34 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQ 98
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQgDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 99 ALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSR 177
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGtLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 178 RLLAAATHCAQEHKAAVTGVV--DAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQM 255
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMqeTLSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1108176189 256 AVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARA 304
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLA 289
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
948-1166 |
1.21e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.51 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 948 HYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---YRNRLGIVTQ 1024
Cdd:PRK11153 10 VFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkARRQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQYVFAG-TVRDAIAY-----GRPDA-TDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVD 1097
Cdd:PRK11153 90 HFNLLSSrTVFDNVALplelaGTPKAeIKARVTELLELVG----LSDKADRYPAQ-------LSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1098 PDILLLDEATVALDPATeavvQRATLTLAA---RR---TTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK11153 159 PKVLLCDEATSALDPAT----TRSILELLKdinRElglTIVLITHEMDvVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
334-555 |
1.34e-25 |
|
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: 106.88 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAI 410
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 G-------LVPEDAVLfsgtigANIAYGRPDA-----------TPEQIataARAAHIEEFVNTLPDGYQtavgaRGLTLS 472
Cdd:cd03256 81 GmifqqfnLIERLSVL------ENVLSGRLGRrstwrslfglfPKEEK---QRALAALERVGLLDKAYQ-----RADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 473 GGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVI------FTRRrsmltLADRVAVLDSG 544
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVslhqvdLARE-----YADRIVGLKDG 221
|
250
....*....|.
gi 1108176189 545 RLLDVGTPDEV 555
Cdd:cd03256 222 RIVFDGPPAEL 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
23-309 |
1.55e-25 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 107.95 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 23 GFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQALL 101
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGgDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 102 RWDGRQQDRWSSGQLIVRTTNDLQLVQ-ALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRRLL 180
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQdTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 181 AAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFAL 260
Cdd:cd18576 161 RKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1108176189 261 GGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18576 241 GGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
941-1190 |
1.78e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.80 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 941 EVVFDAVHYSYRTR---EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL----REFDVD 1013
Cdd:PRK13634 2 DITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1014 GYRNRLGIVTQ--EQYVFAGTVRDAIAYGRPD--ATDAQVERAARE----VGahpmitaLDNGYLHQVTAggrNLSAGQL 1085
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREmielVG-------LPEELLARSPF---ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1086 QLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHT 1162
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPR 231
|
250 260
....*....|....*....|....*...
gi 1108176189 1163 ELLAAGGhysrlWAAHTRLCSPEITQLQ 1190
Cdd:PRK13634 232 EIFADPD-----ELEAIGLDLPETVKFK 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
335-542 |
1.89e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 105.69 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGYVaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELtldslRSAIGLVP 414
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 -------------EDAVLfSGTIGANIAYGRPDATPEQIATAARAAhieefvntlpdgyqtaVGARGL------TLSGGQ 475
Cdd:cd03235 75 qrrsidrdfpisvRDVVL-MGLYGHKGLFRRLSKADKAKVDEALER----------------VGLSELadrqigELSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 476 RQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTR--RRSMLTLADRVAVLD 542
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVThdLGLVLEYFDRVLLLN 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
948-1170 |
2.34e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 108.63 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 948 HYSYRTREVPALAGINLRIPAGQtvVF--VGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD---LREFDVDGYRNRLGIV 1022
Cdd:COG1135 10 TFPTKGGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAARRKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 TQEqyvF----AGTVRDAIAY-----GRPDAtdaqvERAAR------EVGahpmITALDNGYLHQvtaggrnLSAGQLQL 1087
Cdd:COG1135 88 FQH---FnllsSRTVAENVALpleiaGVPKA-----EIRKRvaelleLVG----LSDKADAYPSQ-------LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1088 LALARArLV-DPDILLLDEATVALDPA-TEAVVQ-----RATLTLaarrTTLIVAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:COG1135 149 VGIARA-LAnNPKVLLCDEATSALDPEtTRSILDllkdiNRELGL----TIVLITHEMDvVRRICDRVAVLENGRIVEQG 223
|
250
....*....|.
gi 1108176189 1160 AHTELLAAGGH 1170
Cdd:COG1135 224 PVLDVFANPQS 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
959-1165 |
2.89e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 105.88 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgyRNRLGIVTQEQYVFAG-TVRDAI 1037
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYG--RPDATDAQVERAAREVGAHPMITALDNGYlhqvtagGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATE 1115
Cdd:cd03299 93 AYGlkKRKVDKKEIERKVLEIAEMLGIDHLLNRK-------PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1116 AVVqRATLTLAARR---TTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTELL 1165
Cdd:cd03299 166 EKL-REELKKIRKEfgvTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
346-554 |
3.97e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.89 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRElTLDSLRSAIGLVPEDAVLFSG-TI 424
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANIA-YGRPDATPEQIATAARAAHIEEFvnTLPDGYQTAVGarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA 503
Cdd:cd03263 93 REHLRfYARLKGLPKSEIKEEVELLLRVL--GLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 504 VIECGIQEVLREAIADRTAVIFTrrRSML---TLADRVAVLDSGRLLDVGTPDE 554
Cdd:cd03263 167 ASRRAIWDLILEVRKGRSIILTT--HSMDeaeALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
340-546 |
4.00e-25 |
|
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: 104.53 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLaslaTRCY----DVTQGAVRIGGQDV--RELTLDSLRSAIGLV 413
Cdd:cd03262 9 SFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTL----LRCInlleEPDSGTIIIDGLKLtdDKKNINELRQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAY------GRPDATPEQIATAA-RAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARAL 485
Cdd:cd03262 82 FQQFNLFPHlTVLENITLapikvkGMSKAEAEERALELlEKVGLADKADAYPA-----------QLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 486 LHQPRLLIMDDPTSAVDAVIecgIQEVL----REAIADRTAVI------FTRRrsmltLADRVAVLDSGRL 546
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPEL---VGEVLdvmkDLAEEGMTMVVvthemgFARE-----VADRVIFMDDGRI 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
944-1165 |
4.29e-25 |
|
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: 105.55 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHG-TVRVDGCDLREFDVDGYRNRLGIV 1022
Cdd:COG1119 6 LRNVTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 T---QEQYVFAGTVRDAIAYGR-------PDATDAQVERAAR---EVGahpmITALDNGYLHQvtaggrnLSAGQLQLLA 1089
Cdd:COG1119 84 SpalQLRFPRDETVLDVVLSGFfdsiglyREPTDEQRERARElleLLG----LAHLADRPFGT-------LSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1090 LARArLV-DPDILLLDEATVALDP-ATEAVVQR-ATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTELL 1165
Cdd:COG1119 153 IARA-LVkDPELLILDEPTAGLDLgARELLLALlDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
338-524 |
4.38e-25 |
|
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: 104.26 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLdslRSAIGLVPEDA 417
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 418 --VLFSGTIGANIAYG--RPDATPEQIATAARAAHIEEFVNTLPdgyqtavgargLTLSGGQRQRIALARALLHQPRLLI 493
Cdd:cd03226 81 dyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190
....*....|....*....|....*....|.
gi 1108176189 494 MDDPTSAVDAVIECGIQEVLREAIADRTAVI 524
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVI 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
950-1152 |
4.40e-25 |
|
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: 104.10 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGIVTQEQYVF 1029
Cdd:COG4133 9 SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AG-TVRDAIAY----GRPDATDAQVERAAREVGahpmitaLDnGYLHQVTaggRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:COG4133 88 PElTVRENLRFwaalYGLRADREAIDEALEAVG-------LA-GLADLPV---RQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1108176189 1105 EATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEH 1152
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
945-1163 |
4.61e-25 |
|
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: 104.82 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 945 DAVHYSYRTRE--VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGY----RNR 1018
Cdd:COG4181 12 RGLTKTVGTGAgeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LGIVTQ-EQYVFAGTVRDAIAY-----GRPDATdaqvERAAREvgahpmitaldngyLHQVTAGGR------NLSAGQLQ 1086
Cdd:COG4181 92 VGFVFQsFQLLPTLTALENVMLplelaGRRDAR----ARARAL--------------LERVGLGHRldhypaQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1087 LLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR-TTLI-VAHGLAIAEHADRIVVLEHGTVVEDGAHTE 1163
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVlVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
334-555 |
4.66e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 105.06 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSL-RSAIGL 412
Cdd:COG0410 4 LEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSG-TIGANI---AYGRPDAtpeqiatAARAAHIEEFVNTLPDGYQTAvGARGLTLSGGQRQRIALARALLHQ 488
Cdd:COG0410 83 VPEGRRIFPSlTVEENLllgAYARRDR-------AEVRADLERVYELFPRLKERR-RQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 489 PRLLIMDDPTSavdaviecGIQEVLREAIADRTAVIftRRRSM------------LTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:COG0410 155 PKLLLLDEPSL--------GLAPLIVEEIFEIIRRL--NREGVtillveqnarfaLEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
956-1164 |
5.34e-25 |
|
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: 104.96 E-value: 5.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD---LREFDVDGYRNRLGIVTQE-QYVFAG 1031
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQIGMIFQQfNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRDAIAYGRPDATDA------QVERAAREVGAHpmitALDN-GYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:cd03256 94 SVLENVLSGRLGRRSTwrslfgLFPKEEKQRALA----ALERvGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1105 EATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
955-1159 |
5.65e-25 |
|
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: 104.26 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLRefDVDGYRNRLGIVTQEQYVFAG-TV 1033
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYPHmTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 RDAIAYG------RPDATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:cd03301 90 YDNIAFGlklrkvPKDEIDERVREVAELLQ----IEHLLDRKPKQ-------LSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1108 VALDpATEAVVQRATLTLAARR---TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:cd03301 159 SNLD-AKLRVQMRAELKRLQQRlgtTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
951-1156 |
6.41e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.12 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 951 YRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGIVTQEQYVFA 1030
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 G-TVRD-----AIAYGRPDAT-DAQVERAAREVGAHPmitaldngYLHQVTaggRNLSAGQLQLLALARARLVDPDILLL 1103
Cdd:cd03263 89 ElTVREhlrfyARLKGLPKSEiKEEVELLLRVLGLTD--------KANKRA---RTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVV 1156
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
332-566 |
6.49e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.86 E-value: 6.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRV--SFGYVAdrpVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRsa 409
Cdd:PRK10851 1 MSIEIANIkkSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPEDAVLFSG-TIGANIAYG--------RPDATpeqiATAARAAHIEEFVNT--LPDGYQTavgarglTLSGGQRQR 478
Cdd:PRK10851 76 VGFVFQHYALFRHmTVFDNIAFGltvlprreRPNAA----AIKAKVTQLLEMVQLahLADRYPA-------QLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 479 IALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFTR-RRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
250
....*....|.
gi 1108176189 556 WeRCPRYRELL 566
Cdd:PRK10851 225 W-REPATRFVL 234
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
20-309 |
6.78e-25 |
|
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: 106.33 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-------DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDL 92
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGlgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 93 RMDAFQALLR-----WDGRqqdrwSSGQLIVRTTNDL-QLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVP----LALLA 162
Cdd:cd18547 81 RKDLFEKLQRlplsyFDTH-----SHGDIMSRVTNDVdNISQALSQSLTQLISSILTIVGTLIMMLYISPLltliVLVTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 163 VLLVPVIGLIAHRSRRLLAAathcAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHF 242
Cdd:cd18547 156 PLSLLVTKFIAKRSQKYFRK----QQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 243 GPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18547 232 MPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
942-1164 |
7.91e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.65 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDP---THGTVRVDGCDLREFDVDGYRNR 1018
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LGIVTQ---EQYVFAgTVRDAIAYGRPDatdaqveraaREVGAHPMITALDN-----GYLHQVTAGGRNLSAGQLQLLAL 1090
Cdd:PRK13640 86 VGIVFQnpdNQFVGA-TVGDDVAFGLEN----------RAVPRPEMIKIVRDvladvGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1091 ARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
640-918 |
9.44e-25 |
|
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: 105.72 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 640 AGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDD 719
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 720 GDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHR 799
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 800 LGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVI 879
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1108176189 880 SVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
942-1164 |
1.40e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRtrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLreFDVDGYRNRLGI 1021
Cdd:COG3842 6 LELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEqyvFA----GTVRDAIAYG------RPDATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALA 1091
Cdd:COG3842 82 VFQD---YAlfphLTVAENVAFGlrmrgvPKAEIRARVAELLELVG----LEGLADRYPHQ-------LSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1092 RARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAH----GLAIaehADRIVVLEHGTVVEDGAHTEL 1164
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHdqeeALAL---ADRIAVMNDGRIEQVGTPEEI 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
955-1166 |
1.61e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.52 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgYRNRLGI--VTQEQYVFAG- 1031
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH-RIARLGIgyVPEGRRIFPSl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRD---AIAYGRPDatDAQVERAAREVgahpmitaldngY---------LHQvtaGGRNLSAGQLQLLALARARLVDPD 1099
Cdd:COG0410 94 TVEEnllLGAYARRD--RAEVRADLERV------------YelfprlkerRRQ---RAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1100 ILLLDEATVALDPATEAVVQRATLTLAARRTT-LIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTiLLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
942-1165 |
1.77e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.08 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGI 1021
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYV-FAGTVRDAIAYGR------PDATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARAr 1094
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRaphglsRAEDDALVAAALAQVD----LAHLAGRDYPQ-------LSGGEQQRVQLARV- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1095 LV-------DPDILLLDEATVALDPATeavvQRATLTLAARRTT------LIVAHGLAIAEH-ADRIVVLEHGTVVEDGA 1160
Cdd:PRK13548 149 LAqlwepdgPPRWLLLDEPTSALDLAH----QHHVLRLARQLAHerglavIVVLHDLNLAARyADRIVLLHQGRLVADGT 224
|
....*
gi 1108176189 1161 HTELL 1165
Cdd:PRK13548 225 PAEVL 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
335-550 |
2.89e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 100.97 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVP 414
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 edavlfsgtiganiaygrpdatpeQIATAARAAHIEEfvntlpdgyqtavgaRGL-TLSGGQRQRIALARALLHQPRLLI 493
Cdd:cd03214 80 ------------------------QALELLGLAHLAD---------------RPFnELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 494 MDDPTSAVDaviecgI---QEVL----REAIADRTAVIFTrrrsM--LTLA----DRVAVLDSGRLLDVG 550
Cdd:cd03214 121 LDEPTSHLD------IahqIELLellrRLARERGKTVVMV----LhdLNLAaryaDRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
958-1159 |
3.10e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 102.52 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGyRNRLGIV-----TQeqyVFAG- 1031
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGrtfqiPR---LFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRDAIAYGRP--------DATDAQVERAAREVgAHPMITALDNGYLHQVTAGgrNLSAGQLQLLALARARLVDPDILLL 1103
Cdd:cd03219 91 TVLENVMVAAQartgsgllLARARREEREARER-AEELLERVGLADLADRPAG--ELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGL-AIAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERgITVLLVEHDMdVVMSLADRVTVLDQGRVIAEG 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
940-1164 |
7.67e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.38 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 940 GEVVFDAVHYSYRtrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVdGYRNrL 1019
Cdd:COG3839 2 ASLELENVSKSYG--GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP-KDRN-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1020 GIVTQEqyvFA----GTVRDAIAYG------RPDATDAQVERAAREVGahpmITAldngYLHqvtaggR---NLSAGQLQ 1086
Cdd:COG3839 78 AMVFQS---YAlyphMTVYENIAFPlklrkvPKAEIDRRVREAAELLG----LED----LLD------RkpkQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1087 LLALARArLV-DPDILLLDEATVALDPA------TE-AVVQRATltlaaRRTTLIVAH----GLAIAehaDRIVVLEHGT 1154
Cdd:COG3839 141 RVALGRA-LVrEPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRL-----GTTTIYVTHdqveAMTLA---DRIAVMNDGR 211
|
250
....*....|
gi 1108176189 1155 VVEDGAHTEL 1164
Cdd:COG3839 212 IQQVGTPEEL 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
333-503 |
8.98e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.63 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFgYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYD---VTQGAVRIGGQDVRelTLDSLRSA 409
Cdd:COG4136 1 MLSLENLTI-TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLT--ALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPEDAVLFSG-TIGANIAYgrpdATPEQIATAARAAHIEEfvnTLpdgyqTAVGARGL------TLSGGQRQRIALA 482
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAF----ALPPTIGRAQRRARVEQ---AL-----EEAGLAGFadrdpaTLSGGQRARVALL 145
|
170 180
....*....|....*....|.
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDA 503
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDA 166
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
365-557 |
1.23e-23 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 103.34 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 365 VVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTlDSLRSaIGLVPEDAVLFSG-TIGANIAYG-RPDATP-EQIA 441
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRH-INMVFQSYALFPHmTVEENVAFGlKMRKVPrAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 442 TAARAA----HIEEFVNTLPdgyqtavgargLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLReAI 517
Cdd:TIGR01187 79 PRVLEAlrlvQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK-TI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1108176189 518 ADR---TAVIFTR-RRSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:TIGR01187 147 QEQlgiTFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
942-1190 |
1.89e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRT---REVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGY--- 1015
Cdd:PRK13646 3 IRFDNVSYTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1016 -RNRLGIVTQ--EQYVFAGTVRDAIAYGrPDATDAQVEraarEVGAHPMITALDNGYLHQVTAGGR-NLSAGQLQLLALA 1091
Cdd:PRK13646 83 vRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLD----EVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1092 RARLVDPDILLLDEATVALDPATEAVVQR--ATLTLAARRTTLIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTELLAAG 1168
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRllKSLQTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDK 237
|
250 260
....*....|....*....|..
gi 1108176189 1169 ghySRLWAAHTRLcsPEITQLQ 1190
Cdd:PRK13646 238 ---KKLADWHIGL--PEIVQLQ 254
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
947-1166 |
2.00e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYR--TRevpALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQ 1024
Cdd:PRK13647 10 LHFRYKdgTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 --EQYVFAGTVRDAIAYG------RPDATDAQVERAAREVGahpMITALDNGYLHqvtaggrnLSAGQLQLLALARARLV 1096
Cdd:PRK13647 87 dpDDQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVR---MWDFRDKPPYH--------LSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVA-HGLAIA-EHADRIVVLEHGTVVEDGAhTELLA 1166
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAaEWADQVIVLKEGRVLAEGD-KSLLT 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
943-1166 |
2.17e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.21 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 943 VFDAVHYSYRTREVPAlagiNLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVdgYRNRLGIV 1022
Cdd:COG3840 3 RLDDLTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 TQEQYVFAG-TVRDAIAYG-----RPDATD-AQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARL 1095
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVG----LAGLLDRLPGQ-------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1096 VDPDILLLDEATVALDPAteavvQRATL-----TLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:COG3840 146 RKRPILLLDEPFSALDPA-----LRQEMldlvdELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-546 |
2.87e-23 |
|
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: 98.27 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGLVPED----AVLFS 421
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDrkreGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 422 GTIGANIAYGRpdatpeqiataaraahieefvntlpdgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAV 501
Cdd:cd03215 93 LSVAENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 502 D--AVIEcgIQEVLREAIADRTAVIFTrrrS-----MLTLADRVAVLDSGRL 546
Cdd:cd03215 136 DvgAKAE--IYRLIRELADAGKAVLLI---SseldeLLGLCDRILVMYEGRI 182
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
957-1164 |
3.00e-23 |
|
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: 100.11 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVdgyRNR-LGIVTQEQYVFAG-TVR 1034
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnVGFVFQHYALFRHmTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1035 DAIAYG--------RPDAtdAQVERAAREVGAHPMITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEA 1106
Cdd:cd03296 93 DNVAFGlrvkprseRPPE--AEIRAKVHELLKLVQLDWLADRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1107 TVALDpateAVVqRATLTLAARR-------TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:cd03296 164 FGALD----AKV-RKELRRWLRRlhdelhvTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
347-557 |
3.14e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTldSLRSAIGLVPEDAVLFSG-TIG 425
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 426 ANIAYG-RPDATPEQiATAARAA------HIEEFVNTLPdgYQtavgargltLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:PRK11607 110 QNIAFGlKQDKLPKA-EIASRVNemlglvHMQEFAKRKP--HQ---------LSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 499 SAVDAVIECGIQ-EVLReaIADR---TAVIFTR-RRSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:PRK11607 178 GALDKKLRDRMQlEVVD--ILERvgvTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-558 |
3.81e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 107.17 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSGTIGANIaygRP--DATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQP 489
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 490 RLLI-MDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PTZ00243 1465 SGFIlMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
952-1159 |
4.08e-23 |
|
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: 99.33 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGIV--TQEQYVF 1029
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AGTVRDAIAYGRP--DATDAQVERAAREVGAHPMITALdngyLHQVTaggRNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:cd03267 109 DLPVIDSFYLLAAiyDLPPARFKKRLDELSELLDLEEL----LDTPV---RQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1108 VALDPATEAVVQRATLTLAARR--TTLIVAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKdIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
959-1190 |
4.86e-23 |
|
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: 100.31 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDpTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAI- 1037
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYGRpdATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAV 1117
Cdd:cd03289 99 PYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1118 VQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYS---------RLWAAH-----TRLCS 1183
Cdd:cd03289 177 IRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKqaispsdrlKLFPRRnssksKRKPR 256
|
....*..
gi 1108176189 1184 PEITQLQ 1190
Cdd:cd03289 257 PQIQALQ 263
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
23-278 |
5.06e-23 |
|
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: 100.71 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 23 GFGAALAGTVIAVLVPLVTKRVIDDAIAADHR-PLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQALL 101
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLdVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 102 RWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRRLL 180
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDnLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 181 AAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFAL 260
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250
....*....|....*...
gi 1108176189 261 GGWMAAQGSITVGTFVAF 278
Cdd:cd18557 241 GGYLVLSGQLTVGELTSF 258
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
334-546 |
6.19e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 98.25 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVREL---TLDSLRSAI 410
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-TIGANIA------YGRPDATPEQIATAARAAHIEEFVNTLPDGyqtavgargltLSGGQRQRIALAR 483
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAfalevtGVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLrEAIADR--TAVIFTRRRSML-TLADRVAVLDSGRL 546
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAgtTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
347-557 |
6.33e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 98.77 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDS-LRSAIGLVPEDAVLFSG-TI 424
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANI---AYGRPDATPEQIATAarAAHIEEFvntlpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAV 501
Cdd:cd03218 93 EENIlavLEIRGLSKKEREEKL--EELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 502 D--AVIEcgIQEVLREAIADRTAVIFTRR--RSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:cd03218 165 DpiAVQD--IQKIIKILKDRGIGVLITDHnvRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
952-1159 |
6.38e-23 |
|
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: 98.37 E-value: 6.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG--CDLREFDVdGYRNRLgivtqeqyvf 1029
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGG-GFNPEL---------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 agTVRD-----AIAYGRPDATDAQVER---AAREVGAH---PMitaldngylhqvtaggRNLSAGQLQLLALARARLVDP 1098
Cdd:cd03220 100 --TGREniylnGRLLGLSRKEIDEKIDeiiEFSELGDFidlPV----------------KTYSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARRTTLI-VAHGL-AIAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPsSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
944-1166 |
6.91e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.06 E-value: 6.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYrTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFD-VDGYRNRLGIV 1022
Cdd:PRK13644 4 LENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 TQE-QYVFAG-TVRDAIAYG------RPDATDAQVERAAREVGAHPmitaldngYLHQvtaGGRNLSAGQLQLLALARAR 1094
Cdd:PRK13644 83 FQNpETQFVGrTVEEDLAFGpenlclPPIEIRKRVDRALAEIGLEK--------YRHR---SPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1095 LVDPDILLLDEATVALDPAT-EAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
341-544 |
9.25e-23 |
|
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: 97.79 E-value: 9.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 341 FGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAV----RIGGQDVRELTLDSLRSAIGLVPED 416
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 AVLFSGTIGANIAYGRPdATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDD 496
Cdd:cd03290 88 PWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 497 PTSAVDA-----VIECGIQEVLREaiADRTAVIFTRRRSMLTLADRVAVLDSG 544
Cdd:cd03290 167 PFSALDIhlsdhLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
964-1159 |
1.11e-22 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 97.56 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 964 LRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgyRNRLGIVTQEQYVFAG-TVRDAIAYGRP 1042
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1043 -----DATDAQ-VERAAREVGAHPMITALdngylhqvtagGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEA 1116
Cdd:cd03298 97 pglklTAEDRQaIEVALARVGLAGLEKRL-----------PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1108176189 1117 VVQRATLTLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:cd03298 166 EMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
348-566 |
1.13e-22 |
|
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: 99.55 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvreltldslrsaIGLVPEDAVLFSGTIGAN 427
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 428 IAYGRpDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIEC 507
Cdd:cd03291 118 IIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 508 GIQE-VLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYRELL 566
Cdd:cd03291 197 EIFEsCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
332-584 |
1.17e-22 |
|
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: 103.61 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFG-YVADRPVLREISLSVRAGETLAVVGAPGSGKSTLA----SLATRCYDVTQGAVRIGGQDVRELTLDSL 406
Cdd:COG4172 7 LSVEDLSVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 407 R----SAIGLV---------PedavLFsgTIGANIAygrpdatpEQIA-------TAARAAHIE--EFVNtLPDGyqtav 464
Cdd:COG4172 87 RrirgNRIAMIfqepmtslnP----LH--TIGKQIA--------EVLRlhrglsgAAARARALEllERVG-IPDP----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 465 gARGLT-----LSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR-TAVIF-------TRRrsm 531
Cdd:COG4172 147 -ERRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgMALLLithdlgvVRR--- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 532 ltLADRVAVLDSGRLLDVGTPDEVWERcPR--Y-RELLSPAPDLADDLVVAERSPV 584
Cdd:COG4172 223 --FADRVAVMRQGEIVEQGPTAELFAA-PQhpYtRKLLAAEPRGDPRPVPPDAPPL 275
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
944-1159 |
1.30e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.43 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRTR---EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREF----DVDGYR 1016
Cdd:PRK13649 5 LQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1017 NRLGIVTQ--EQYVFAGTVRDAIAYGRPD--ATDAQVERAAREVGAhpMITALDNGYlhqvtagGRN---LSAGQLQLLA 1089
Cdd:PRK13649 85 KKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLA--LVGISESLF-------EKNpfeLSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1090 LARARLVDPDILLLDEATVALDPATeavvQRATLTL-----AARRTTLIVAHGL-AIAEHADRIVVLEHGTVVEDG 1159
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKG----RKELMTLfkklhQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSG 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
338-555 |
1.49e-22 |
|
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: 97.89 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFGYVAdrpVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDsLRSAIGLV---- 413
Cdd:cd03219 7 TKRFGGLV---ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGrtfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 ---------PEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVgarglTLSGGQRQRIALARA 484
Cdd:cd03219 83 iprlfpeltVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAG-----ELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVehDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
959-1154 |
1.52e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.73 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyRNRLGIVTQEQYVFAGTVRDAIA 1038
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLREALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1039 YGRP--DATDAQVERAAREVGAHPMITALDngylhQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEA 1116
Cdd:COG4178 448 YPATaeAFSDAELREALEAVGLGHLAERLD-----EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
170 180 190
....*....|....*....|....*....|....*....
gi 1108176189 1117 VVqRATLTLAARRTTLI-VAHGLAIAEHADRIVVLEHGT 1154
Cdd:COG4178 523 AL-YQLLREELPGTTVIsVGHRSTLAAFHDRVLELTGDG 560
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
347-546 |
2.08e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.40 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGLVPED----AVLFS 421
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEDrkgeGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 422 GTIGANIAYGRPD--ATPEQIATAARAAHIEEFVNTL---PDGYQTAVGarglTLSGGQRQRIALARALLHQPRLLIMDD 496
Cdd:COG1129 345 LSIRENITLASLDrlSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 497 PTSAVD--AVIEcgIQEVLREAIADRTAVIFTrrrS-----MLTLADRVAVLDSGRL 546
Cdd:COG1129 421 PTRGIDvgAKAE--IYRLIRELAAEGKAVIVI---SselpeLLGLSDRILVMREGRI 472
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
334-555 |
2.10e-22 |
|
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: 97.85 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAV------RIGGQDVRELtldslR 407
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVWEL-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 408 SAIGLV-------------PEDAVL--FSGTIGAniaYGRPdaTPEQIATAARAAHieefvntlpdgyqtAVGARGL--- 469
Cdd:COG1119 78 KRIGLVspalqlrfprdetVLDVVLsgFFDSIGL---YREP--TDEQRERARELLE--------------LLGLAHLadr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 470 ---TLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAViecGIQEVLR--EAIADR--TAVIF-TRRRS-MLTLADRVAV 540
Cdd:COG1119 139 pfgTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLG---ARELLLAllDKLAAEgaPTLVLvTHHVEeIPPGITHVLL 215
|
250
....*....|....*
gi 1108176189 541 LDSGRLLDVGTPDEV 555
Cdd:COG1119 216 LKDGRVVAAGPKEEV 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-526 |
2.24e-22 |
|
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: 96.39 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLATrcydVTQGAVRIGGQDVRELTlDSLRSA 409
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLlrilAGLLP----PSAGEVLWNGEPIRDAR-EDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPEDAVLFSG-TIGANIAY----GRPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARA 484
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1108176189 485 LLHQPRLLIMDDPTSAVD-AVIECgIQEVLREAIADRTAVIFT 526
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDaAGVAL-LAELIAAHLARGGAVLLT 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-558 |
2.25e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.72 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYV-ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCY---DVTQGAVRIGGQDVRELTLDSLRSA 409
Cdd:PRK13640 6 VEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPE--DAVLFSGTIGANIAYG---RPDATPEQIATAARAAH---IEEFVNTLPDgyqtavgarglTLSGGQRQRIAL 481
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVLAdvgMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIF--TRRRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsiTHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
341-548 |
2.45e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 97.95 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 341 FGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDS---LRSAIGLVPED- 416
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 --AVLFSGTIGANIA-----YGRPDATPEQiataARAAHIEEFVNTLPDGYQTavgaRGLTLSGGQRQRIALARALLHQP 489
Cdd:TIGR02769 98 psAVNPRMTVRQIIGeplrhLTSLDESEQK----ARIAELLDMVGLRSEDADK----LPRQLSGGQLQRINIARALAVKP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 490 RLLIMDDPTSAVDAVIECGIQEVLREAIADR-TAVIFTRR--RSMLTLADRVAVLDSGRLLD 548
Cdd:TIGR02769 170 KLIVLDEAVSNLDMVLQAVILELLRKLQQAFgTAYLFITHdlRLVQSFCQRVAVMDKGQIVE 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
950-1159 |
2.50e-22 |
|
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: 96.52 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLreFDVDGYRNRLGIVTQEQYVF 1029
Cdd:cd03268 9 TYGKKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AG-TVRD-----AIAYGRPdatDAQVERAAREVGAHpmitaldnGYLHQVTaggRNLSAGQLQLLALARARLVDPDILLL 1103
Cdd:cd03268 85 PNlTAREnlrllARLLGIR---KKRIDEVLDVVGLK--------DSAKKKV---KGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-555 |
2.76e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.88 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLR-----------SAIGLVPEDAV 418
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 419 LFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 499 SAVDAVIECGIQEVL--REAIADRTAVIFTRR-RSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
344-555 |
3.11e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.49 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 344 VADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVL-FSG 422
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 T------IGAnIAYGRPDATPEQIATAARAAhieefvntlpdgyqtaVGARGL------TLSGGQRQRIALARAL--LHQ 488
Cdd:COG4559 91 TveevvaLGR-APHGSSAAQDRQIVREALAL----------------VGLAHLagrsyqTLSGGEQQRVQLARVLaqLWE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 489 -----PRLLIMDDPTSAVDaviecgI---QEVLREAiadRTaviFTRRRSM-------LTL----ADRVAVLDSGRLLDV 549
Cdd:COG4559 154 pvdggPRWLFLDEPTSALD------LahqHAVLRLA---RQ---LARRGGGvvavlhdLNLaaqyADRILLLHQGRLVAQ 221
|
....*.
gi 1108176189 550 GTPDEV 555
Cdd:COG4559 222 GTPEEV 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
695-1174 |
4.44e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.52 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 695 QVLFRLRSV----VFAHAQRLGLDAFEDDGDAQIVTAVTADVEAI--VAFLRTGLVVAVISVVTLVGILVALLAIRARL- 767
Cdd:PLN03232 367 RVGFRLRSTlvaaIFHKSLRLTHEARKNFASGKVTNMITTDANALqqIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 768 VLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLreyaAGLRIAQAFRAEyRGLQSYFAHSDDYRRLGVRGQRL 847
Cdd:PLN03232 447 SLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEIL----ASMDTVKCYAWE-KSFESRIQGIRNEELSWFRKAQL 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 848 LALYYPFVALLCSLATTLVLLdGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSL------ 921
Cdd:PLN03232 522 LSAFNSFILNSIPVVVTLVSF-GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseer 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 922 -LSTRTPSSPAARPVGTLRGEVVFDAvhysyrTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTV 1000
Cdd:PLN03232 601 iLAQNPPLQPGAPAISIKNGYFSWDS------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSS 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1001 RVdgcdlrefdvdgYRNRLGIVTQEQYVFAGTVRDAIAYGrpdaTDAQVERAAREVGAHPMITALD---NGYLHQVTAGG 1077
Cdd:PLN03232 675 VV------------IRGSVAYVPQVSWIFNATVRENILFG----SDFESERYWRAIDVTALQHDLDllpGRDLTEIGERG 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1078 RNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLAIAEHADRIVVLEHGTVV 1156
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKgKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
490
....*....|....*...
gi 1108176189 1157 EDGAHTELLAAGGHYSRL 1174
Cdd:PLN03232 819 EEGTFAELSKSGSLFKKL 836
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
959-1170 |
4.47e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 96.74 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDgcdlrEFDVDG-------------YRNRLGIVTQE 1025
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG-----DITIDTarslsqqkglirqLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1026 QYVFAG-TVRDAIAYG----RPDATDAQVERAaREVGAHPMITALDNGYlhqvtagGRNLSAGQLQLLALARARLVDPDI 1100
Cdd:PRK11264 94 FNLFPHrTVLENIIEGpvivKGEPKEEATARA-RELLAKVGLAGKETSY-------PRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1101 LLLDEATVALDPATEAVVQRATLTLAA-RRTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLAAGGH 1170
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
72-309 |
4.78e-22 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 98.41 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 72 LLTYVRRYYGGRIAHLVQHDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGV-AV 150
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIgAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 151 MTWLSVPLALLAVLLVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYA 230
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 231 AQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQG------SITVGTFVAFwacLTLLAR---PACDLAGMLTIAQQ 301
Cdd:cd18565 229 ANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTF---LFYTQRllwPLTRLGDLIDQYQR 305
|
....*...
gi 1108176189 302 ARAGAVRV 309
Cdd:cd18565 306 AMASAKRV 313
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
325-547 |
5.09e-22 |
|
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: 94.93 E-value: 5.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 325 PLSPEARLsLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLATRCYdvTQGAVRIGGQDVRe 400
Cdd:cd03213 1 GVTLSFRN-LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnalAGRRTGLG--VSGEVLINGRPLD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 401 ltLDSLRSAIGLVPEDAVLFsgtiganiaygrPDATPEQiaTAARAAHIeefvntlpdgyqtavgaRGltLSGGQRQRIA 480
Cdd:cd03213 77 --KRSFRKIIGYVPQDDILH------------PTLTVRE--TLMFAAKL-----------------RG--LSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDAVIECGIQEVLReAIAD--RTaVIFT---RRRSMLTLADRVAVLDSGRLL 547
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADtgRT-IICSihqPSSEIFELFDKLLLLSQGRVI 191
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
952-1159 |
5.17e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.69 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlR-----EFDVdGYRNRLgivtqeq 1026
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RvsallELGA-GFHPEL------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 yvfagTVRD-----AIAYG-RPDATDAQVERAAR--EVGAhpmitaldngYLHQ-VtaggRNLSAGQLQLLALARARLVD 1097
Cdd:COG1134 104 -----TGREniylnGRLLGlSRKEIDEKFDEIVEfaELGD----------FIDQpV----KTYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1098 PDILLLDEATVALDpatEAVVQRATLTLAAR----RTTLIVAHGL-AIAEHADRIVVLEHGTVVEDG 1159
Cdd:COG1134 165 PDILLVDEVLAVGD---AAFQKKCLARIRELresgRTVIFVSHSMgAVRRLCDRAIWLEKGRLVMDG 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
955-1159 |
5.24e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.81 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVD--GYRNRLGIVTQ--EQYVFA 1030
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRDAIAYG------RPDATDAQVERAAREVGahpmitaLD-NGYLHQVTAggrNLSAGQLQLLALARARLVDPDILLL 1103
Cdd:PRK13637 99 ETIEKDIAFGpinlglSEEEIENRVKRAMNIVG-------LDyEDYKDKSPF---ELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1104 DEATVALDPAT--EAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:PRK13637 169 DEPTAGLDPKGrdEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCELQG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
334-558 |
5.74e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.25 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslRSAIGLV 413
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAYG-RPDATPEQ-IAT----AARAAHIEEFVNTLPdgyqtavgargLTLSGGQRQRIALARALL 486
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlRMQKTPAAeITPrvmeALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLRE-----AIadrTAVIFTR-RRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKAlqrklGI---TFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
956-1156 |
7.35e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 93.65 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlREFDVDGYR--NRLGIvtqeqyvfaGTV 1033
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRdaRRAGI---------AMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 rdaiaygrpdatdaqveraarevgahpmitaldngylHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVALDPA 1113
Cdd:cd03216 81 -------------------------------------YQ-------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1108176189 1114 -TEAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHGTVV 1156
Cdd:cd03216 117 eVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
952-1166 |
7.77e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.09 E-value: 7.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQ---EQYV 1028
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpdNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 FAgTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGylhqvTAGGRNLSAGQLQLLALARARLVDPDILLLDEATV 1108
Cdd:PRK13642 96 GA-TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFK-----TREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1109 ALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
332-551 |
8.25e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 93.26 E-value: 8.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYVadrPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAI 410
Cdd:cd03216 1 LELRGITKRFGGV---KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVpedavlfsgtiganiaygrpdatpeqiataaraahieefvntlpdgYQtavgargltLSGGQRQRIALARALLHQPR 490
Cdd:cd03216 78 AMV----------------------------------------------YQ---------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 491 LLIMDDPTSA-----VDAVIecgiqEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSGRLldVGT 551
Cdd:cd03216 103 LLILDEPTAAltpaeVERLF-----KVIRRLRAQGVAVIFIshRLDEVFEIADRVTVLRDGRV--VGT 163
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
20-278 |
8.91e-22 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 97.08 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQ 98
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANgDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 99 ALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFdvpNVLRHVLT---LLLGVAVMT-----WLSVPLALLAVLLVPVIG 170
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVM---MLLRMLVRapiMLIGAIIMAfrinpKLALILLVAIPILALVVF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 171 LIAHRSRRLLAAAthcaQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLP 250
Cdd:cd18548 158 LIMKKAIPLFKKV----QKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIM 233
|
250 260
....*....|....*....|....*...
gi 1108176189 251 ALGQMAVFALGGWMAAQGSITVGTFVAF 278
Cdd:cd18548 234 NLAIVAILWFGGHLINAGSLQVGDLVAF 261
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
334-552 |
8.94e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.73 E-value: 8.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 ---PEDAVlFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPdgYQtavgargltLSGGQRQRIALARA 484
Cdd:PRK13647 85 fqdPDDQV-FSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPP--YH---------LSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTL--ADRVAVLDSGRLLDVGTP 552
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAewADQVIVLKEGRVLAEGDK 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-558 |
1.20e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.88 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 352 EISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGG---QDVRE-LTLDSLRSAIGLVPEDAVLFSG-TIGA 426
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYGRPDATPEQiataaRAAHIEEFVNTLpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIE 506
Cdd:TIGR02142 95 NLRYGMKRARPSE-----RRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 507 CGIQEVLREAIAD-RTAVIFTRR--RSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:TIGR02142 168 YEILPYLERLHAEfGIPILYVSHslQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
958-1159 |
1.28e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGtVRVDGC------DLREFDVD--GYRNRLGIVTQEQYVF 1029
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKvtfhgkNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AGTVRDAIAYG-RPDA----TDAQVERAAREvgahpmiTALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:PRK14243 104 PKSIYDNIAYGaRINGykgdMDELVERSLRQ-------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1105 EATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDG 1159
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-555 |
1.56e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSA-IGLVPED-----AVLf 420
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 421 SGTIGANIAYGRPDATP---------EQIATAARAAhIEEFvNTLPDGYQTAVGArgltLSGGQRQRIALARALLHQPRL 491
Cdd:COG3845 350 DMSVAENLILGRYRRPPfsrggfldrKAIRAFAEEL-IEEF-DVRTPGPDTPARS----LSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 492 LIMDDPTSAVD-AVIEcGIQEVLREAIADRTAVIFTrrrSM-----LTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:COG3845 424 LIAAQPTRGLDvGAIE-FIHQRLLELRDAGAAVLLI---SEdldeiLALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
349-572 |
1.64e-21 |
|
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: 96.08 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDvTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANI 428
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 429 -AYGRpdATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIEC 507
Cdd:cd03289 98 dPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 508 GIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYRELLSPAPDL 572
Cdd:cd03289 176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
959-1190 |
1.83e-21 |
|
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: 101.53 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDpTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAI- 1037
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLd 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYGRpdATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAV 1117
Cdd:TIGR01271 1314 PYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1118 VqRATLTLAARRTTLIVA-HGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYS---------RLWAAHTRLCS---- 1183
Cdd:TIGR01271 1392 I-RKTLKQSFSNCTVILSeHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKqamsaadrlKLFPLHRRNSSkrkp 1470
|
....*...
gi 1108176189 1184 -PEITQLQ 1190
Cdd:TIGR01271 1471 qPKITALR 1478
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
334-547 |
3.25e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.18 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLasLATRCYD--VTQGAVRIGGQDVREL-TLDSLRSAI 410
Cdd:PRK11614 6 LSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTL--LGTLCGDprATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-TIGANIAYGRPDATPEQIATaaraaHIEEFVNTLPDGYQTAVgARGLTLSGGQRQRIALARALLHQP 489
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQE-----RIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 490 RLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRS--MLTLADRVAVLDSGRLL 547
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVV 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
348-566 |
3.29e-21 |
|
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: 100.76 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvreltldslrsaIGLVPEDAVLFSGTIGAN 427
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 428 IAYGRpDATPEQIATAARAAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIEC 507
Cdd:TIGR01271 507 IIFGL-SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 508 GIQE-VLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERCPRYRELL 566
Cdd:TIGR01271 586 EIFEsCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
352-558 |
3.37e-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: 96.71 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 352 EISLSVRAGETLAVVGAPGSGKSTL----ASLATrcydVTQGAVRIGGQ----DVRELTLDSLRSAIGLVPEDAVLFSG- 422
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLlraiAGLER----PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TIGANIAYGRPDAtpeqiATAARAAHIEEFVNTLpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:COG4148 93 SVRGNLLYGRKRA-----PRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 503 AVIECGIQEVLrEAIADRTAV-IFTRRRSM---LTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:COG4148 166 LARKAEILPYL-ERLRDELDIpILYVSHSLdevARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
360-550 |
3.40e-21 |
|
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: 93.13 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 360 GETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQ---DVR-ELTLDSLRSAIGLVPEDAVLFSG-TIGANIAYGRPD 434
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPHlNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 435 ATPEQIATAAraahiEEFVNTLpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLR 514
Cdd:cd03297 103 KRNREDRISV-----DELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1108176189 515 EAIAD-RTAVIFTRR--RSMLTLADRVAVLDSGRLLDVG 550
Cdd:cd03297 176 QIKKNlNIPVIFVTHdlSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
957-1159 |
3.67e-21 |
|
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: 93.84 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLRefDVDGYRNRLGIVTQEQYVFAG-TVRD 1035
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1036 AIAYG------RPDATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVA 1109
Cdd:cd03300 92 NIAFGlrlkklPKAEIKERVAEALDLVQ----LEGYANRKPSQ-------LSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1110 LDpateaVVQRATLTLAARR-------TTLIVAH----GLAIaehADRIVVLEHGTVVEDG 1159
Cdd:cd03300 161 LD-----LKLRKDMQLELKRlqkelgiTFVFVTHdqeeALTM---SDRIAVMNKGKIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
931-1167 |
4.00e-21 |
|
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: 98.60 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 931 AARPVGTLR-----GEVVFDA----VHYSYR-------TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFyD 994
Cdd:COG4172 258 AAEPRGDPRpvppdAPPLLEArdlkVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-I 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 995 PTHGTVRVDGCDLREFDVDG---YRNRLGIVTQEQYvfaG------TVRDAIAYG----RPDATDAQ----VERAAREVG 1057
Cdd:COG4172 337 PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPF---GslsprmTVGQIIAEGlrvhGPGLSAAErrarVAEALEEVG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1058 AHPmitALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVALDpateAVVQRATLTLAARrttLIVAHG 1137
Cdd:COG4172 414 LDP---AARHRYPHE-------FSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDLLRD---LQREHG 476
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1108176189 1138 LA----------IAEHADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:COG4172 477 LAylfishdlavVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
20-278 |
4.19e-21 |
|
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: 94.63 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLVPLVTKRVIDDAI---AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDA 96
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpdgDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 97 FQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPN-VLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHR 175
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGlLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 176 SRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQM 255
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260
....*....|....*....|...
gi 1108176189 256 AVFALGGWMAAQGSITVGTFVAF 278
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAF 263
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
853-1172 |
4.47e-21 |
|
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: 100.41 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 853 PFVALLCSLATtLVLLDGAREVRAGVisvgALVTYLLYiELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRT--PSSP 930
Cdd:TIGR00957 551 PFLVALITFAV-YVTVDENNILDAEK----AFVSLALF-NILRFPLNILPMVISSIVQASVSLKRLRIFLSHEElePDSI 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 931 AARPVGTLRGEVVfdAVH---YSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdl 1007
Cdd:TIGR00957 625 ERRTIKPGEGNSI--TVHnatFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--- 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1008 refdvdgyrnRLGIVTQEQYVFAGTVRDAIAYGRPdaTDAQVERAAREVGAH-PMITALDNGYLHQVTAGGRNLSAGQLQ 1086
Cdd:TIGR00957 700 ----------SVAYVPQQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQ 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1087 LLALARARLVDPDILLLDEATVALDPAT-----EAVVqrATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAH 1161
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDAHVgkhifEHVI--GPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSY 845
|
330
....*....|.
gi 1108176189 1162 TELLAAGGHYS 1172
Cdd:TIGR00957 846 QELLQRDGAFA 856
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
969-1159 |
5.23e-21 |
|
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: 92.74 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 969 GQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLRE----FDVDGYRNRLGIVTQEQYVFAG-TVRDAIAYGRPD 1043
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1044 ATDAQVERAAREVGAHPMITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATL 1123
Cdd:cd03297 103 KRNREDRISVDELLDLLGLDHLLNRYPAQ-------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1108176189 1124 TLAAR--RTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:cd03297 176 QIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
354-546 |
6.41e-21 |
|
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: 92.56 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 354 SLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRelTLDSLRSAIGLVPEDAVLFSG-TIGANIAYGR 432
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 433 PDA---TPEQ---IATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIE 506
Cdd:cd03298 96 SPGlklTAEDrqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1108176189 507 CGIQEVLREAIADR--TAVIFTRRRS-MLTLADRVAVLDSGRL 546
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
952-1173 |
6.58e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 95.18 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD---LREFDVDGYRNRLGIVTQEQYv 1028
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDPY- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 faG------TVRDAIA-------YGRPDATDAQVERAAREVGAHPmitALDNGYLHQvtaggrnLSAGQLQLLALARARL 1095
Cdd:COG4608 106 --AslnprmTVGDIIAeplrihgLASKAERRERVAELLELVGLRP---EHADRYPHE-------FSGGQRQRIGIARALA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1096 VDPDILLLDEATVALDPATEAVV--------QRATLTLaarrttLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:COG4608 174 LNPKLIVCDEPVSALDVSIQAQVlnlledlqDELGLTY------LFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYA 247
|
....*...
gi 1108176189 1167 AGGH-YSR 1173
Cdd:COG4608 248 RPLHpYTQ 255
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
942-1168 |
7.60e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.66 E-value: 7.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTV-----RVDGCDLREFdvdgyR 1016
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1017 NRLGIVTQ---EQYVfAGTVRDAIAYGRPD---ATDAQVERAAREVGAHPMITALDngylHQVTAggrnLSAGQLQLLAL 1090
Cdd:PRK13648 83 KHIGIVFQnpdNQFV-GSIVKYDVAFGLENhavPYDEMHRRVSEALKQVDMLERAD----YEPNA----LSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1091 ARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVA--HGLAIAEHADRIVVLEHGTVVEDGAHTELLAAG 1168
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
344-555 |
7.98e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 344 VADRPVLREISLSVRAGETLAVVGAPGSGKSTLasLATRCYDVT--QGAVRIGGQDVRELTLDSLRSAIGLVPEDAVL-F 420
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL--LRALSGELSpdSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 421 SGTIGANIAYGRpdaTPEQIATAARAAHIEEfvntlpdgYQTAVGARGL------TLSGGQRQRIALARALL------HQ 488
Cdd:PRK13548 90 PFTVEEVVAMGR---APHGLSRAEDDALVAA--------ALAQVDLAHLagrdypQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 489 PRLLIMDDPTSAVDaviecgI---QEVLReaIADRtaviFTRRRSM--------LTLA----DRVAVLDSGRLLDVGTPD 553
Cdd:PRK13548 159 PRWLLLDEPTSALD------LahqHHVLR--LARQ----LAHERGLavivvlhdLNLAaryaDRIVLLHQGRLVADGTPA 226
|
..
gi 1108176189 554 EV 555
Cdd:PRK13548 227 EV 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
956-1164 |
8.04e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 8.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlREFDVDGYRN--RLGIVT--QEQYVFAG 1031
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDaqAAGIAIihQELNLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 -TVRDAIAYGRPDAT-----DAQVERAARE----VGAHpmitaLDngylhqVTAGGRNLSAGQLQLLALARARLVDPDIL 1101
Cdd:COG1129 94 lSVAENIFLGREPRRgglidWRAMRRRAREllarLGLD-----ID------PDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1102 LLDEATVALDPA-TE---AVVQRatltLAARRTTLI-VAHGLA-IAEHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:COG1129 163 ILDEPTASLTEReVErlfRIIRR----LKAQGVAIIyISHRLDeVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-557 |
8.27e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.37 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 343 YVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQ-----GAVRIGGQDVRELTLDSL--RSAIGLVPE 415
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIevRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 416 DAVLFSG-TIGANIAYG--------RPDATPEQIATA-ARAAHIEEFVNTLPDgYQTavgarglTLSGGQRQRIALARAL 485
Cdd:PRK14267 93 YPNPFPHlTIYDNVAIGvklnglvkSKKELDERVEWAlKKAALWDEVKDRLND-YPS-------NLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 486 LHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLT-LADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAArVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
945-1164 |
8.31e-21 |
|
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: 92.43 E-value: 8.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 945 DAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGIVTQ 1024
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQYVFAG-TVRDAIA-----YGRPDATDAqvERAAREVGAHPMITALDNgylhQVtaggRNLSAGQLQLLALARARLVDP 1098
Cdd:cd03265 81 DLSVDDElTGWENLYiharlYGVPGAERR--ERIDELLDFVGLLEAADR----LV----KTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTEL 1164
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
343-556 |
1.05e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 343 YVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDV-----TQGAVRIGGQDVRELTLDS--LRSAIGLVPE 415
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 416 DAVLFSGTIGANIAYG-------RPDATPEQIATAARAAHI-EEFVNTLPDgyqTAVGargltLSGGQRQRIALARALLH 487
Cdd:PRK14239 94 QPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIwDEVKDRLHD---SALG-----LSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTrrRSMLT---LADRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT--RSMQQasrISDRTGFFLDGDLIEYNDTKQMF 235
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
638-918 |
1.18e-20 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 93.70 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:cd18575 9 AAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 DDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQF----RRASnwty 793
Cdd:cd18575 89 TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFgrrvRRLS---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 794 RRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGARE 873
Cdd:cd18575 165 RASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1108176189 874 VRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18575 245 VLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
308-528 |
1.27e-20 |
|
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: 98.83 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 308 RVLELID-----SRPTlvDGTKPLSPEARLSLE---------------FQRVSFGYVAD-RPVLREISLSVRAGETLAVV 366
Cdd:TIGR01271 1174 RVFKFIDlpqeePRPS--GGGGKYQLSTVLVIEnphaqkcwpsggqmdVQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLL 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 367 GAPGSGKSTLASLATRCYDvTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANI-AYGRpdATPEQIATAAR 445
Cdd:TIGR01271 1252 GRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQ--WSDEEIWKVAE 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 446 AAHIEEFVNTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIF 525
Cdd:TIGR01271 1329 EVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
...
gi 1108176189 526 TRR 528
Cdd:TIGR01271 1409 EHR 1411
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
334-550 |
1.78e-20 |
|
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: 91.10 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGeTLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRElTLDSLRSAIGLV 413
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAY-----GRPDATPEqiataARAAHIEEFVNtLPDGYQTAVGArgltLSGGQRQRIALARALLH 487
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYiawlkGIPSKEVK-----ARVDEVLELVN-LGDRAKKKIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRS-MLTLADRVAVLDSGRLLDVG 550
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
637-898 |
1.94e-20 |
|
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: 92.71 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 637 QTCAGLLPPLLIRHGIDVGI--RRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLD 714
Cdd:pfam00664 11 SGAISPAFPLVLGRILDVLLpdGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 715 AFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYR 794
Cdd:pfam00664 91 FFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 795 RARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREV 874
Cdd:pfam00664 171 KEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLV 250
|
250 260
....*....|....*....|....
gi 1108176189 875 RAGVISVGALVTYLLYIELLYTPI 898
Cdd:pfam00664 251 ISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
963-1165 |
2.11e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.10 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 963 NLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFD----VDGYRNRLGIVTQEQYVFAG-TVRDAI 1037
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYGRPDATDAQVERAAREVGAHPMItALDNgYLHQVTaggRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAV 1117
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQV-GLEN-YAHSYP---DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1118 VQRATLTLAAR--RTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELL 1165
Cdd:PRK10070 203 MQDELVKLQAKhqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
334-551 |
2.68e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVS--FGYVadrPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAI 410
Cdd:COG1129 5 LEMRGISksFGGV---KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-TIGANIAYGRPDATPEQI---ATAARAAHI-EEF-VNTLPDgyqTAVGarglTLSGGQRQRIALARA 484
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRGGLIdwrAMRRRARELlARLgLDIDPD---TPVG----DLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 485 LLHQPRLLIMDDPTSA-----VDAVIecgiqEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSGRLldVGT 551
Cdd:COG1129 155 LSRDARVLILDEPTASltereVERLF-----RIIRRLKAQGVAIIYIshRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
303-552 |
3.04e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.41 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 303 RAGAVRVLEL---IDSRPTLVDGTKPLSPEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLasl 379
Cdd:COG4178 329 RATVDRLAGFeeaLEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 380 atrcydvtqgavriggqdvreltldsLRSAIGL---------VPEDA-VLF--------SGTIGANIAYGRP--DATPEQ 439
Cdd:COG4178 406 --------------------------LRAIAGLwpygsgriaRPAGArVLFlpqrpylpLGTLREALLYPATaeAFSDAE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 440 IATAARAAHIEEFVNTLpdgyqTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIAD 519
Cdd:COG4178 460 LREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG 534
|
250 260 270
....*....|....*....|....*....|....*.
gi 1108176189 520 RTAVIFTRRRSMLTLADRVAVLD---SGRLLDVGTP 552
Cdd:COG4178 535 TTVISVGHRSTLAAFHDRVLELTgdgSWQLLPAEAP 570
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
343-555 |
3.26e-20 |
|
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: 89.89 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 343 YVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRC--YDVTQGAVRIGGQDVRELTLDSlRSAIGLVpedavlf 420
Cdd:cd03217 9 SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGIF------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 421 sgtiganIAYGRPDATPEqiataaraAHIEEFVNTLPDGyqtavgargltLSGGQRQRIALARALLHQPRLLIMDDPTSA 500
Cdd:cd03217 81 -------LAFQYPPEIPG--------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 501 VD----AVIECGIQEVLREaiaDRTAVIFTRRRSMLTL--ADRVAVLDSGRLLDVGTPDEV 555
Cdd:cd03217 135 LDidalRLVAEVINKLREE---GKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSGDKELA 192
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
957-1170 |
3.65e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.08 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIP-AGQTVV--------------FVGSTGSGKSTLIKLVARFYDPTHG-----TVRVDGCDLREF-DVDGY 1015
Cdd:PRK14271 20 PAMAAVNLTLGfAGKTVLdqvsmgfparavtsLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1016 RNRLGIVTQEQYVFAGTVRDAIAYGRpdATDAQVERAAREVGAHPMIT--ALDNGYLHQVTAGGRNLSAGQLQLLALARA 1093
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGV--RAHKLVPRKEFRGVAQARLTevGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1094 RLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGGH 1170
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
338-555 |
5.59e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.87 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFGYVAdrpVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV------------------- 398
Cdd:COG0411 11 TKRFGGLV---AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriarlgiartfqn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 399 ----RELT-LDSLRSAiglvpedAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVgarglTLSG 473
Cdd:COG0411 88 prlfPELTvLENVLVA-------AHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAG-----NLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 474 GQRQRIALARALLHQPRLLIMDDPTSAVDAViEC-GIQEVLREAIADR-TAVIFT--RRRSMLTLADRVAVLDSGRLLDV 549
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPE-ETeELAELIRRLRDERgITILLIehDMDLVMGLADRIVVLDFGRVIAE 234
|
....*.
gi 1108176189 550 GTPDEV 555
Cdd:COG0411 235 GTPAEV 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
334-555 |
5.90e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGL 412
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 V---PEDAvlFSG-TIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALA 482
Cdd:PRK13644 82 VfqnPETQ--FVGrTVEEDLAFGpenlclPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 483 RALLHQPRLLIMDDPTSAVD-----AVIEcGIQEVLREAiadRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDpdsgiAVLE-RIKKLHEKG---KTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
956-1159 |
6.33e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.87 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGyRNRLGIV-----TQeqyVFA 1030
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIArtfqnPR---LFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 G-TVRDAIAYGRPDATDAQV-------------ERAAREVGAHpmitALD----NGYLHQVTAggrNLSAGQLQLLALAR 1092
Cdd:COG0411 93 ElTVLENVLVAAHARLGRGLlaallrlprarreEREARERAEE----LLErvglADRADEPAG---NLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1093 ARLVDPDILLLDEATVALDPA-TEAVVQRaTLTLAARR--TTLIVAHGL-AIAEHADRIVVLEHGTVVEDG 1159
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEeTEELAEL-IRRLRDERgiTILLIEHDMdLVMGLADRIVVLDFGRVIAEG 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
957-1165 |
6.81e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.52 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLrefdvdgYRNRlgiVTQEQ---YVFAG-- 1031
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-------FTNL---PPRERrvgFVFQHya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 -----TVRDAIAYG---RP---DATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDI 1100
Cdd:COG1118 86 lfphmTVAENIAFGlrvRPpskAEIRARVEELLELVQ----LEGLADRYPSQ-------LSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1101 LLLDEATVALDpateAVVqRATLtlaaRR-----------TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELL 1165
Cdd:COG1118 155 LLLDEPFGALD----AKV-RKEL----RRwlrrlhdelggTTVFVTHDQEEAlELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
340-568 |
7.26e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 90.63 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLaslaTRCYDV----TQGAVRIGGQDVR-------ELT------ 402
Cdd:COG4598 17 SFG---DLEVLKGVSLTARKGDVISIIGSSGSGKSTF----LRCINLletpDSGEIRVGGEEIRlkpdrdgELVpadrrq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 403 LDSLRSAIGLVPEDAVLFSG-TIGANI------AYGRPDAtpEQIATAARAAH---IEEFVNTLPDgyqtavgarglTLS 472
Cdd:COG4598 90 LQRIRTRLGMVFQSFNLWSHmTVLENVieapvhVLGRPKA--EAIERAEALLAkvgLADKRDAYPA-----------HLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 473 GGQRQRIALARALLHQPRLLIMDDPTSAVDAVIecgIQEVLR--EAIAD--RTAVIFTRRRSML-TLADRVAVLDSGRLL 547
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPEL---VGEVLKvmRDLAEegRTMLVVTHEMGFArDVSSHVVFLHQGRIE 233
|
250 260
....*....|....*....|...
gi 1108176189 548 DVGTPDEVWE--RCPRYRELLSP 568
Cdd:COG4598 234 EQGPPAEVFGnpKSERLRQFLSS 256
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
335-555 |
9.19e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 9.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGY-VADRPV--LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSA-- 409
Cdd:PRK11153 3 ELKNISKVFpQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 -IGLVPEDAVLFSG-TIGANIAYgrpdatPEQIATAARAaHIEEFVNTLPDgyqtAVGargLT---------LSGGQRQR 478
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNVAL------PLELAGTPKA-EIKARVTELLE----LVG---LSdkadrypaqLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 479 IALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREaIADR---TAVIFT------RRrsmltLADRVAVLDSGRLLDV 549
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKD-INRElglTIVLIThemdvvKR-----ICDRVAVIDAGRLVEQ 222
|
....*.
gi 1108176189 550 GTPDEV 555
Cdd:PRK11153 223 GTVSEV 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-582 |
1.05e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 343 YVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQ------DVRELTLDSLRSAIGLVPED 416
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 AVLFSG-TIGANIAYgrpdatPEQIATAARAAHIEEFVNT------LPDGYQTAVGARGLTLSGGQRQRIALARALLHQP 489
Cdd:PRK14246 99 PNPFPHlSIYDNIAY------PLKSHGIKEKREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 490 RLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRR-RSMLTLADRVAVLDSGRLLDVGTPDEVWErcpryrellSP 568
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIFT---------SP 243
|
250
....*....|....
gi 1108176189 569 APDLADDLVVAERS 582
Cdd:PRK14246 244 KNELTEKYVIGRIS 257
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-573 |
1.17e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.94 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRV--SFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTldslRSAI 410
Cdd:COG4152 1 MLELKGLtkRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-TIGANIAY-----GRPDATpeqiatAARAAH--IEEFvnTLPDGYQTAVGarglTLSGGQRQRIALA 482
Cdd:COG4152 74 GYLPEERGLYPKmKVGEQLVYlarlkGLSKAE------AKRRADewLERL--GLGDRANKKVE----ELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAV---IecgIQEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVnveL---LKDVIRELAAKGTTVIFSshQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
250
....*....|....*.
gi 1108176189 558 RCPRYRELLSPAPDLA 573
Cdd:COG4152 219 QFGRNTLRLEADGDAG 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-576 |
1.20e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.56 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRE---LTLDSLRSAIGLV---PEDAVLFSGTIGA 426
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVfqnPYGSLNPRKKVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAygrpdaTPEQIAT-------AARAAHIEEFVNTLPDGYQtavgaR-GLTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:PRK11308 114 ILE------EPLLINTslsaaerREKALAMMAKVGLRPEHYD-----RyPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 499 SAVDAVIECGI-------QEVLREA---IADRTAVIftrrrsmLTLADRVAVLDSGRLLDVGTPDEVWERcPRY---REL 565
Cdd:PRK11308 183 SALDVSVQAQVlnlmmdlQQELGLSyvfISHDLSVV-------EHIADEVMVMYLGRCVEKGTKEQIFNN-PRHpytQAL 254
|
250
....*....|.
gi 1108176189 566 LSPAPDLADDL 576
Cdd:PRK11308 255 LSATPRLNPDD 265
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
349-554 |
1.33e-19 |
|
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: 89.03 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDS---LRSA-IG-------LVPeda 417
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarLRARhVGfvfqsfqLLP--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 418 vlfsgTIGA--NIAY-----GRPDAtpeqiatAARAAHIEEFVntlpdgyqtAVGARgLT-----LSGGQRQRIALARAL 485
Cdd:COG4181 104 -----TLTAleNVMLplelaGRRDA-------RARARALLERV---------GLGHR-LDhypaqLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 486 LHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDE 554
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
957-1150 |
1.45e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyRNRLGIVTQEQYV---FAGTV 1033
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 RDAIAYG---------RPDATD-AQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLL 1103
Cdd:NF040873 75 RDLVAMGrwarrglwrRLTRDDrAAVDDALERVG----LADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLAIAEHADRIVVL 1150
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
353-571 |
1.48e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 91.31 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSL---RSAIGLVPEDAvLFS----GTIG 425
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASlnprMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 426 ANIA-----YgRPDATPEQI-----ATAARAAHIEEFVNTLPDGYqtavgargltlSGGQRQRIALARALLHQPRLLIMD 495
Cdd:PRK15079 119 EIIAeplrtY-HPKLSRQEVkdrvkAMMLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 496 DPTSAVDAVIECGI----QEVLREA------IADRTAVIftrrrsmLTLADRVAVLDSGRLLDVGTPDEVWE--RCPRYR 563
Cdd:PRK15079 187 EPVSALDVSIQAQVvnllQQLQREMglslifIAHDLAVV-------KHISDRVLVMYLGHAVELGTYDEVYHnpLHPYTK 259
|
250
....*....|
gi 1108176189 564 ELLS--PAPD 571
Cdd:PRK15079 260 ALMSavPIPD 269
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
334-586 |
1.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRP----VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV----RELTLDS 405
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 406 LRSAIGLV---PEDAvLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAvgarGLTLSGGQRQRIALA 482
Cdd:PRK13643 82 VRKKVGVVfqfPESQ-LFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKS----PFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVLrEAI--ADRTAVIFTR-RRSMLTLADRVAVLDSGRLLDVGTPDEVWERC 559
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIhqSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQEV 235
|
250 260 270
....*....|....*....|....*....|....*
gi 1108176189 560 P--RYRELLSP-APDLADDL-----VVAERSPVCR 586
Cdd:PRK13643 236 DflKAHELGVPkATHFADQLqktgaVTFEKLPITR 270
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-558 |
1.86e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.44 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLATrcydVTQGAVRIGGQDVRELTldslrs 408
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmvAGLER----ITSGEIWIGGRVVNELE------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 409 aiglvPED---AVLFSG-------TIGANIAYG---R--PDATPEQ-IATAARAAHIEEFVNTLPDgyqtavgarglTLS 472
Cdd:PRK11650 73 -----PADrdiAMVFQNyalyphmSVRENMAYGlkiRgmPKAEIEErVAEAARILELEPLLDRKPR-----------ELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 473 GGQRQRIALARALLHQPRLLIMDDPTSAVDAV------IEcgIQEVLREAIAdrTAVIFTRRR--SMlTLADRVAVLDSG 544
Cdd:PRK11650 137 GGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlrvqmrLE--IQRLHRRLKT--TSLYVTHDQveAM-TLADRVVVMNGG 211
|
250
....*....|....
gi 1108176189 545 RLLDVGTPDEVWER 558
Cdd:PRK11650 212 VAEQIGTPVEVYEK 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
959-1168 |
2.07e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAG-TVRDAI 1037
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYGRP----------DATDAQVERAAREVGahpmITALDNgylHQVTAggrnLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:PRK11231 98 AYGRSpwlslwgrlsAEDNARVNQAMEQTR----INHLAD---RRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1108 VALDPATEAVVQRATLTLAAR-RTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLAAG 1168
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
947-1174 |
2.10e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREF-DVDG----------- 1014
Cdd:PRK10619 11 LHKRYGEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrDKDGqlkvadknqlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1015 -YRNRLGIVTQE------QYVFAGTVRDAIAYGRPDATDAQvERAARevgahpmitaldngYLHQVTAGGR-------NL 1080
Cdd:PRK10619 89 lLRTRLTMVFQHfnlwshMTVLENVMEAPIQVLGLSKQEAR-ERAVK--------------YLAKVGIDERaqgkypvHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1081 SAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLAIAEHADRIVVLEHGTVVEDG 1159
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250
....*....|....*
gi 1108176189 1160 AHTELLAAGGHYSRL 1174
Cdd:PRK10619 234 GAPEQLFGNPQSPRL 248
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
332-555 |
2.69e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.72 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYVADRP----VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV--RELTLDS 405
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 406 LRSAIGLV---PEDAvLFSGTIGANIAYG--RPDATPEQIATAARAAhieefVNTLPDGYQTAVGARGLTLSGGQRQRIA 480
Cdd:PRK13637 81 IRKKVGLVfqyPEYQ-LFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSM---LTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMedvAKLADRIIVMNKGKCELQGTPREV 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
955-1174 |
2.72e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 94.42 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVdgcdlrefdvdgYRNRLGIVTQEQYVFAGTVR 1034
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1035 DAIAYGRP-DAtdAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDpa 1113
Cdd:PLN03130 697 DNILFGSPfDP--ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD-- 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1114 teAVVQRATLTLAARR-----TTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRL 1174
Cdd:PLN03130 773 --AHVGRQVFDKCIKDelrgkTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
334-550 |
3.18e-19 |
|
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: 87.34 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTldslRSAIGLV 413
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAY-GR-PDATPEQIATAAR----AAHIEEFVNTlpdgyqtavgaRGLTLSGGQRQRIALARALL 486
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYlAQlKGLKKEEARRRIDewleRLELSEYANK-----------RVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLT--LADRVAVLDSGRLLDVG 550
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVeeLCDRVLLLNKGRAVLYG 210
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
957-1165 |
3.32e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 88.71 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---YRNRLGIVTQEQYVFAG-- 1031
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDSPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 -TVRDAIA-----YGRPDATdAQVERAA---REVGahpmitaLDNGYLHQVTaggRNLSAGQLQLLALARARLVDPDILL 1102
Cdd:TIGR02769 105 mTVRQIIGeplrhLTSLDES-EQKARIAellDMVG-------LRSEDADKLP---RQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1103 LDEATVALDPATEAVVQRATLTLAARRTT--LIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELL 1165
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
352-554 |
3.35e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.89 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 352 EISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVreltldsLRSAIGLVP-----EDAVLFSG-TIG 425
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-------TALPPAERPvsmlfQENNLFPHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 426 ANIAYG-RPDA--TPEQ---IATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPTS 499
Cdd:COG3840 90 QNIGLGlRPGLklTAEQraqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 500 AVDAVIECGIQEVLREAIADRTAVIFtrrrsMLT--------LADRVAVLDSGRLLDVGTPDE 554
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVL-----MVThdpedaarIADRVLLVADGRIAADGPTAA 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
947-1150 |
3.48e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgyrnRlGIVTQEQ 1026
Cdd:COG4525 11 VRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD----R-GVVFQKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 YVFAG-TVRDAIAYGrpdATDAQVERAAREVGAHPMITALDngyLHQvtAGGRN---LSAGQLQLLALARARLVDPDILL 1102
Cdd:COG4525 86 ALLPWlNVLDNVAFG---LRLRGVPKAERRARAEELLALVG---LAD--FARRRiwqLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1103 LDEATVALDPATEAVVQRATLTLAAR--RTTLIVAHGlaIAEH---ADRIVVL 1150
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHS--VEEAlflATRLVVM 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
343-539 |
3.61e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.69 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 343 YVADRPVLREISLSVRAGETLAVVGAPGSGKSTLaslaTRCYDVT---------QGAVRIGGQDVRELTLD--SLRSAIG 411
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTI----LRCFNRLndlipgfrvEGKVTFHGKNLYAPDVDpvEVRRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSGTIGANIAYG-RPDA----TPEQIATAARAAhieefvnTLPDGYQTAVGARGLTLSGGQRQRIALARALL 486
Cdd:PRK14243 95 MVFQKPNPFPKSIYDNIAYGaRINGykgdMDELVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRrsmLTLADRVA 539
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHN---MQQAARVS 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
952-1174 |
3.78e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.76 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD--LREFDvdgYRNRLGIV----TQ- 1024
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfKRRKE---FARRIGVVfgqrSQl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 -------EQYVFAGTVrdaiaYGRPdatDAQVERAAREvgahpMITALD-NGYLHQVTaggRNLSAGQLQLLALARARLV 1096
Cdd:COG4586 108 wwdlpaiDSFRLLKAI-----YRIP---DAEYKKRLDE-----LVELLDlGELLDTPV---RQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1097 DPDILLLDEATVALDpateAVVQRATLTL-----AARRTTLIVA-HGLA-IAEHADRIVVLEHGTVVEDGAHTELLAAGG 1169
Cdd:COG4586 172 RPKILFLDEPTIGLD----VVSKEAIREFlkeynRERGTTILLTsHDMDdIEALCDRVIVIDHGRIIYDGSLEELKERFG 247
|
....*
gi 1108176189 1170 HYSRL 1174
Cdd:COG4586 248 PYKTI 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
942-1165 |
5.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTRE---VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL----REFDVDG 1014
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1015 YRNRLGIVTQ--EQYVFAGTVRDAIAYGrPDATDAQVERAAREVGAHPMITALDNGYLHQVTAggrNLSAGQLQLLALAR 1092
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPF---ELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1093 ARLVDPDILLLDEATVALDPATEAVVQRATLTL-AARRTTLIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTELL 1165
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-556 |
7.80e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.23 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPV--LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPE--DAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTLpdGYQTAVGARgltLSGGQRQRIALARALLHQP 489
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPAR---LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 490 RLLIMDDPTSAVDAVIECGIQEVLREaIADR---TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
334-566 |
8.71e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.83 E-value: 8.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVR--ELTLDSLRSAIG 411
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LV---PEDAvLFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALA 482
Cdd:PRK13639 82 IVfqnPDDQ-LFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVL----REAIadrTAVIFTRRRSMLTL-ADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLydlnKEGI---TIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
250
....*....|....*....
gi 1108176189 558 ----------RCPRYRELL 566
Cdd:PRK13639 227 dietirkanlRLPRVAHLI 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
349-567 |
8.80e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.11 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLaslaTRCYDV----TQGAVRIGgqdvrELTLDS-------------LRSAIG 411
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTL----LRCINLleqpEAGTIRVG-----DITIDTarslsqqkglirqLRQHVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSG-TIGANIAYGrpdatPEQIATAARAAHIEEFVNTLP----DGYQTAVGARgltLSGGQRQRIALARALL 486
Cdd:PRK11264 89 FVFQNFNLFPHrTVLENIIEG-----PVIVKGEPKEEATARARELLAkvglAGKETSYPRR---LSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIecgIQEVLR--EAIAD--RTAVIFTRRRSML-TLADRVAVLDSGRLLDVGTPDEVWE--RC 559
Cdd:PRK11264 161 MRPEVILFDEPTSALDPEL---VGEVLNtiRQLAQekRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFAdpQQ 237
|
....*...
gi 1108176189 560 PRYRELLS 567
Cdd:PRK11264 238 PRTRQFLE 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
959-1160 |
1.23e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfdVDGYRNRLGIVTQEQYVFAG-TVRDAI 1037
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYG--------RPDAtdAQVERAAREVGAHPMITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVA 1109
Cdd:PRK10851 96 AFGltvlprreRPNA--AAIKAKVTQLLEMVQLAHLADRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1110 LDPATEAVVQRATLTLAA--RRTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGA 1160
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAmEVADRVVVMSQGNIEQAGT 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-555 |
1.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.77 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRP----VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQ----DVRELTLDS 405
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 406 LRSAIGLV---PEdAVLFSGTIGANIAYGRPD-ATPEQIATAaRAAHIEEFVntlpdGYQTAVGARG-LTLSGGQRQRIA 480
Cdd:PRK13634 83 LRKKVGIVfqfPE-HQLFEETVEKDICFGPMNfGVSEEDAKQ-KAREMIELV-----GLPEELLARSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDAViecGIQEVL-------REaiADRTAVIFTrrRSM---LTLADRVAVLDSGRLLDVG 550
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPK---GRKEMMemfyklhKE--KGLTTVLVT--HSMedaARYADQIVVMHKGTVFLQG 228
|
....*
gi 1108176189 551 TPDEV 555
Cdd:PRK13634 229 TPREI 233
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
955-1141 |
1.61e-18 |
|
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: 84.78 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLrEFDVDG---YRNRLGIVTQ--EQYVF 1029
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGlleRRQRVGLVFQdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AGTVRDAIAYGRPD--ATDAQVERAAREVgahpmITALD-NGYLHQVTaggRNLSAGQLQLLALARARLVDPDILLLDEA 1106
Cdd:TIGR01166 83 AADVDQDVAFGPLNlgLSEAEVERRVREA-----LTAVGaSGLRERPT---HCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1108176189 1107 TVALDPATEAVVQRATLTLAARRTTLIVA-HGLAIA 1141
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVIStHDVDLA 190
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
352-550 |
1.68e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 85.30 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 352 EISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVreLTLDSLRSAIGLVPEDAVLFSG-TIGANIAY 430
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHlTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 431 G-RPD-----ATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAV 504
Cdd:TIGR01277 94 GlHPGlklnaEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1108176189 505 IECGIQEVLREAIA--DRTAVIFTRRRS-MLTLADRVAVLDSGRLLDVG 550
Cdd:TIGR01277 163 LREEMLALVKQLCSerQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
341-548 |
1.69e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 341 FGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAIGLVPED- 416
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 --AVLFSGTIGANIAygRPDATPEQIATAARAAHIEEFVNT--LPDGYQTAVGARgltLSGGQRQRIALARALLHQPRLL 492
Cdd:PRK10419 99 isAVNPRKTVREIIR--EPLRHLLSLDKAERLARASEMLRAvdLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREAIADR-TAVIFTRR--RSMLTLADRVAVLDSGRLLD 548
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFgTACLFITHdlRLVERFCQRVMVMDNGQIVE 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
334-565 |
1.84e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.07 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVAD-----RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVREL-TLDSLR 407
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 408 SAIGLVPE--DAVLFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRI 479
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDAViecGIQEVLR--EAIADR---TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDE 554
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPS---GRREVVNtiKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
250
....*....|.
gi 1108176189 555 VWERCPRYREL 565
Cdd:PRK13633 231 IFKEVEMMKKI 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-486 |
2.24e-18 |
|
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: 90.24 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 20 LLLGFGAALAGTVIAVLvplvtkrvIDDAIAADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMDAFQA 99
Cdd:COG4615 19 LLLGLLSGLANAGLIAL--------INQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 100 LLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRRL 179
Cdd:COG4615 91 ILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 180 LAAATHCAQEHKAAVTGVVDAAVCGIRVVKaFGQEERETVklvtASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFA 259
Cdd:COG4615 171 ARRHLRRAREAEDRLFKHFRALLEGFKELK-LNRRRRRAF----FDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 260 LGG----WMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV----LELIDSRPTLVDGTKPLSPEAR 331
Cdd:COG4615 246 LIGlilfLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIeeleLALAAAEPAAADAAAPPAPADF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYVADRP----VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLR 407
Cdd:COG4615 326 QTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 408 SAIGLVPEDAVLFSGTIGaniayGRPDATPEQIATAARAAHIEEfvntlpdgyQTAVGARGLT---LSGGQRQRIALARA 484
Cdd:COG4615 406 QLFSAVFSDFHLFDRLLG-----LDGEADPARARELLERLELDH---------KVSVEDGRFSttdLSQGQRKRLALLVA 471
|
..
gi 1108176189 485 LL 486
Cdd:COG4615 472 LL 473
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
349-569 |
2.36e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLaslaTRCYDV----TQGAVRIGGQDVREL-------------TLDSLRSAIG 411
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTF----LRCINFlekpSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSG-TIGANIAygrpdATPEQIATAARAAHIEEFVNtlpdgYQTAVG----ARG---LTLSGGQRQRIALAR 483
Cdd:PRK10619 96 MVFQHFNLWSHmTVLENVM-----EAPIQVLGLSKQEARERAVK-----YLAKVGiderAQGkypVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIecgIQEVLR--EAIAD--RTAVIFTRRRSMLT-LADRVAVLDSGRLLDVGTPDEVW-- 556
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPEL---VGEVLRimQQLAEegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFgn 242
|
250
....*....|...
gi 1108176189 557 ERCPRYRELLSPA 569
Cdd:PRK10619 243 PQSPRLQQFLKGS 255
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
334-558 |
2.59e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVAD--RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:PRK13650 5 IEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LV---PEDAvlFSG-TIGANIAYGRPDATPEQIATAARAAHIEEFVNTLpdGYQTAVGARgltLSGGQRQRIALARALLH 487
Cdd:PRK13650 85 MVfqnPDNQ--FVGaTVEDDVAFGLENKGIPHEEMKERVNEALELVGMQ--DFKEREPAR---LSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 488 QPRLLIMDDPTSAVDAViecGIQEVLR--EAIADR---TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PRK13650 158 RPKIIILDEATSMLDPE---GRLELIKtiKGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-562 |
2.72e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.73 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDV-----TQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:PRK14247 10 KVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 V---PEDAVLFSgtIGANIAYGrpdatPEQIATAARAAHIEEFVN------TLPDGYQTAVGARGLTLSGGQRQRIALAR 483
Cdd:PRK14247 87 VfqiPNPIPNLS--IFENVALG-----LKLNRLVKSKKELQERVRwalekaQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLT-LADRVAVLDSGRLLDVGTPDEVWERcPRY 562
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAArISDYVAFLYKGQIVEWGPTREVFTN-PRH 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
952-1159 |
2.76e-18 |
|
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: 84.64 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 952 RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlREFDVDGyRNRLGIV--------- 1022
Cdd:cd03269 9 RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGYLpeerglypk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 --TQEQYVFAGTVRDaiaYGRPDATdAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDI 1100
Cdd:cd03269 85 mkVIDQLVYLAQLKG---LKKEEAR-RRIDEWLERLE----LSEYANKRVEE-------LSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1101 LLLDEATVALDPATEAVVQRATLTLAARRTTLI-VAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
339-555 |
2.84e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 339 VSFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAV 418
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 419 L-FSGTIGANIAYGR-PDATPEQIATAARAAHIEEFVNTlpdGYQTAVGARGLT-LSGGQRQRIALARALLHQPRLLIMD 495
Cdd:PRK09536 88 LsFEFDVRQVVEMGRtPHRSRFDTWTETDRAAVERAMER---TGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 496 DPTSAVDAVIECGIQEVLREAIAD-RTAVIFTRRrsmLTLA----DRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDgKTAVAAIHD---LDLAarycDELVLLADGRVRAAGPPADV 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
947-1164 |
2.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.29 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSY----RTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD-LREFDVDGYRNRLGI 1021
Cdd:PRK13633 10 VSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtSDEENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQ---EQYVfAGTVRDAIAYG------RPDATDAQVERAAREVGA-----HPMitaldngylHQvtaggrnLSAGQLQL 1087
Cdd:PRK13633 90 VFQnpdNQIV-ATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMyeyrrHAP---------HL-------LSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1088 LALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
325-546 |
3.25e-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: 84.89 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 325 PLSPEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLd 404
Cdd:cd03220 13 YKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 405 slrsAIGLVPE----DAVLFSGTIganiaYGRpdaTPEQIatAARAAHIEEFvNTLPDGYQTAVGarglTLSGGQRQRIA 480
Cdd:cd03220 92 ----GGGFNPEltgrENIYLNGRL-----LGL---SRKEI--DEKIDEIIEF-SELGDFIDLPVK----TYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDA--VIECgiQEVLREAIADRTAVIFTR--RRSMLTLADRVAVLDSGRL 546
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAafQEKC--QRRLRELLKQGKTVILVShdPSSIKRLCDRALVLEKGKI 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
963-1166 |
4.07e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 963 NLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgyRNRLGIVTQEQYVFAG-TVRDAIAYG- 1040
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1041 RP-----DATDAQVERAAREVGAHPMITALDngylHQvtaggrnLSAGQLQLLALARARLVDPDILLLDEATVALDPA-- 1113
Cdd:PRK10771 97 NPglklnAAQREKLHAIARQMGIEDLLARLP----GQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALDPAlr 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1114 ------TEAVVQRATLTLaarrttLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK10771 166 qemltlVSQVCQERQLTL------LMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
332-558 |
4.62e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.95 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYVA----DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT----L 403
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 404 DSLRSAIGLV---PEDAvLFSGTIGANIAYGRPD--ATPEQIATAARAAHI-----EEFVNTLPdgyqtavgargLTLSG 473
Cdd:PRK13649 81 KQIRKKVGLVfqfPESQ-LFEETVLKDVAFGPQNfgVSQEEAEALAREKLAlvgisESLFEKNP-----------FELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 474 GQRQRIALARALLHQPRLLIMDDPTSAVD------------AVIECGIQEVLREAIADRTAviftrrrsmlTLADRVAVL 541
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDpkgrkelmtlfkKLHQSGMTIVLVTHLMDDVA----------NYADFVYVL 218
|
250
....*....|....*..
gi 1108176189 542 DSGRLLDVGTPDEVWER 558
Cdd:PRK13649 219 EKGKLVLSGKPKDIFQD 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
959-1166 |
4.69e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVtqeQYVFAG------- 1031
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDI---QMVFQDsisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 --TVRDAIAYGRPDATDaqVERAAREVGAHPMITA--LDNGYLHQVTAggrNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:PRK10419 105 rkTVREIIREPLRHLLS--LDKAERLARASEMLRAvdLDDSVLDKRPP---QLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1108 VALDPATEAVVQRATLTLAARRTT--LIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
953-1154 |
4.85e-18 |
|
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: 84.30 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 953 TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG--CDLREFDVDGYRNRLGI--VTQEQYV 1028
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknESEPSFEATRSRNRYSVayAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 FAGTVRDAIAYGRPdaTDAQVERAAREVGA-HPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:cd03290 91 LNATVEENITFGSP--FNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1108 VALD-PATEAVVQRATLTLAA--RRTTLIVAHGLAIAEHADRIVVLEHGT 1154
Cdd:cd03290 169 SALDiHLSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
348-547 |
4.90e-18 |
|
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: 84.69 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTlDSLRSAIGLV------------PE 415
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR-KKFLRRIGVVfgqktqlwwdlpVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 416 DAVLFSGTIganiaYGRPDAT-PEQIATAARAAHIEEFVNTlpdgyqtavGARGLTLsgGQRQRIALARALLHQPRLLIM 494
Cdd:cd03267 114 DSFYLLAAI-----YDLPPARfKKRLDELSELLDLEELLDT---------PVRQLSL--GQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 495 DDPTSAVDAVIECGIQEVLREAIADR-TAVIFTRR--RSMLTLADRVAVLDSGRLL 547
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERgTTVLLTSHymKDIEALARRVLVIDKGRLL 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
348-545 |
5.36e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 84.41 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRI--GGQDV-------RELtLDSLRSAIGLV----- 413
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaqaspREI-LALRRRTIGYVsqflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 --P----EDAVlfsgtIGANIAYGRPDATPEqiataARAAHIEEFVNtLPDGYQTAVGArglTLSGGQRQRIALARALLH 487
Cdd:COG4778 104 viPrvsaLDVV-----AEPLLERGVDREEAR-----ARARELLARLN-LPERLWDLPPA---TFSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 488 QPRLLIMDDPTSAVDA-----VIecgiqEVLREAIADRTAV--IFTRRRSMLTLADRVAVLDSGR 545
Cdd:COG4778 170 DPPLLLLDEPTASLDAanravVV-----ELIEEAKARGTAIigIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
955-1170 |
6.31e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.96 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYD-----PTHGTVRVDGCDLREFDVDGYRNRLGIVTQ-EQYV 1028
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 FAGTVRDAIAYG----RPDATDAQVERAAREvgahpmitALDNGYL-----HQVTAGGRNLSAGQLQLLALARARLVDPD 1099
Cdd:PRK14247 95 PNLSIFENVALGlklnRLVKSKKELQERVRW--------ALEKAQLwdevkDRLDAPAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1100 ILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGGH 1170
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-556 |
8.78e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFGYVADRpVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDV-----TQGAVRIGGQDV--RELTLDS 405
Cdd:PRK14258 7 AIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 406 LRSAIGLVPEDAVLFSGTIGANIAYG------RPDATPEQIATAA-RAAHieefvntLPDGYQTAVGARGLTLSGGQRQR 478
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 479 IALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAI--ADRTAVIFTRRRSMLT-LADRVAVLDS-----GRLLDVG 550
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrLSDFTAFFKGnenriGQLVEFG 238
|
....*.
gi 1108176189 551 TPDEVW 556
Cdd:PRK14258 239 LTKKIF 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
327-567 |
9.36e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 327 SPEARLSLEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdVRELtldsL 406
Cdd:COG1134 19 EPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL----L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 407 RSAIGLVPE----DAVLFSGTIganiaYGrpdATPEQIatAARAAHIEEFVNtLPDGYQTAVGarglTLSGGQRQRIALA 482
Cdd:COG1134 94 ELGAGFHPEltgrENIYLNGRL-----LG---LSRKEI--DEKFDEIVEFAE-LGDFIDQPVK----TYSSGMRARLAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAV--IECgiQEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSGRLLDVGTPDEVwer 558
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDAAfqKKC--LARIRELRESGRTVIFVshSMGAVRRLCDRAIWLEKGRLVMDGDPEEV--- 233
|
....*....
gi 1108176189 559 CPRYRELLS 567
Cdd:COG1134 234 IAAYEALLA 242
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
957-1136 |
1.08e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.37 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlreFDVDGYRNRLGIVTQEQYVFA-GTVRD 1035
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQNEGLLPwRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1036 AIAYGrpdATDAQVERAAREVGAHPMITALDngylhQVTAGGR---NLSAGQLQLLALARARLVDPDILLLDEATVALDP 1112
Cdd:PRK11248 90 NVAFG---LQLAGVEKMQRLEIAHQMLKKVG-----LEGAEKRyiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*.
gi 1108176189 1113 ATEAVVQRATLTLAAR--RTTLIVAH 1136
Cdd:PRK11248 162 FTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
334-557 |
1.13e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRP-VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGL 412
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 V---PEDAvlFSGTIGA-NIAYGRPD-ATP-----EQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALA 482
Cdd:PRK13648 88 VfqnPDNQ--FVGSIVKyDVAFGLENhAVPydemhRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWE 557
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
334-558 |
1.31e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 ---PEDAVlFSGTIGANIAYG------RPDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARA 484
Cdd:PRK13652 84 fqnPDDQI-FSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAViecGIQEVLR--EAIADR--TAVIFTRRRSML--TLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQ---GVKELIDflNDLPETygMTVIFSTHQLDLvpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
334-542 |
1.71e-17 |
|
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: 81.05 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLaslatrcydvtqgavriggqdvreltldsLRSAIGLV 413
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL-----------------------------FRALAGLW 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PedavLFSGTI----GANIAY--GRPDATP----EQIAtaaraahieefvntlpdgYqtavgARGLTLSGGQRQRIALAR 483
Cdd:cd03223 52 P----WGSGRIgmpeGEDLLFlpQRPYLPLgtlrEQLI------------------Y-----PWDDVLSGGEQQRLAFAR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAiadRTAVIF-TRRRSMLTLADRVAVLD 542
Cdd:cd03223 105 LLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISvGHRPSLWKFHDRVLDLD 161
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
346-550 |
2.53e-17 |
|
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: 81.88 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-----LDSLRSAIGLVP----ED 416
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIealrrIGALIEAPGFYPnltaRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 AVLFSGTIganiaYGRPDATpeqiataaraahIEEFVNTLpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDD 496
Cdd:cd03268 92 NLRLLARL-----LGIRKKR------------IDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 497 PTSAVDAViecGIQEvLREAIAD-----RTAVIFTRRRS-MLTLADRVAVLDSGRLLDVG 550
Cdd:cd03268 153 PTNGLDPD---GIKE-LRELILSlrdqgITVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
642-918 |
2.58e-17 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 84.01 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 642 LLPPLLIRHGIDVGIRRHVLSALWWAALAGTAT-------VVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLD 714
Cdd:cd18554 16 LLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIgimffifLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 715 AFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQF-RRASNWTY 793
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFfGRLRKLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 794 RRARhRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGARE 873
Cdd:cd18554 176 ERSQ-ALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYL 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1108176189 874 VRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18554 255 VIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
948-1181 |
3.50e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 84.25 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 948 HYSYR------TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---YRNR 1018
Cdd:PRK11308 14 HYPVKrglfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LGIVTQEQYvfaGTV--RDAIAY--GRPDATDAQVERAAREVGAHPMITALD------NGYLHQvtaggrnLSAGQLQLL 1088
Cdd:PRK11308 94 IQIVFQNPY---GSLnpRKKVGQilEEPLLINTSLSAAERREKALAMMAKVGlrpehyDRYPHM-------FSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTT--LIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELL 1165
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 243
|
250
....*....|....*...
gi 1108176189 1166 AAGGH-YSR-LWAAHTRL 1181
Cdd:PRK11308 244 NNPRHpYTQaLLSATPRL 261
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
347-555 |
4.16e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslRSA---IGLVPEDAVLFSG- 422
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH--KRArlgIGYLPQEASIFRKl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TIGANIA-----YGRPDATPEQIAtaarAAHIEEF-VNTLPDgyqtavgARGLTLSGGQRQRIALARALLHQPRLLIMDD 496
Cdd:COG1137 94 TVEDNILavlelRKLSKKEREERL----EELLEEFgITHLRK-------SKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 497 PTSAVD--AVIEcgIQEVLREaIADR-TAVIFT--RRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:COG1137 163 PFAGVDpiAVAD--IQKIIRH-LKERgIGVLITdhNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
340-556 |
4.16e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTlDSLRSaIGLVPEDAVL 419
Cdd:PRK11000 12 AYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERG-VGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 420 FSG-TIGANIAYGRpdatpeQIATAARAaHIEEFVNTLPDGYQTA--VGARGLTLSGGQRQRIALARALLHQPRLLIMDD 496
Cdd:PRK11000 87 YPHlSVAENMSFGL------KLAGAKKE-EINQRVNQVAEVLQLAhlLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 497 PTSAVDAVIEcgIQevLREAIA------DRTAVIFTRRR-SMLTLADRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK11000 160 PLSNLDAALR--VQ--MRIEISrlhkrlGRTMIYVTHDQvEAMTLADKIVVLDAGRVAQVGKPLELY 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
345-549 |
4.51e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 345 ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvrelTLDSLRSAIGLVPEDAVLFS-GT 423
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMFQDARLLPwKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 424 IGANIAYG-----RPDATpeqiaTAARAAHIEEFVNTLPdgyqtavgargLTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:PRK11247 98 VIDNVGLGlkgqwRDAAL-----QALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 499 SAVDAVIECGIQEvLREAIADR---TAVIFTRRRS-MLTLADRVAVLDSGRL-LDV 549
Cdd:PRK11247 162 GALDALTRIEMQD-LIESLWQQhgfTVLLVTHDVSeAVAMADRVLLIEEGKIgLDL 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
347-552 |
5.22e-17 |
|
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: 87.38 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVrELTLDSLRSAIGLVPEDAVLFSG-TIG 425
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 426 ANIA-YGRPDATPEQIATAARAAHIEEfvntlpDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAV 504
Cdd:TIGR01257 1022 EHILfYAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1108176189 505 IECGIQEVLREAIADRTAVIFTRRRSML-TLADRVAVLDSGRLLDVGTP 552
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
949-1138 |
5.26e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 949 YSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDpTHGTVRVDG--------CDLREFDVDGYRNRLG 1020
Cdd:PRK14258 15 FYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1021 IVTQEQYVFAGTVRDAIAYGrpdatdaqveraAREVGAHPMI-------TALDNGYL-----HQVTAGGRNLSAGQLQLL 1088
Cdd:PRK14258 92 MVHPKPNLFPMSVYDNVAYG------------VKIVGWRPKLeiddiveSALKDADLwdeikHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDPATEAVVQR--ATLTLAARRTTLIVAHGL 1138
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESliQSLRLRSELTMVIVSHNL 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-513 |
5.52e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.22 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSF---GYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVReltldslrsai 410
Cdd:COG4525 4 LTVRHVSVrypGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-------TIGANIAYGRPDATPEQIATAARAAHIEEFVntlpdGYQTAVGARGLTLSGGQRQRIALAR 483
Cdd:COG4525 73 GPGADRGVVFQKdallpwlNVLDNVAFGLRLRGVPKAERRARAEELLALV-----GLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190
....*....|....*....|....*....|
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVL 513
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
332-555 |
5.62e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRElTLDSLRSAIG 411
Cdd:PRK13536 40 VAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPE-DAVLFSGTIGAN-IAYGRpdatpeqiATAARAAHIEEFVNTLPD--GYQTAVGARGLTLSGGQRQRIALARALLH 487
Cdd:PRK13536 118 VVPQfDNLDLEFTVRENlLVFGR--------YFGMSTREIEAVIPSLLEfaRLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRR--RSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
690-918 |
6.84e-17 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 82.59 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 690 GYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVL 769
Cdd:cd18572 61 SYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 770 LIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLA 849
Cdd:cd18572 141 LAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYA 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 850 LYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18572 221 GYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
947-1166 |
8.03e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.20 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYrTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG--CDLREFDVDGYRNRLGIVTQ 1024
Cdd:PRK13636 11 LNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 --EQYVFAGTVRDAIAYGR------PDATDAQVERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLV 1096
Cdd:PRK13636 90 dpDNQLFSASVYQDVSFGAvnlklpEDEVRKRVDNALKRTG----IEHLKDKPTHC-------LSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAI-AEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
33-309 |
8.57e-17 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 82.47 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 33 IAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATYLL--------TYVRRYYGGRIAHLVQHDLRMDAFQALLRWD 104
Cdd:cd18554 14 IPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIflilrppvEYYRQYFAQWIANKILYDIRKDLFDHLQKLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 105 GRQQDRWSSGQLIVRTTNDLQLVQA-LLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRSRRLLAAA 183
Cdd:cd18554 94 LRYYANNRSGEIISRVINDVEQTKDfITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 184 THCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFALGGW 263
Cdd:cd18554 174 TKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAY 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1108176189 264 MAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18554 254 LVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
350-555 |
9.37e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVReLT--LDSLRSAIGLVPEDAVLFSG-TIGA 426
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRspRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYGRPDATPEQIATAARAAHIEEFVNTL-----PDGYqtaVGarglTLSGGQRQRIALARALLHQPRLLIMDDPTS-- 499
Cdd:COG3845 100 NIVLGLEPTKGGRLDRKAARARIRELSERYgldvdPDAK---VE----DLSVGEQQRVEILKALYRGARILILDEPTAvl 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 500 ---AVDAVIecgiqEVLREAIADRTAVIF-TRR-RSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:COG3845 173 tpqEADELF-----EILRRLAAEGKSIIFiTHKlREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
332-555 |
1.10e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.21 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIG 411
Cdd:PRK11231 1 MTLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEDAVLFSG-TIGANIAYGRP----------DATPEQIATAARAAHIEEFVNtlpdgyqtavgaRGLT-LSGGQRQRI 479
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLAD------------RRLTdLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIftrrrSML-------TLADRVAVLDSGRLLDVGTP 552
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVV-----TVLhdlnqasRYCDHLVVLANGHVMAQGTP 222
|
...
gi 1108176189 553 DEV 555
Cdd:PRK11231 223 EEV 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-550 |
1.15e-16 |
|
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: 80.10 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSaIGLVPEDAVLFSG-TIGAN 427
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 428 IAY-GRPDATPEQIATAAraahIEEFVNTLpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIE 506
Cdd:cd03266 99 LEYfAGLYGLKGDELTAR----LEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1108176189 507 CGIQEVLREAIADRTAVIFTRRR--SMLTLADRVAVLDSGRLLDVG 550
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHImqEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
334-556 |
1.17e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQ--DVRELTLDSLRSAIG 411
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPE--DAVLFSGTIGANIAYGRPD-ATPE-QIATAARAAHIEEFVNTLPDGYQTAvgargltLSGGQRQRIALARALLH 487
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGAVNlKLPEdEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEVLREAIA--DRTAVIFTRRRSMLTL-ADRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
959-1167 |
1.27e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGC------DLREFDVDGYRNRLGIVTQEQYVFAG- 1031
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRDAIAY-----GRPDATDAQ--VERAAREVGahpmitaLDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:PRK14246 106 SIYDNIAYplkshGIKEKREIKkiVEECLRKVG-------LWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1105 EATVALDPATEAVVQRATLTLAARRTTLIVAHG-LAIAEHADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
354-502 |
1.28e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 354 SLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRElTLDSLRSAIGLVPEDAvLFSG-TIGANIAYG- 431
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRPVSMLFQENN-LFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 432 RP-----DATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:PRK10771 97 NPglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
347-555 |
1.34e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDS-LRSAIGLVPEDAVLFSG-TI 424
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANIAYG---RPDATPEQIATAARAA----HIEEFVNTLpdgyqtavgarGLTLSGGQRQRIALARALLHQPRLLIMDDP 497
Cdd:PRK10895 96 YDNLMAVlqiRDDLSAEQREDRANELmeefHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 498 TSAVDAVIECGIQEVLREAIADRTAVIFTRR--RSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHnvRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
329-541 |
1.47e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.14 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 329 EARLSLEFQRVSFgYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRS 408
Cdd:PRK10247 3 ENSPLLQLQNVGY-LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 409 AIGLVPEDAVLFSGTIGANIAYgrpdatPEQIAT-----AARAAHIEEFvnTLPDgyqTAVGARGLTLSGGQRQRIALAR 483
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIF------PWQIRNqqpdpAIFLDDLERF--ALPD---TILTKNIAELSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR-TAVIF-TRRRSMLTLADRVAVL 541
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQnIAVLWvTHDKDEINHADKVITL 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
958-1162 |
1.77e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.44 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlREFDVDG---------YRNRLGIVTQeQYV 1028
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG---NHFDFSKtpsdkaireLRRNVGMVFQ-QYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 FAG--TVRDAIAygrpDA-------TDAQVERAAREVGAHPMITALDNGY-LHqvtaggrnLSAGQLQLLALARARLVDP 1098
Cdd:PRK11124 93 LWPhlTVQQNLI----EApcrvlglSKDQALARAEKLLERLRLKPYADRFpLH--------LSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARR-TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHT 1162
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
343-555 |
1.92e-16 |
|
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: 84.08 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 343 YVADRPVLR---EISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGA--VRIGGQ--DVRELTLDSLRSA---IGL 412
Cdd:TIGR03269 290 ISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDGRGRAkryIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFS-GTIGANIAYGRPDATPEQIATAaRAAHI-----------EEFVNTLPDgyqtavgarglTLSGGQRQRIA 480
Cdd:TIGR03269 370 LHQEYDLYPhRTVLDNLTEAIGLELPDELARM-KAVITlkmvgfdeekaEEILDKYPD-----------ELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDAVIECGIQEVL---REAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
947-1189 |
2.55e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVpALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLReFDVDG---YRNRLGIVT 1023
Cdd:PRK13639 7 LKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSlleVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1024 Q--EQYVFAGTVRDAIAYG------RPDATDAQVERAAREVGahpmITALDNGYLHqvtaggrNLSAGQLQLLALARARL 1095
Cdd:PRK13639 85 QnpDDQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVG----MEGFENKPPH-------HLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1096 VDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVA-HGLAIAE-HADRIVVLEHGTVVEDGAHTELLAaggHYSR 1173
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS---DIET 230
|
250
....*....|....*.
gi 1108176189 1174 LWAAHTRLcsPEITQL 1189
Cdd:PRK13639 231 IRKANLRL--PRVAHL 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
959-1159 |
3.63e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.50 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYD-----PTHGTVRVDGCDLREFDVDG--YRNRLGIVTQEQYVFAG 1031
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPieVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 -TVRDAIAYG--------RPDATDAQVERAAREVGAHPMITALDNGYlhqvtagGRNLSAGQLQLLALARARLVDPDILL 1102
Cdd:PRK14267 100 lTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1103 LDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-581 |
5.00e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.75 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 320 VDGTKPLSPEARLSLEFqrvsfgyvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGA-----VRIG 394
Cdd:PRK14271 15 VDAAAPAMAAVNLTLGF--------AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 395 GQDV---RELTldSLRSAIGLVPEDAVLFSGTIGANIAYG--RPDATPEQIATAARAAHIEEFvnTLPDGYQTAVGARGL 469
Cdd:PRK14271 87 GRSIfnyRDVL--EFRRRVGMLFQRPNPFPMSIMDNVLAGvrAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 470 TLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLReAIADRTAVIFTRRR--SMLTLADRVAVLDSGRLL 547
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR-SLADRLTVIIVTHNlaQAARISDRAALFFDGRLV 241
|
250 260 270
....*....|....*....|....*....|....
gi 1108176189 548 DVGtPDEVWERCPRYRELLSPAPDLADDLVVAER 581
Cdd:PRK14271 242 EEG-PTEQLFSSPKHAETARYVAGLSGDVKDAKR 274
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
336-498 |
5.21e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 336 FQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGqDVReltldslrsaIGLVPE 415
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 416 DAVLFSG-TIGANIAYGRPD-------------ATPEQIATAARAAHIEEFVNTLpDGYQTAVGARGL------------ 469
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGDAElraleaeleeleaKLAEPDEDLERLAELQEEFEAL-GGWEAEARAEEIlsglgfpeedld 147
|
170 180 190
....*....|....*....|....*....|...
gi 1108176189 470 ----TLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:COG0488 148 rpvsELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
957-1164 |
5.49e-16 |
|
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: 79.90 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyrnRLGIVTQEQYVFAGTVRDA 1036
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1037 IAYG--------RPDATDAQVERaarEVGAHPmitALDNGYLHQvtaGGRNLSAGQLQLLALARARLVDPDILLLDEATV 1108
Cdd:cd03291 118 IIFGvsydeyryKSVVKACQLEE---DITKFP---EKDNTVLGE---GGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1109 ALDPATEA-VVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:cd03291 189 YLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
947-1107 |
5.64e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyRNRLGIVTQEQ 1026
Cdd:COG0488 4 LSKSFGGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 YVFAG-TVRDAI----------------AYGRPDATDAQVERAARevgAHPMITALDnGY-----LHQVTAG-G------ 1077
Cdd:COG0488 71 PLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAE---LQEEFEALG-GWeaearAEEILSGlGfpeedl 146
|
170 180 190
....*....|....*....|....*....|....
gi 1108176189 1078 ----RNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
346-547 |
5.76e-16 |
|
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: 78.47 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLAT---RCYDVTQGAVRIGGQdvrELTLDSLRSAIGLVPEDAVLFSG 422
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 -TIGANIAYGRPDATPEQIATAARAAHIEEFVntLPDGYQTAVGARGLT-LSGGQRQRIALARALLHQPRLLIMDDPTSA 500
Cdd:cd03234 96 lTVRETLTYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1108176189 501 VDAVIECGIQEVLREAIADRTAVIFT---RRRSMLTLADRVAVLDSGRLL 547
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTihqPRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
945-1159 |
5.97e-16 |
|
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: 78.18 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 945 DAVHYSYR--TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLRE--FDVdgyRNRLG 1020
Cdd:cd03266 5 DALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEA---RRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1021 IVTQEQYVFAG-TVRDAIAY-GR-----PDATDAQVERAAREVGAHPmitaldngYLHQVTAGgrnLSAGQLQLLALARA 1093
Cdd:cd03266 82 FVSDSTGLYDRlTARENLEYfAGlyglkGDELTARLEELADRLGMEE--------LLDRRVGG---FSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1094 RLVDPDILLLDEATVALD-PATEAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
957-1164 |
7.04e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLRefDVDGYRNRLGIVTQEQYVFAG-TVRD 1035
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1036 AIAYGRPDATDAQVERAARevgAHPMITaldngYLHQVTAGGR---NLSAGQLQLLALARARLVDPDILLLDEATVALDP 1112
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASR---VNEMLG-----LVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1113 ATEAVVQRATLTLAAR--RTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK11607 183 KLRDRMQLEVVDILERvgVTCVMVTHDQEEAmTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-549 |
7.16e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 342 GYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSlRSA-IGLVPEDAVL- 419
Cdd:COG1101 14 GTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 420 --FSGTIGAN--IAYGRPDATPEQIA-TAARAAHIEEFVNTLPDGY----QTAVGArgltLSGGQRQRIALARALLHQPR 490
Cdd:COG1101 93 taPSMTIEENlaLAYRRGKRRGLRRGlTKKRRELFRELLATLGLGLenrlDTKVGL----LSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 491 LLIMDDPTSAVD---AVIecgIQEVLREAIADR--TAVIFTrrRSM---LTLADRVAVLDSGR-LLDV 549
Cdd:COG1101 169 LLLLDEHTAALDpktAAL---VLELTEKIVEENnlTTLMVT--HNMeqaLDYGNRLIMMHEGRiILDV 231
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
17-309 |
7.76e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 79.45 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 17 RRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAA-DHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMD 95
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPgTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 96 AFQALlrwdgrQQ------DRWSSGQLIVRTTNDLQLVQAL----LFDvpnvLRHVLTLLLGVA-VMTWLSVPLALLAVL 164
Cdd:cd18540 81 AFEHL------QTlsfsyfDKTPVGWIMARVTSDTQRLGEIiswgLVD----LVWGITYMIGILiVMLILNWKLALIVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 165 LVPVIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGP 244
Cdd:cd18540 151 VVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLP 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 245 LLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18540 231 IVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
948-1150 |
8.26e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 948 HYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQY 1027
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 VFAGTVRDAIAYG---RPDATDAQVERAAREVGAHPmitaldngyLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:PRK10247 92 LFGDTVYDNLIFPwqiRNQQPDPAIFLDDLERFALP---------DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1108176189 1105 EATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEHADRIVVL 1150
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
958-1157 |
8.79e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.66 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYD-----PTHGTVRVDGCDL--REFDVDGYRNRLGIVTQEQYVFA 1030
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRDAIAYG-------RPDATDAQVERAARevGAHPMITALDNgyLHQVTAGgrnLSAGQLQLLALARARLVDPDILLL 1103
Cdd:PRK14239 100 MSIYENVVYGlrlkgikDKQVLDEAVEKSLK--GASIWDEVKDR--LHDSALG---LSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVVE 1157
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIE 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
955-1169 |
9.29e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlREFDVDgYRNRLGIVTQEQyvfaG--- 1031
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPE-DRRRIGYLPEER----Glyp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 --TVRDAIAY-GR-PDATDAQVERAAREvgahpmitaldngYLHQVTAGGR------NLSAGQLQLLALARARLVDPDIL 1101
Cdd:COG4152 85 kmKVGEQLVYlARlKGLSKAEAKRRADE-------------WLERLGLGDRankkveELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1102 LLDEATVALDPATEAVVQRATLTLAARRTTLIVA-HGLAIAE-HADRIVVLEHGTVVEDGAHTELLAAGG 1169
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVEeLCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
955-1158 |
1.02e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.08 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGY----RNRLGIVTQEQYVF- 1029
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 ----AGTVRDAIAYgrpdatdAQVERAAREVGAHPMITALdnGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDE 1105
Cdd:PRK10535 100 hltaAQNVEVPAVY-------AGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1106 ATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLAIAEHADRIVVLEHGTVVED 1158
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
959-1159 |
1.35e-15 |
|
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: 76.44 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVA--RFYDPTHGTVRVDGCDLREFDvdgYRNRLGIVTQEQYVFAG-TVRD 1035
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRS---FRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1036 AIAYgrpdatdaqveraarevgahpmitaldngylhqvTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATE 1115
Cdd:cd03213 102 TLMF----------------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1108176189 1116 AVVQRATLTLAAR-RTTLIVAHGLA--IAEHADRIVVLEHGTVVEDG 1159
Cdd:cd03213 148 LQVMSLLRRLADTgRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
944-1166 |
1.51e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.72 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYR---TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG----CDLREFDVDGYR 1016
Cdd:PRK13641 5 FENVDYIYSpgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1017 NRLGIVTQ--EQYVFAGTVRDAIAYGRPD--ATDAQVERAA----REVGahpmitaLDNGYLHQVTAggrNLSAGQLQLL 1088
Cdd:PRK13641 85 KKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAlkwlKKVG-------LSEDLISKSPF---ELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDP-ATEAVVQRATLTLAARRTTLIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPeGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
324-546 |
1.54e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 324 KPLSPEARLSLEF---QRVSfgyVADRPVL----------REISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGA 390
Cdd:PRK15439 243 KSLSASQKLWLELpgnRRQQ---AAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 391 VRIGGQDVREL-TLDSLRSAIGLVPED----AVLFSGTIGANI---AYGRPdatPEQIATAARAAHIEefvntlpdGYQT 462
Cdd:PRK15439 320 IMLNGKEINALsTAQRLARGLVYLPEDrqssGLYLDAPLAWNVcalTHNRR---GFWIKPARENAVLE--------RYRR 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 463 AVG---------ARglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRR--RSM 531
Cdd:PRK15439 389 ALNikfnhaeqaAR--TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSdlEEI 466
|
250
....*....|....*
gi 1108176189 532 LTLADRVAVLDSGRL 546
Cdd:PRK15439 467 EQMADRVLVMHQGEI 481
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
345-555 |
1.57e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.04 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 345 ADRPVLREISLSVRAGETLAVVGAPGSGKSTLAS-LATRCyDVTQGAVRIGGQDVRELTLDSL---------RSAIGLV- 413
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNaLSARL-APDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 --PEDAVLFSGTIGANIA----------YGRPDATPEQ------IAtAARaahieefVNTLPDgyqtavgarglTLSGGQ 475
Cdd:PRK11701 96 qhPRDGLRMQVSAGGNIGerlmavgarhYGDIRATAGDwlerveID-AAR-------IDDLPT-----------TFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 476 RQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFTRRRSMLT-LADRVAVLDSGRLLDVGTP 552
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARlLAHRLLVMKQGRVVESGLT 236
|
...
gi 1108176189 553 DEV 555
Cdd:PRK11701 237 DQV 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
311-514 |
1.64e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 311 ELIDSRPT-----LVDGTKPLspearLSLEFQRVSFGY--------VADRPVLREISLSVRAGETLAVVGAPGSGKSTlA 377
Cdd:PRK15134 255 KLLNSEPSgdpvpLPEPASPL-----LDVEQLQVAFPIrkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKST-T 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 378 SLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAIGLV---PEDAVLFSGTIGANIAYG----RPDATPEQIATAARAA 447
Cdd:PRK15134 329 GLALLRLINSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVfqdPNSSLNPRLNVLQIIEEGlrvhQPTLSAAQREQQVIAV 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 448 HIEefVNTLPDGYQTAVGArgltLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLR 514
Cdd:PRK15134 409 MEE--VGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLK 469
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
345-541 |
1.82e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.12 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 345 ADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvRELTLDSLRSAIG----LVPEDAVLF 420
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSEVPdslpLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 421 sGTIGANIAYGRPDATPEQIATAAraahieefvntlpdgyQTAVGARGL------TLSGGQRQRIALARALLHQPRLLIM 494
Cdd:NF040873 81 -GRWARRGLWRRLTRDDRAAVDDA----------------LERVGLADLagrqlgELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1108176189 495 DDPTSAVDAVIECGIQEVLREAIAD-RTAVIFTRRRSMLTLADRVAVL 541
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
334-513 |
1.96e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslRSAI--- 410
Cdd:PRK11248 2 LQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--RGVVfqn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 -GLVPEDAVLfsgtigANIAYGRpdatpeQIATAARAAHIEEFVNTLPDGYQTAVGARGL-TLSGGQRQRIALARALLHQ 488
Cdd:PRK11248 79 eGLLPWRNVQ------DNVAFGL------QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAAN 146
|
170 180
....*....|....*....|....*
gi 1108176189 489 PRLLIMDDPTSAVDAVIECGIQEVL 513
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLL 171
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
947-1159 |
2.09e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.03 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARF--YDPTHGTVRVDGCDLREFDVDgYRNRLGIVtq 1024
Cdd:cd03217 6 LHVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 eqyvfagtvrdaIAYGRPDATdaqveraarevgahPMITALDngYLHQVTAGgrnLSAGQ------LQLLALararlvDP 1098
Cdd:cd03217 81 ------------LAFQYPPEI--------------PGVKNAD--FLRYVNEG---FSGGEkkrneiLQLLLL------EP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1099 DILLLDEATVALD-PATEAVVQRATLTLAARRTTLIVAHGLAIAEH--ADRIVVLEHGTVVEDG 1159
Cdd:cd03217 124 DLAILDEPDSGLDiDALRLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSG 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
332-553 |
2.10e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYVADRpVLREISLSVRAGETLAVVGAPGSGKSTLA--------------SLATRCYDVTQgavRIGGQD 397
Cdd:PRK11124 1 MSIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLrvlnllemprsgtlNIAGNHFDFSK---TPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 398 VRELtldslRSAIGLV-------PEDAVLfSGTIGANI---AYGRPDATPEQIATAARAaHIEEFVNTLPdgyqtavgar 467
Cdd:PRK11124 77 IREL-----RRNVGMVfqqynlwPHLTVQ-QNLIEAPCrvlGLSKDQALARAEKLLERL-RLKPYADRFP---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 468 gLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLRE-AIADRTAVIFTRRRSML-TLADRVAVLDSGR 545
Cdd:PRK11124 140 -LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVArKTASRVVYMENGH 218
|
....*...
gi 1108176189 546 LLDVGTPD 553
Cdd:PRK11124 219 IVEQGDAS 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
958-1173 |
2.70e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.59 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRN-RLGIvtqeQYVFAG----- 1031
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvRSDI----QMIFQDplasl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 ----TVRDAIA-----YgRPDATDAQVERAARE----VGAHPmitALDNGYLHQvtaggrnLSAGQLQLLALARARLVDP 1098
Cdd:PRK15079 112 nprmTIGEIIAeplrtY-HPKLSRQEVKDRVKAmmlkVGLLP---NLINRYPHE-------FSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1099 DILLLDEATVALDPATEAVV-------QRAT-LTLaarrttLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGG 1169
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVvnllqqlQREMgLSL------IFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPL 254
|
....*
gi 1108176189 1170 H-YSR 1173
Cdd:PRK15079 255 HpYTK 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-567 |
2.80e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 339 VSFGYVADRP----VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGG-------QDVRELTldSLR 407
Cdd:PRK13645 12 VSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVK--RLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 408 SAIGLV---PEDAvLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVnTLPDGYqtaVGARGLTLSGGQRQRIALARA 484
Cdd:PRK13645 90 KEIGLVfqfPEYQ-LFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAVIE---CGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVWERcpr 561
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN--- 241
|
....*.
gi 1108176189 562 yRELLS 567
Cdd:PRK13645 242 -QELLT 246
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
349-556 |
2.97e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLAS-----LATRCYDVTQGAVRIGGQDVRELTLDS-----------LRSAIGL 412
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 V---PEDAvLFSGTIGANIAYGRPDATPEQIATAARAAHieeFVNTLPDGYqTAVGARGLTLSGGQRQRIALARALLHQP 489
Cdd:PRK13631 121 VfqfPEYQ-LFKDTIEKDIMFGPVALGVKKSEAKKLAKF---YLNKMGLDD-SYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 490 RLLIMDDPTSAVDAVIECGIQEVLREAIAD-RTAVIFTRR-RSMLTLADRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTmEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
959-1169 |
3.50e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.98 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDgcdlrefdvdgyrNRLGIVTQEQYVFAGTVRDAIA 1038
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1039 YGRPDATdAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPAT-EAV 1117
Cdd:PTZ00243 743 FFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERV 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1118 VQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVV-----EDGAHTEL---LAAGG 1169
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEfsgssADFMRTSLyatLAAEL 881
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
340-558 |
3.53e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDslRSAIGLVPEDAVL 419
Cdd:PRK11432 15 RFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 420 FSG-TIGANIAYG-----RPDA-TPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALARALLHQPRLL 492
Cdd:PRK11432 90 FPHmSLGENVGYGlkmlgVPKEeRKQRVKEALELVDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 493 IMDDPTSAVDAVIECGIQEVLREAIA--DRTAVIFTRRRS-MLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
957-1174 |
4.90e-15 |
|
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: 80.72 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyrnRLGIVTQEQYVFAGTVRDA 1036
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1037 IAYG--------RPDATDAQVERAarevgahpmITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATV 1108
Cdd:TIGR01271 507 IIFGlsydeyryTSVIKACQLEED---------IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1109 ALDPATEA-VVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRL 1174
Cdd:TIGR01271 578 HLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
332-557 |
5.29e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.79 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYVADRPV----LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT----L 403
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 404 DSLRSAIGLV---PEdAVLFSGTIGANIAYGRPD--ATPEQIATAA-----RAAHIEEFVNTLPdgyqtavgargLTLSG 473
Cdd:PRK13641 81 KKLRKKVSLVfqfPE-AQLFENTVLKDVEFGPKNfgFSEDEAKEKAlkwlkKVGLSEDLISKSP-----------FELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 474 GQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLRE-AIADRTAVIFTRRRSMLT-LADRVAVLDSGRLLDVGT 551
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHAS 228
|
....*.
gi 1108176189 552 PDEVWE 557
Cdd:PRK13641 229 PKEIFS 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
338-556 |
6.76e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.46 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFGyVADRPV--LREISLSVRAGETLAVVGAPGSGKSTLAS-----LATRcyDVTQGAVRIGGQDV---RELTLDSLR 407
Cdd:PRK09473 19 RVTFS-TPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFalmglLAAN--GRIGGSATFNGREIlnlPEKELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 408 SAiglvpEDAVLFSGTIGANIAYGRpdaTPEQIATA-------ARAAHIEEFVNTLpDGYQTAVGARGLTL-----SGGQ 475
Cdd:PRK09473 96 AE-----QISMIFQDPMTSLNPYMR---VGEQLMEVlmlhkgmSKAEAFEESVRML-DAVKMPEARKRMKMyphefSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 476 RQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIAD-RTAVIftrrrsMLT--------LADRVAVLDSGRL 546
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAII------MIThdlgvvagICDKVLVMYAGRT 240
|
250
....*....|
gi 1108176189 547 LDVGTPDEVW 556
Cdd:PRK09473 241 MEYGNARDVF 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
346-545 |
7.46e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLAS-----LATRCYDVTQGAVRIGGQDV---RELTLDSLRS--------- 408
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALsilrlLPSPPVVYPSGDIRFHGESLlhaSEQTLRGVRGnkiamifqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 409 -AIGLVP---------EDAVLFSGTiganiayGRPDATPEQIATAARAAhIEEFVNTLPD-GYQtavgargltLSGGQRQ 477
Cdd:PRK15134 101 pMVSLNPlhtlekqlyEVLSLHRGM-------RREAARGEILNCLDRVG-IRQAAKRLTDyPHQ---------LSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 478 RIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIAD-RTAVIF-TRRRSML-TLADRVAVLDSGR 545
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFiTHNLSIVrKLADRVAVMQNGR 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
300-498 |
7.48e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 300 QQARAGAVRVLELIDSRPtlVDGTKPLS--PEARLS---LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKS 374
Cdd:COG0488 279 AQSRIKALEKLEREEPPR--RDKTVEIRfpPPERLGkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 375 TLASLATRCYDVTQGAVRIgGQDVRELTLDSLRSAigLVPEDAVLfsgtigANIAYGRPDATPEQIataarAAHIEEFvn 454
Cdd:COG0488 356 TLLKLLAGELEPDSGTVKL-GETVKIGYFDQHQEE--LDPDKTVL------DELRDGAPGGTEQEV-----RGYLGRF-- 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1108176189 455 tL--PDGYQTAVGarglTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:COG0488 420 -LfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
349-503 |
7.81e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATrCYD-VTQGAVRIGGQDVRELTLDSL----RSAIGLVPEDAVLFSG- 422
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILG-CLDkPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TIGANIAYgrpDATPEQIATAARAAHIEEFVNTLpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:PRK10535 102 TAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
.
gi 1108176189 503 A 503
Cdd:PRK10535 177 S 177
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
962-1166 |
8.55e-15 |
|
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: 77.45 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 962 INLRIPA-GQTVVFvGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL----REFDVDGYRNRLGIVTQEQYVFAG-TVRD 1035
Cdd:COG4148 18 VDFTLPGrGVTALF-GPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1036 AIAYGRPDAtdaqvERAAREVGAHPMITALDNGYLhqVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPAT- 1114
Cdd:COG4148 97 NLLYGRKRA-----PRAERRISFDEVVELLGIGHL--LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARk 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1115 -------EAVVQRATLTLaarrttLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:COG4148 170 aeilpylERLRDELDIPI------LYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
927-1155 |
8.58e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 927 PSSPAARPVGTlrgEVVFDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD 1006
Cdd:PRK11247 1 MMNTARLNQGT---PLLLNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1007 LREFdvdgyRNRLGIVTQEQYVFA-GTVRDAIAYGRPDATDAQVERAAREVG----AHPMITAldngylhqvtaggrnLS 1081
Cdd:PRK11247 76 LAEA-----REDTRLMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGladrANEWPAA---------------LS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1082 AGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGL--AIAeHADRIVVLEHGTV 1155
Cdd:PRK11247 136 GGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVseAVA-MADRVLLIEEGKI 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
962-1171 |
9.49e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 962 INLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDgcDLREFDVDGYRNRLGIVTQEQYVFAG-TVRDAIAYG 1040
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVFQSYALYPHlSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1041 RPDATDAQVERAAReVGAHPMITALDngylHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPA--TEAVV 1118
Cdd:PRK11000 100 LKLAGAKKEEINQR-VNQVAEVLQLA----HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrVQMRI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1119 QRATLTLAARRTTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLaaggHY 1171
Cdd:PRK11000 175 EISRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLELY----HY 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
947-1169 |
1.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.92 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRT-REVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQ- 1024
Cdd:PRK13650 10 LTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 --EQYVFAgTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDngYLHQVTAggrNLSAGQLQLLALARARLVDPDILL 1102
Cdd:PRK13650 90 pdNQFVGA-TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQD--FKEREPA---RLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1103 LDEATVALDP--------ATEAVVQRATLTLaarrttLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGG 1169
Cdd:PRK13650 164 LDEATSMLDPegrlelikTIKGIRDDYQMTV------ISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
953-1177 |
1.15e-14 |
|
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: 78.19 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 953 TREVPALAGINLRIPAGQTVVFVGSTGSGKS----TLIKLVARFYDPTHGTVRVDGCDLREFDVDGYR----NRLGIVTQ 1024
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQY-----VFagTVRDAIA--------YGRPDATDAQVE--------RAAREVGAHPmitaldngylHQvtaggrnLSAG 1083
Cdd:COG4172 100 EPMtslnpLH--TIGKQIAevlrlhrgLSGAAARARALEllervgipDPERRLDAYP----------HQ-------LSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1084 QLQLLALARARLVDPDILLLDEATVALDpateAVVQRATLTLAA---RRTT---LIVAHGLAI-AEHADRIVVLEHGTVV 1156
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQILDLLKdlqRELGmalLLITHDLGVvRRFADRVAVMRQGEIV 236
|
250 260
....*....|....*....|...
gi 1108176189 1157 EDGAHTELLAAGGH-YSR-LWAA 1177
Cdd:COG4172 237 EQGPTAELFAAPQHpYTRkLLAA 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-572 |
1.26e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTldslRSAIGLVPEDAVLFSGTIGAN 427
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS----RQVIELSEQSAAQMRHVRGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 428 IA--YGRPDAT-------PEQIATAAR----AAHIEEFVNT--------LPDGyQTAVGARGLTLSGGQRQRIALARALL 486
Cdd:PRK10261 106 MAmiFQEPMTSlnpvftvGEQIAESIRlhqgASREEAMVEAkrmldqvrIPEA-QTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRT-AVIFTRRRS--MLTLADRVAVLDSGRLLDVGTPDEVWERC--PR 561
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmGVIFITHDMgvVAEIADRVLVMYQGEAVETGSVEQIFHAPqhPY 264
|
250
....*....|.
gi 1108176189 562 YRELLSPAPDL 572
Cdd:PRK10261 265 TRALLAAVPQL 275
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
951-1178 |
1.32e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 951 YRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLrEFDVDGYRN-RLGIVTQEQYVf 1029
Cdd:PRK15112 21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMIFQDPST- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AGTVRDAIAYG-----------RPDATDAQVERAAREVGahpMITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDP 1098
Cdd:PRK15112 99 SLNPRQRISQIldfplrlntdlEPEQREKQIIETLRQVG---LLPDHASYYPHM-------LAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1099 DILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGGH--YSR 1173
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASPLHelTKR 248
|
....*
gi 1108176189 1174 LWAAH 1178
Cdd:PRK15112 249 LIAGH 253
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
962-1152 |
1.60e-14 |
|
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: 72.57 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 962 INLRIPAGQTVVFVGSTGSGKSTLIKLVARFYdpTHGTVRVDGCDlrefdvdgyRNRLGIVTQEQYVFAGTVRDAIAYgr 1041
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLW--PWGSGRIGMPE---------GEDLLFLPQRPYLPLGTLREQLIY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1042 pdatdaqveraarevgahpmitaldngylhqvtAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRA 1121
Cdd:cd03223 87 ---------------------------------PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180 190
....*....|....*....|....*....|..
gi 1108176189 1122 tltLAARRTTLI-VAHGLAIAEHADRIVVLEH 1152
Cdd:cd03223 134 ---LKELGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
23-278 |
2.02e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 75.27 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 23 GFGAALAGTVIAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATY-LLTYVR----RYYGGRIAHLVQHDLrmdaF 97
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSgLFSGLRggcfSYAGTRLVRRLRRDL----F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 98 QALLRWDGRQQDRWSSGQLIVRTTNDLQLV-QALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAHRS 176
Cdd:cd18572 77 RSLLRQDIAFFDATKTGELTSRLTSDCQKVsDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 177 RRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMA 256
Cdd:cd18572 157 GRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVL 236
|
250 260
....*....|....*....|..
gi 1108176189 257 VFALGGWMAAQGSITVGTFVAF 278
Cdd:cd18572 237 VLFYGGHLVLSGRMSAGQLVTF 258
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
347-546 |
2.73e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYD-VTQGAVRIGGQDVRELT-LDSLRSAIGLVPED-----AVL 419
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDrkrdgIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 420 FSGtIGANIAYGRPD--ATPEQIATAARAAHIEEFVNTL------PDgyqTAVGarglTLSGGQRQRIALARALLHQPRL 491
Cdd:PRK13549 355 VMG-VGKNITLAALDrfTGGSRIDDAAELKTILESIQRLkvktasPE---LAIA----RLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 492 LIMDDPTSAVD----AVIECGIQEVLREAIAdrTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:PRK13549 427 LILDEPTRGIDvgakYEIYKLINQLVQQGVA--IIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
955-1164 |
3.12e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVD----GCDLREFDVDGY------------RNR 1018
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNpyskkiknfkelRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LGIVTQ--EQYVFAGTVRDAIAYGrPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGgrnLSAGQLQLLALARARLV 1096
Cdd:PRK13631 118 VSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFG---LSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEhVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
349-515 |
3.40e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.31 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvrelTLDSLRSAiglvpEDAVLFSGTIGANI 428
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-----PMSKLSSA-----AKAELRNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 429 AYGR--PD-------ATPEQIATAARAAHIEEFVNTLpdgyqTAVGA------RGLTLSGGQRQRIALARALLHQPRLLI 493
Cdd:PRK11629 94 QFHHllPDftalenvAMPLLIGKKKPAEINSRALEML-----AAVGLehranhRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180
....*....|....*....|..
gi 1108176189 494 MDDPTSAVDAVIECGIQEVLRE 515
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGE 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
959-1156 |
3.49e-14 |
|
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: 73.07 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVA---RFYDPTHGTVRVDGCdlrEFDVDGYRNRLGIVTQEQYVFAG-TVR 1034
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1035 DAIAY------GRPDATDAQVERAAREVGAHPMITALDNGYLhqvtaggRNLSAGQLQLLALARARLVDPDILLLDEATV 1108
Cdd:cd03234 100 ETLTYtailrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLV-------KGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1109 ALDPATEAVVQRATLTLAAR-RTTLIVAH--GLAIAEHADRIVVLEHGTVV 1156
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRnRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
950-1166 |
3.69e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 73.35 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDgYRNRLGI--VTQEQY 1027
Cdd:cd03218 9 RYGKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLGIgyLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 VFAG-TVRD---AIAYGRPDATDAQVERAARevgahpMITALDNGYLHQVTAGGrnLSAGQLQLLALARARLVDPDILLL 1103
Cdd:cd03218 86 IFRKlTVEEnilAVLEIRGLSKKEREEKLEE------LLEEFHITHLRKSKASS--LSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAARRT-TLIVAHG----LAIaehADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNvretLSI---TDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
940-1166 |
4.49e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 940 GEVVFDAVHYSYRTR---EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG----CDLREF-D 1011
Cdd:PRK13645 5 KDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1012 VDGYRNRLGIVTQ--EQYVFAGTVRDAIAYGrPDATDAQVERAAREVGAHPMITALDNGYlhqVTAGGRNLSAGQLQLLA 1089
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1090 LARARLVDPDILLLDEATVALDPATEAVVQRATLTLAA--RRTTLIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
957-1153 |
5.30e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.36 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLrEFDVDGYRNRLGIVTQEQYVFAG-TVRD 1035
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1036 AIAYGrpdatdAQVERAAREVGAHPMITAL-DNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPAT 1114
Cdd:TIGR01257 1023 HILFY------AQLKGRSWEEAQLEMEAMLeDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1108176189 1115 EAVVQRATLTLAARRTTLIVAHGLAIAE-HADRIVVLEHG 1153
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQG 1136
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
955-1166 |
7.04e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVR-----------------------VDGCDLREF- 1010
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklvIQKTRFKKIk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1011 DVDGYRNRLGIVTQ--EQYVFAGTVRDAIAYGrPDATDAQVERAAREVGAHPMITALDNGYLHQVTAggrNLSAGQLQLL 1088
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPF---ELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDPA-TEAVVQRATLTLAARRTTLIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
334-558 |
8.74e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSlRSAIGLV 413
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PE-DAVLFSGTIGANI-AYGRPDATPEQiATAARAAHIEEFVNtlpdgYQTAVGARGLTLSGGQRQRIALARALLHQPRL 491
Cdd:PRK13537 86 PQfDNLDPDFTVRENLlVFGRYFGLSAA-AARALVPPLLEFAK-----LENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 492 LIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRR--RSMLTLADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHfmEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
334-536 |
8.76e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.83 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAI 410
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDA-VLFSGTIGANIAygrpdaTPEQIATAArAAHIEEFVNTLPDGYQTAVGARG--LTLSGGQRQRIALARALLH 487
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVA------IPLIIAGAS-GDDIRRRVSAALDKVGLLDKAKNfpIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 488 QPRLLIMDDPTSAVDAVIECGIQEVLRE----------AIADrTAVIFTRRRSMLTLAD 536
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEfnrvgvtvlmATHD-IGLISRRSYRMLTLSD 212
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
23-278 |
1.04e-13 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 73.32 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 23 GFGAALAGTVIAVLVPLVTKRVIDdaiAADHRPLAPWAVVLVAAAGATYLL---------TYVRRYYGGRIAHLVQHDLR 93
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLID---VASKESGDIEIFGLSLKTFALALLgvfvvgaaaNFGRVYLLRIAGERIVARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 94 MDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLV-QALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLI 172
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVgKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 173 A----HRSRRL-------LAAATHCAQEHKAAvtgvvdaavcgIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAH 241
Cdd:cd18573 158 AvfygRYVRKLskqvqdaLADATKVAEERLSN-----------IRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGL 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 1108176189 242 FGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAF 278
Cdd:cd18573 227 FFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSF 263
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
334-546 |
1.11e-13 |
|
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: 75.25 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLR--EISLSVRAGETLAVVGAPGSGKSTLASLATRCYD-VTQGAVRIGGQDVRELT-LDSLRSA 409
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 IGLVPED----AVLFSGTIGANIAY---------GRPDATPEQ--IATAARAAHIEEFVNTLPDGyqtavgarglTLSGG 474
Cdd:TIGR02633 338 IAMVPEDrkrhGIVPILGVGKNITLsvlksfcfkMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 475 QRQRIALARALLHQPRLLIMDDPTSAVD----AVIECGIQEVLREAIAdrTAVIFTRRRSMLTLADRVAVLDSGRL 546
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDvgakYEIYKLINQLAQEGVA--IIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
949-1164 |
1.15e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 949 YSYRTrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQ--EQ 1026
Cdd:PRK13652 11 YSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 YVFAGTVRDAIAYG------RPDATDAQVERAAREVGAHPMITALDNgylhqvtaggrNLSAGQLQLLALARARLVDPDI 1100
Cdd:PRK13652 90 QIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1101 LLLDEATVALDPATEAVVQRATLTLAAR--RTTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDlVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
959-1150 |
1.44e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.98 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIA 1038
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1039 YGRPDATDAQVERAAREVGAhpmitaldNGYLHQVTAggrNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVV 1118
Cdd:cd03231 96 FWHADHSDEQVEEALARVGL--------NGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|....
gi 1108176189 1119 QRATLTLAARRTTLIVA--HGLAIAEHADRIVVL 1150
Cdd:cd03231 165 AEAMAGHCARGGMVVLTthQDLGLSEAGARELDL 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
951-1168 |
1.61e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 951 YRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDG--CDLREFDVDGYRNRLGIVTQ--EQ 1026
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQdpEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 YVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITAldNGYLHQVTaggRNLSAGQLQLLALARARLVDPDILLLDEA 1106
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA--QHFRHQPI---QCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1107 TVALDPATE----AVVQRatlTLAARRTTLIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTELLAAG 1168
Cdd:PRK13638 164 TAGLDPAGRtqmiAIIRR---IVAQGNHVIISSHDIdLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-545 |
2.15e-13 |
|
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: 68.63 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLatrcydvtqgavrIGGQDVREltldslrsaiglv 413
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKL-------------IAGELEPD------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 pedavlfSGTIganiaygrpdatpeQIATAARAAHIEEfvntlpdgyqtavgargltLSGGQRQRIALARALLHQPRLLI 493
Cdd:cd03221 54 -------EGIV--------------TWGSTVKIGYFEQ-------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 494 MDDPTSAVDavIECgiQEVLREAIAD-RTAVIF-TRRRSML-TLADRVAVLDSGR 545
Cdd:cd03221 94 LDEPTNHLD--LES--IEALEEALKEyPGTVILvSHDRYFLdQVATKIIELEDGK 144
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
346-558 |
2.47e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQ--DVRELTLDSLRSAIGLVPEDA--VLFS 421
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 422 GTIGANIAYG-RPDATPEqiATAARAAhieefvntlpDGYQTAVGARGL------TLSGGQRQRIALARALLHQPRLLIM 494
Cdd:PRK13638 93 TDIDSDIAFSlRNLGVPE--AEITRRV----------DEALTLVDAQHFrhqpiqCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 495 DDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLT--LADRVAVLDSGRLLDVGTPDEVWER 558
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyeISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
932-1165 |
2.54e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 932 ARPVGTLRGEVV-FDAVHYSYRTRevPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREf 1010
Cdd:PRK13536 31 ASIPGSMSTVAIdLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1011 DVDGYRNRLGIVTQ-EQYVFAGTVRD-AIAYGRpdatdaQVERAAREVGAhPMITALDNGYLH-QVTAGGRNLSAGQLQL 1087
Cdd:PRK13536 108 RARLARARIGVVPQfDNLDLEFTVREnLLVFGR------YFGMSTREIEA-VIPSLLEFARLEsKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1088 LALARARLVDPDILLLDEATVALDP-ATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELL 1165
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPhARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
349-503 |
2.66e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 71.41 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvrELTL--DSLRSA-IGLVPEDAvlfSGTIG 425
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYgdYKYRCKhIRMIFQDP---NTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 426 ANIAYGRPDATPEQIAT----AARAAHIEE---FVNTLPDGYQTAVGarglTLSGGQRQRIALARALLHQPRLLIMDDPT 498
Cdd:COG4167 102 PRLNIGQILEEPLRLNTdltaEEREERIFAtlrLVGLLPEHANFYPH----MLSSGQKQRVALARALILQPKIIIADEAL 177
|
....*
gi 1108176189 499 SAVDA 503
Cdd:COG4167 178 AALDM 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
940-1157 |
2.67e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 940 GEVVFDA--VHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVdgcdlrefdvdGYRN 1017
Cdd:COG0488 312 GKKVLELegLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-----------GETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1018 RLGIVTQEQYVFAG--TVRDAIAYGRPDATDAQV-----------ERAAREVGAhpmitaldngylhqvtaggrnLSAGQ 1084
Cdd:COG0488 379 KIGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVrgylgrflfsgDDAFKPVGV---------------------LSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1085 LQLLALARARLVDPDILLLDEATVALDPATeavvqRATLTLAARR---TTLIVAH--GLaIAEHADRIVVLEHGTVVE 1157
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIET-----LEALEEALDDfpgTVLLVSHdrYF-LDRVATRILEFEDGGVRE 509
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
934-1159 |
3.54e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.67 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 934 PVGTLRGevvfdaVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLRefDVD 1013
Cdd:PRK09452 13 PLVELRG------ISKSFDGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1014 GYRNRLGIVTQEQYVFAG-TVRDAIAYG-----RPDA-TDAQVERAAREVgahpMITALDNGYLHQvtaggrnLSAGQLQ 1086
Cdd:PRK09452 83 AENRHVNTVFQSYALFPHmTVFENVAFGlrmqkTPAAeITPRVMEALRMV----QLEEFAQRKPHQ-------LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1087 LLALARARLVDPDILLLDEATVALDPATEAVVQratLTLAA-RRTTLI----VAHGlaiAEHA----DRIVVLEHGTVVE 1157
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQ---NELKAlQRKLGItfvfVTHD---QEEAltmsDRIVVMRDGRIEQ 225
|
..
gi 1108176189 1158 DG 1159
Cdd:PRK09452 226 DG 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
364-556 |
6.12e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 364 AVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQdvrelTLDSLRSAIGLVPE---------DAVLFSG-TIGANIAYGRP 433
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-----VLFDAEKGICLPPEkrrigyvfqDARLFPHyKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 434 DATPEQIATAARAAHIEEFVNTLPdgyqtavgargLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD--------AVI 505
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellPYL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 506 ECGIQEVlreaiadRTAVIFTrRRSM---LTLADRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK11144 172 ERLAREI-------NIPILYV-SHSLdeiLRLADRVVVLEQGKVKAFGPLEEVW 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
332-572 |
6.15e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGYVADRP----VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLD--- 404
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 405 -SLRSAIGLV---PEdAVLFSGTIGANIAYGrpdatPEQIATAARAAHIEEFVNTLPDGYQTAVGARG-LTLSGGQRQRI 479
Cdd:PRK13646 81 rPVRKRIGMVfqfPE-SQLFEDTVEREIIFG-----PKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTLA---DRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVAryaDEVIVMKEGSIVSQTSPKELF 234
|
250
....*....|....*.
gi 1108176189 557 ERCPRYRELLSPAPDL 572
Cdd:PRK13646 235 KDKKKLADWHIGLPEI 250
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
337-503 |
6.30e-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: 73.05 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 337 QRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLATRcYD---VTQGAVRIG----------GQDVR 399
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKD-FNgeaRPQPGIKVGylpqepqldpTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 400 ELTLDSLRSAIGLVPE-DAVlfsgtigaNIAYGRPDAtpEQIATAARAAHIEEFVNTLpDGY----QTAVGARGL----- 469
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRfNEI--------SAKYAEPDA--DFDKLAAEQAELQEIIDAA-DAWdldsQLEIAMDALrcppw 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1108176189 470 -----TLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA 503
Cdd:TIGR03719 156 dadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 194
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
345-567 |
6.69e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 345 ADRPVLREISLSVRAGETLAVVGAPGSGKS--TLASLATRCYDVTQ--GAVRIGGQDVRELTLDSLRSA-IGLVPEDAVL 419
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltCAAALGILPAGVRQtaGRVLLDGKPVAPCALRGRKIAtIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 420 FSGTIGAN-----IAYGRPdATPEQIATAARAAHIEEfVNTLPDGYQtavgargLTLSGGQRQRIALARALLHQPRLLIM 494
Cdd:PRK10418 94 PLHTMHTHaretcLALGKP-ADDATLTAALEAVGLEN-AARVLKLYP-------FEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 495 DDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSM---LTLADRVAVLDSGRLLDVGTPDEVWERcPRY---RELLS 567
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMgvvARLADDVAVMSHGRIVEQGDVETLFNA-PKHavtRSLVS 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
956-1164 |
7.52e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDvDGYRNRLGI--VTQEQYVFAG-T 1032
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1033 VRDAIAYG--RPDATDAQVERAAREVGAHpmitaLDngyLHqVTAGgrNLSAGQLQLLALARARLVDPDILLLDEATVAL 1110
Cdd:PRK15439 103 VKENILFGlpKRQASMQKMKQLLAALGCQ-----LD---LD-SSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1111 DPA-TEAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK15439 172 TPAeTERLFSRIRELLAQGVGIVFISHKLPeIRQLADRISVMRDGTIALSGKTADL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
955-1168 |
8.39e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYV-FAGTV 1033
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 RDAIAYGRP----------DATDAQVERAAREVGAHPMITaldngylHQVTAggrnLSAGQLQLLALARARLVDPDILLL 1103
Cdd:PRK09536 95 RQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFAD-------RPVTS----LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1104 DEATVALDpateavVQRA--TLTLAAR-----RTTLIVAHGLAI-AEHADRIVVLEHGTVVEDGAHTELLAAG 1168
Cdd:PRK09536 164 DEPTASLD------INHQvrTLELVRRlvddgKTAVAAIHDLDLaARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
959-1167 |
1.15e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAG-TVRDAI 1037
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGmTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYGR----------PDATDAQVERAAREVGAHPMITALDNgylhqvtaggrNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:PRK10575 107 AIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1108 VALDPATEAVVQRATLTLAARR--TTLIVAHGLAI-AEHADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERglTVIAVLHDINMaARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
350-570 |
1.85e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTL-ASLATRCY-DVT-QGAVRIGGqdvRELTLDSLRSAIGLVPEDAvLFSGTIGA 426
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLmNALAFRSPkGVKgSGSVLLNG---MPIDAKEMRAISAYVQQDD-LFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 N-----IAYGRpdaTPEQIATAARAAHIEEFVN--TLPDGYQTAVGARGLT--LSGGQRQRIALARALLHQPRLLIMDDP 497
Cdd:TIGR00955 117 RehlmfQAHLR---MPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 498 TSAVDAVIECGIQEVLREAIADRTAVIFTRRR---SMLTLADRVAVLDSGRLLDVGTPDEVwerCPRYRELLSPAP 570
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpssELFELFDKIILMAEGRVAYLGSPDQA---VPFFSDLGHPCP 266
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
962-1164 |
1.86e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 962 INLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVdgyRNR-LGIVTQEQYVFAG-TVRDAIAY 1039
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI---QQRdICMVFQSYALFPHmSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1040 GRPDATDAQVERAAREVGAHPMI--TALDNGYLHQVtaggrnlSAGQLQLLALARARLVDPDILLLDEATVALDpateav 1117
Cdd:PRK11432 102 GLKMLGVPKEERKQRVKEALELVdlAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLD------ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1118 vqrATLTLAARR-----------TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK11432 169 ---ANLRRSMREkirelqqqfniTSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
353-570 |
1.94e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT---LDSLRSAIGLVPED---AVLFSGTIGA 426
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyaSLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYG-RPDATPEQIATAARAAHIEEFVNTLPDG---YQTAvgargltLSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:PRK10261 423 SIMEPlRVHGLLPGKAAAARVAWLLERVGLLPEHawrYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 503 AVIECGIQEVLREAIADR-TAVIFTRRRSMLT--LADRVAVLDSGRLLDVGTPDEVWE--RCPRYRELLSPAP 570
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFgIAYLFISHDMAVVerISHRVAVMYLGQIVEIGPRRAVFEnpQHPYTRKLMAAVP 568
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
346-558 |
2.63e-12 |
|
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: 70.99 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASL--ATRCYDVTQGAV-----------------RIG------GQDVRE 400
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVlrGMDQYEPTSGRIiyhvalcekcgyverpsKVGepcpvcGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 401 LTLD------------SLRSAIGLVPEDAVLFSGTIGANIAYGRPDATPEQIATAARAAHIEEFVNTlpdGYQTAVGARg 468
Cdd:TIGR03269 92 EEVDfwnlsdklrrriRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL---SHRITHIAR- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 469 lTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR--TAVIFTRRRSMLT-LADRVAVLDSGR 545
Cdd:TIGR03269 168 -DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEdLSDKAIWLENGE 246
|
250
....*....|...
gi 1108176189 546 LLDVGTPDEVWER 558
Cdd:TIGR03269 247 IKEEGTPDEVVAV 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
956-1156 |
3.01e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlREFDVDGYR--NRLGI--VTQEqyvF-- 1029
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRdaIALGIgmVHQH---Fml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 --AGTVRDAIAYGRPDATDAQVERAArevgAHPMITALDNGY-----LHQVTAggrNLSAGQLQLLALARARLVDPDILL 1102
Cdd:COG3845 92 vpNLTVAENIVLGLEPTKGGRLDRKA----ARARIRELSERYgldvdPDAKVE---DLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1103 LDEATVALDPA-TE---AVVQRatltLAARRTT-LIVAHGLA-IAEHADRIVVLEHGTVV 1156
Cdd:COG3845 165 LDEPTAVLTPQeADelfEILRR----LAAEGKSiIFITHKLReVMAIADRVTVLRRGKVV 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
944-1167 |
3.02e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 944 FDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGIVT 1023
Cdd:PRK13537 10 FRNVEKRYGDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1024 QEQYVFAG-TVRDAI-AYGRPDATDAQVERAArevgahpMITALDNGYLHQ-VTAGGRNLSAGQLQLLALARARLVDPDI 1100
Cdd:PRK13537 87 QFDNLDPDfTVRENLlVFGRYFGLSAAAARAL-------VPPLLEFAKLENkADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1101 LLLDEATVALDP-ATEAVVQRATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:PRK13537 160 LVLDEPTTGLDPqARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
946-1166 |
3.71e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 946 AVHYSyrtrEVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG-YRNRLGIVTQ 1024
Cdd:PRK11614 12 SAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1025 EQYVFAG-TVRDAIAYGRPDATDAQV-ERAAREVGAHPMItaldngYLHQVTAGGrNLSAGQLQLLALARARLVDPDILL 1102
Cdd:PRK11614 88 GRRVFSRmTVEENLAMGGFFAERDQFqERIKWVYELFPRL------HERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1103 LDEATVALDPateAVVQRATLTLAARR----TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK11614 161 LDEPSLGLAP---IIIQQIFDTIEQLReqgmTIFLVEQNANQAlKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-502 |
3.94e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRiggqdvREltlDSLRsaIG 411
Cdd:PRK09544 5 VSLENVSVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RN---GKLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPE----DAVLfSGTIGANIAYgRPDATPEQIATA---ARAAHIEEFVNTlpdgyqtavgarglTLSGGQRQRIALARA 484
Cdd:PRK09544 71 YVPQklylDTTL-PLTVNRFLRL-RPGTKKEDILPAlkrVQAGHLIDAPMQ--------------KLSGGETQRVLLARA 134
|
170
....*....|....*...
gi 1108176189 485 LLHQPRLLIMDDPTSAVD 502
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVD 152
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
955-1135 |
5.73e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVdgyrnrlgivtQEQYVFAG--- 1031
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-----------AEACHYLGhrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 ------TVRDAIAYGRP--DATDAQVERAAREVGAHPmITALDNGYlhqvtaggrnLSAGQLQLLALARARLVDPDILLL 1103
Cdd:PRK13539 83 amkpalTVAENLEFWAAflGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 1108176189 1104 DEATVALDPATEAVVQRATLTLAARRTTLIVA 1135
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
347-544 |
6.02e-12 |
|
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: 65.98 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGA 426
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYGRPDATPEQIATAARAAHIeefvntlpDGYQTAVGArglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIE 506
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGL--------NGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1108176189 507 CGIQEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSG 544
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
335-555 |
6.68e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.03 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV-----REL--TLDSLR 407
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsRELakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 408 SAIGLVP----EDAVLF-----SGtiganiayGRPdatpeqiaTAARAAHIEEfvntlpdgyqtAVGARGLT-------- 470
Cdd:COG4604 82 QENHINSrltvRELVAFgrfpySK--------GRL--------TAEDREIIDE-----------AIAYLDLEdladryld 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 471 -LSGGQRQRIALARALLHQPRLLIMDDPTSAVD---AViecGIQEVLREAiAD---RTAVI------FTRRrsmltLADR 537
Cdd:COG4604 135 eLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhSV---QMMKLLRRL-ADelgKTVVIvlhdinFASC-----YADH 205
|
250
....*....|....*...
gi 1108176189 538 VAVLDSGRLLDVGTPDEV 555
Cdd:COG4604 206 IVAMKDGRVVAQGTPEEI 223
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
639-918 |
6.99e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 67.88 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 639 CAGLLPPL-----------LIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAH 707
Cdd:cd18577 10 AAGAALPLmtivfgdlfdaFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 708 AQRLGLDAFEDDGDAQIVTAVTADVEAIvaflRTG----LVVAVISVVTLV-GILVALlaIR-ARLVLLIFTTMPVLALA 781
Cdd:cd18577 90 LLRQDIAWFDKNGAGELTSRLTSDTNLI----QDGigekLGLLIQSLSTFIaGFIIAF--IYsWKLTLVLLATLPLIAIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 782 TWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSL 861
Cdd:cd18577 164 GGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 862 ATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18577 244 MYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
958-1166 |
8.17e-12 |
|
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: 69.06 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLV--ARFYDPTHGTV-----------RVD------------GCDLREFDV 1012
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVErpskvgepcpvcGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1013 D----------GYRNRLGIVTQEQYVFAG--TVRDAIAYGRPDA---TDAQVERAARevgahpMITALDNGylHQVTAGG 1077
Cdd:TIGR03269 95 DfwnlsdklrrRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIgyeGKEAVGRAVD------LIEMVQLS--HRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1078 RNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAH-GLAIAEHADRIVVLEHGT 1154
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHwPEVIEDLSDKAIWLENGE 246
|
250
....*....|..
gi 1108176189 1155 VVEDGAHTELLA 1166
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
969-1151 |
8.23e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.66 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 969 GQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDlrefdvdgyrnrlgIVTQEQYV---FAGTVRDAIAYGRPDA- 1044
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--------------VSYKPQYIkadYEGTVRDLLSSITKDFy 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1045 TDAQVEraaREVgAHPMitALDNGYLHQVTaggrNLSAGQLQLLALARARLVDPDILLLDEATVALDpateaVVQRATLT 1124
Cdd:cd03237 91 THPYFK---TEI-AKPL--QIEQILDREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-----VEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1108176189 1125 LAARR-------TTLIVAHGLAIAEH-ADRIVVLE 1151
Cdd:cd03237 156 KVIRRfaennekTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
348-546 |
1.01e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLRE-ISLSVRAGETLAVVGAPGSGKSTLASL---ATRCydvTQGAVRIGGQDVR-ELTLDSLRSAIGLVPEDAVlFSG 422
Cdd:PRK11288 266 PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLlygATRR---TAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDRK-AEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TI-GANIAygrpdatpEQIATAARAAHI---------------EEFVNTL----PDGYQTAVgarglTLSGGQRQRIALA 482
Cdd:PRK11288 342 IIpVHSVA--------DNINISARRHHLragclinnrweaenaDRFIRSLniktPSREQLIM-----NLSGGNQQKAILG 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSM--LTLADRVAVLDSGRL 546
Cdd:PRK11288 409 RWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPevLGVADRIVVMREGRI 474
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-565 |
1.14e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKST----LASLATRcydvTQGAVRIGGQDVRELTLDSLRSaIGLV------------ 413
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILVP----TSGEVRVLGYVPFKRRKEFARR-IGVVfgqrsqlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSGTIganiaYGRPDAtpeqiataARAAHIEEFVNTL--PDGYQTAVgaRglTLSGGQRQRIALARALLHQPRL 491
Cdd:COG4586 113 AIDSFRLLKAI-----YRIPDA--------EYKKRLDELVELLdlGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 492 LIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFtrrrsmLT---------LADRVAVLDSGRLLDVGTPDEVWERCPRY 562
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERGTTIL------LTshdmddieaLCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
...
gi 1108176189 563 REL 565
Cdd:COG4586 250 KTI 252
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
27-278 |
1.68e-11 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 66.35 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 27 ALAGTVIAVL-VPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATY-LLTYVRRYYGGRIAHLVQHDLRMDAFQALLRWD 104
Cdd:cd18575 4 ALLIAAAATLaLGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLaLASALRFYLVSWLGERVVADLRKAVFAHLLRLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 105 GRQQDRWSSGQLIVRTTNDLQLVQALL-FDVPNVLRHVLTLLLGVAVMTW----LSVPLALLAVLLVPVIGLIAHRSRRL 179
Cdd:cd18575 84 PSFFETTRTGEVLSRLTTDTTLIQTVVgSSLSIALRNLLLLIGGLVMLFItspkLTLLVLLVIPLVVLPIILFGRRVRRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 180 laaaTHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAhfgpLLQTLPALGQMAVFA 259
Cdd:cd18575 164 ----SRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARA----LLTALVIFLVFGAIV 235
|
250 260
....*....|....*....|...
gi 1108176189 260 LGGWMAAQ----GSITVGTFVAF 278
Cdd:cd18575 236 FVLWLGAHdvlaGRMSAGELSQF 258
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
646-918 |
1.78e-11 |
|
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: 66.53 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 646 LLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIV 725
Cdd:cd18561 17 WLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 726 TAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIR--ARLVLLIFTTMPVLALATWQFRRAS-NWTYRRARHRLGt 802
Cdd:cd18561 97 TTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDplVALILLVFALLIPLSPALWDRLAKDtGRRHWAAYGRLS- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 803 vtATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVG 882
Cdd:cd18561 176 --AQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLS 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 1108176189 883 ALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18561 254 SLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
347-503 |
2.19e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 64.30 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGA 426
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYGRPDATPEQIAtaaraahieefvntlPDGYQTAVGARGLT------LSGGQRQRIALARALLHQPRLLIMDDPTSA 500
Cdd:TIGR01189 93 NLHFWAAIHGGAQRT---------------IEDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
...
gi 1108176189 501 VDA 503
Cdd:TIGR01189 158 LDK 160
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
693-1157 |
2.19e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 693 GEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAI-VAFLRtgLVVAVISVVTLVGILVALLAIRARLVLLi 771
Cdd:PRK10522 76 GHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNItIAFVR--LPELVQGIILTLGSAAYLAWLSPKMLLV- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 772 ftTMPVLALATWqfrrASNWTYRRARHRLGTVTAT----LREYAAGL--RIAQAF---RAEYRGLQSYFAHSDDYRRLGV 842
Cdd:PRK10522 153 --TAIWMAVTIW----GGFVLVARVYKHMATLRETedklYNDYQTVLegRKELTLnreRAEYVFENEYEPDAQEYRHHII 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 843 RGQ--RLLALYYPFVALLCSLATTLVLLDGArevraGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRS 920
Cdd:PRK10522 227 RADtfHLSAVNWSNIMMLGAIGLVFYMANSL-----GWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 921 L-LSTRTPSSPAARPVGTLRgEVVFDAVHYSYRTREVpALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGT 999
Cdd:PRK10522 302 LaLAPYKAEFPRPQAFPDWQ-TLELRNVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1000 VRVDGCDLREFDVDGYRNRLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAarevgahpmitaldnGYLHQVT-AGGR 1078
Cdd:PRK10522 380 ILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPANPALVEKWLERL---------------KMAHKLElEDGR 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1079 ----NLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTL--AARRTTLIVAHGLAIAEHADRIVVLEH 1152
Cdd:PRK10522 445 isnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRN 524
|
....*
gi 1108176189 1153 GTVVE 1157
Cdd:PRK10522 525 GQLSE 529
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
693-918 |
2.19e-11 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family 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. 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. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 66.12 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 693 GEQVLFRLRSVVFAH--AQRLGLdaFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLL 770
Cdd:cd18780 70 GERVVARLRKRLFSAiiAQEIAF--FDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 771 IFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLAL 850
Cdd:cd18780 148 MLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 851 YYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18780 228 FNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
962-1167 |
2.46e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 962 INLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQYVFAG-TVRDAIAYG 1040
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1041 R----PDAT------DAQVERAAREVGahpmITALDNGYLHqvtaggrNLSAGQLQLLALARARLVDPDILLLDEATVAL 1110
Cdd:PRK10253 106 RyphqPLFTrwrkedEEAVTKAMQATG----ITHLADQSVD-------TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 1111 DPATE--------AVVQRATLTLAArrttliVAHGLAIA-EHADRIVVLEHGTVVEDGAHTELLAA 1167
Cdd:PRK10253 175 DISHQidllellsELNREKGYTLAA------VLHDLNQAcRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
638-918 |
3.87e-11 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 65.54 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 638 TCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFE 717
Cdd:cd18570 15 TLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 718 --DDGDaqIVTAVTaDVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRasnwTYRR 795
Cdd:cd18570 95 trKTGE--IISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNK----PFKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 796 ARHRL----GTVTATLREYAAGLRIAQAFRAE---YRGLQSYFahsDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLL 868
Cdd:cd18570 168 KNREVmesnAELNSYLIESLKGIETIKSLNAEeqfLKKIEKKF---SKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILW 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1108176189 869 DGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18570 245 IGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
958-1173 |
4.77e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKST----LIKLVArfydpTHGTVRVDGCDLREFDVDG---YRNRLGIVTQEQYVFA 1030
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 G---TVRDAIAYG----RPDATDAQVE----RAAREVGahpmitaLDNGYLHQVTAggrNLSAGQLQLLALARARLVDPD 1099
Cdd:PRK15134 376 NprlNVLQIIEEGlrvhQPTLSAAQREqqviAVMEEVG-------LDPETRHRYPA---EFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1100 ILLLDEATVALDPAteavVQRATLTLAA------RRTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGGH-Y 1171
Cdd:PRK15134 446 LIILDEPTSSLDKT----VQAQILALLKslqqkhQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQeY 521
|
..
gi 1108176189 1172 SR 1173
Cdd:PRK15134 522 TR 523
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
946-1113 |
4.94e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 63.15 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 946 AVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRLGIVTQE 1025
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1026 QYVFAGTVRDAIAYGRPDATDAQ--VERAAREVGahpmITALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDILLL 1103
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIHGGAQrtIEDALAAVG----LTGFEDLPAAQ-------LSAGQQRRLALARLWLSRRPLWIL 151
|
170
....*....|
gi 1108176189 1104 DEATVALDPA 1113
Cdd:TIGR01189 152 DEPTTALDKA 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
956-1159 |
6.79e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFD-VDGYRNRLGIVTQEQYVFAG-TV 1033
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQELSVIDElTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 RDAIAYGRpdatdaqveRAAREVGAHPMItalDNGYLHQVTA------GGR--------NLSAGQLQLLALARARLVDPD 1099
Cdd:PRK09700 98 LENLYIGR---------HLTKKVCGVNII---DWREMRVRAAmmllrvGLKvdldekvaNLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1100 ILLLDEATVALdpaTEAVVQRATLTLAARRT--TLIV--AHGLA-IAEHADRIVVLEHGTVVEDG 1159
Cdd:PRK09700 166 VIIMDEPTSSL---TNKEVDYLFLIMNQLRKegTAIVyiSHKLAeIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
334-496 |
7.57e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSGTIGaniaygrpdatPEqiATAARAAHIEEFVNTLPDGYQTAV-GARGLT--LSGGQRQRIALARALLHQPR 490
Cdd:PRK10522 403 FTDFHLFDQLLG-----------PE--GKPANPALVEKWLERLKMAHKLELeDGRISNlkLSKGQKKRLALLLALAEERD 469
|
....*.
gi 1108176189 491 LLIMDD 496
Cdd:PRK10522 470 ILLLDE 475
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
334-555 |
9.06e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 9.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLV 413
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLFSG-TIGANIAYGRPDATP----------EQIATAARAAHIEEFVNTLPDgyqtavgarglTLSGGQRQRIALA 482
Cdd:PRK10253 87 AQNATTPGDiTVQELVARGRYPHQPlftrwrkedeEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADR---TAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgytLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
325-528 |
1.03e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 325 PLSPEARLSLEfqrvSFGYVAD---RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIggqDVREL 401
Cdd:COG2401 22 DLSERVAIVLE----AFGVELRvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---DVPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 402 TLDSLRSAIglvpeDAVlfsgtiganiayGRPDATPEQIATAARAahieefvntlpdGYQTAVG--ARGLTLSGGQRQRI 479
Cdd:COG2401 95 QFGREASLI-----DAI------------GRKGDFKDAVELLNAV------------GLSDAVLwlRRFKELSTGQKFRF 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 480 ALARALLHQPRLLIMDDPTSAVDA----VIECGIQEVLREaiADRTAVIFTRR 528
Cdd:COG2401 146 RLALLLAERPKLLVIDEFCSHLDRqtakRVARNLQKLARR--AGITLVVATHH 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
950-1157 |
1.06e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFY--DPTHGTVRVDgcdlrefDVDGYRNRLGIvtqeqy 1027
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------DNQFGREASLI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 vfagtvrDAIayGRPDATDAQVERAAReVGahpmitaLDNGYLHQvtAGGRNLSAGQLQLLALARARLVDPDILLLDEAT 1107
Cdd:COG2401 104 -------DAI--GRKGDFKDAVELLNA-VG-------LSDAVLWL--RRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1108 VALDPATEAVVQRATLTLAARR-TTLIVA-HGLAIAE--HADRIVVLEHGTVVE 1157
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAgITLVVAtHHYDVIDdlQPDLLIFVGYGGVPE 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
338-515 |
1.22e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 338 RVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSLrsaIGLVP--- 414
Cdd:PRK15056 11 DVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPqse 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 ----------EDAVLFsGTIGANIAYGRPDATPEQIATAARAAhieefVNTLpDGYQTAVGArgltLSGGQRQRIALARA 484
Cdd:PRK15056 88 evdwsfpvlvEDVVMM-GRYGHMGWLRRAKKRDRQIVTAALAR-----VDMV-EFRHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190
....*....|....*....|....*....|.
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAVIECGIQEVLRE 515
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
346-542 |
1.45e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLATRcydvTQGAVRIGGQDVRELTlDSLRSA---IG------- 411
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLlrilAGLARP----DAGEVLWQGEPIRRQR-DEYHQDllyLGhqpgikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 -LVPEDAVLFSGTIGAniaygrpDATPEQIATAARAAHIEEFVNtLPDGyqtavgarglTLSGGQRQRIALARALLHQPR 490
Cdd:PRK13538 88 eLTALENLRFYQRLHG-------PGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 491 LLIMDDPTSAVD--AViecgiqEVLREAIADRTA----VIFTRRRSMLTLADRVAVLD 542
Cdd:PRK13538 150 LWILDEPFTAIDkqGV------ARLEALLAQHAEqggmVILTTHQDLPVASDKVRKLR 201
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
642-890 |
1.58e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 63.63 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 642 LLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDD-- 719
Cdd:cd18567 19 LASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRhl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 720 GDaqIVTAVTAdVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRAsnwtYRRARHR 799
Cdd:cd18567 99 GD--IVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPP----LRRATEE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 800 LGTVTA--------TLReyaaGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGA 871
Cdd:cd18567 172 QIVASAkeqshfleTIR----GIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGA 247
|
250
....*....|....*....
gi 1108176189 872 REVRAGVISVGALVTYLLY 890
Cdd:cd18567 248 LLVLDGEFTVGMLFAFLAY 266
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
956-1166 |
1.63e-10 |
|
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: 65.21 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRV----DGCDLREFDVDGyRNR----LGIVTQEQY 1027
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG-RGRakryIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 VFA-----GTVRDAIAYGRPD--ATDAQV---------ERAAREVgahpmitaLDNgYLHQvtaggrnLSAGQLQLLALA 1091
Cdd:TIGR03269 376 LYPhrtvlDNLTEAIGLELPDelARMKAVitlkmvgfdEEKAEEI--------LDK-YPDE-------LSEGERHRVALA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1092 RARLVDPDILLLDEATVALDPATEavVQRATLTLAAR----RTTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITK--VDVTHSILKAReemeQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
340-544 |
1.69e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGYVadrPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGLVPEDAV 418
Cdd:PRK15439 20 QYSGV---EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 419 LFSG-TIGANIAYGRPdatpeqiATAARAAHIEEFVNTLpdGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDP 497
Cdd:PRK15439 97 LFPNlSVKENILFGLP-------KRQASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1108176189 498 TSAVDAVIECGIQEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSG 544
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFIshKLPEIRQLADRISVMRDG 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
337-503 |
1.99e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 337 QRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTL----ASLATrcydVTQGAVR------IG----------GQ 396
Cdd:PRK11819 10 NRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDK----EFEGEARpapgikVGylpqepqldpEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 397 DVRELTLDSLRSAIGLVPE-DAVlfsgtigaNIAYGRPDATPEqiATAARAAHIEEFVNT------------------LP 457
Cdd:PRK11819 86 TVRENVEEGVAEVKAALDRfNEI--------YAAYAEPDADFD--ALAAEQGELQEIIDAadawdldsqleiamdalrCP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1108176189 458 DGyQTAVGarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA 503
Cdd:PRK11819 156 PW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
959-1158 |
2.13e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGyRNRL-----GIVTQeQYVFAGTV 1033
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA-RAKLrakhvGFVFQ-SFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 RDAIAYGRPDATDAQVERAAREvGAHPMITALDNG-YLHQVTAggrNLSAGQLQLLALARARLVDPDILLLDEATVALDP 1112
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRN-GAKALLEQLGLGkRLDHLPA---QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1113 ATEAVVqrATLTLAARR---TTLI-VAHGLAIAEHADRIVVLEHGTVVED 1158
Cdd:PRK10584 180 QTGDKI--ADLLFSLNRehgTTLIlVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
324-555 |
2.24e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 324 KPLSPEARLSLEfqRVSFGyVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTL 403
Cdd:PRK10575 4 YTNHSDTTFALR--NVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 404 DSLRSAIGLVPEDAVLFSG-TIGANIAYGR----------PDATPEQIATAARAAHIEEFVNTLPDgyqtavgarglTLS 472
Cdd:PRK10575 81 KAFARKVAYLPQQLPAAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 473 GGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECgiqEVLreAIADRtaviFTRRRSMLTLA------------DRVAV 540
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV---DVL--ALVHR----LSQERGLTVIAvlhdinmaarycDYLVA 220
|
250
....*....|....*
gi 1108176189 541 LDSGRLLDVGTPDEV 555
Cdd:PRK10575 221 LRGGEMIAQGTPAEL 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
346-546 |
2.53e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGLVPE---DAVLFS 421
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 422 G-TIGANIAYGRP--------------DATPEQIATAARA------AHIEEFVNtlpdgyqtavgarglTLSGGQRQRIA 480
Cdd:PRK09700 355 NfSIAQNMAISRSlkdggykgamglfhEVDEQRTAENQREllalkcHSVNQNIT---------------ELSGGNQQKVL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 481 LARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREaIADRTAVIF---TRRRSMLTLADRVAVLDSGRL 546
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILmvsSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
942-1154 |
2.54e-10 |
|
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: 59.77 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyrnrlgi 1021
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 vtqeqyvfagtvrdaiaygrpdatdaqveraarevgahpmitALDNGYLHQvtaggrnLSAGQLQLLALARARLVDPDIL 1101
Cdd:cd03221 62 ------------------------------------------TVKIGYFEQ-------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1102 LLDEATVALDPATEAVVQRATLTLaaRRTTLIVAHGLA-IAEHADRIVVLEHGT 1154
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
345-546 |
3.27e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 345 ADRPVLREISLSVRAGETLAVVGAPGSGKSTLA-SLATRCYDV-TQGAVRIGGQDVReltLDSLRSAI--GL--VPED-- 416
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVD---VSTVSDAIdaGLayVTEDrk 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 --AVLFSGTIGANIAYgrpdATPEQIATAA--------RAAhiEEFVNTL----PDGYQTAVgarglTLSGGQRQRIALA 482
Cdd:NF040905 348 gyGLNLIDDIKRNITL----ANLGKVSRRGvideneeiKVA--EEYRKKMniktPSVFQKVG-----NLSGGNQQKVVLS 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 483 RALLHQPRLLIMDDPTSAVD--AVIEcgIQEVLREAIADRTAVIFTrrrS-----MLTLADRVAVLDSGRL 546
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDvgAKYE--IYTIINELAAEGKGVIVI---SselpeLLGMCDRIYVMNEGRI 482
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
958-1159 |
3.62e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.93 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL---------REFDVDGYRN-RLG------- 1020
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiaRMGVVRTFQHvRLFremtvie 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1021 --IVTQEQYV----FAGTVRDAiAYGRpdATDAQVERAA---REVGahpmITALDNGylhqvTAGgrNLSAGQLQLLALA 1091
Cdd:PRK11300 100 nlLVAQHQQLktglFSGLLKTP-AFRR--AESEALDRAAtwlERVG----LLEHANR-----QAG--NLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1092 RARLVDPDILLLDEATVALDPateavvqRATLTLAARRTTLIVAHGLAI--AEH--------ADRIVVLEHGTVVEDG 1159
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNP-------KETKELDELIAELRNEHNVTVllIEHdmklvmgiSDRIYVVNQGTPLANG 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
349-555 |
4.64e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.41 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTL-----ASL------------------ATRCYDVTQGAVRIGGQDVRELT-LD 404
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFiehlnALLlpdtgtiewifkdeknkkKTKEKEKVLEKLVIQKTRFKKIKkIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 405 SLRSAIGLVPEDA--VLFSGTIGANIAYG-RPDATPEQIATAaRAAHIEEFVNtLPDGYqtaVGARGLTLSGGQRQRIAL 481
Cdd:PRK13651 102 EIRRRVGVVFQFAeyQLFEQTIEKDIIFGpVSMGVSKEEAKK-RAAKYIELVG-LDESY---LQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAViecGIQEVLReaIAD------RTAVIFTRR-RSMLTLADRVAVLDSGRLLDVGTPDE 554
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQ---GVKEILE--IFDnlnkqgKTIILVTHDlDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
.
gi 1108176189 555 V 555
Cdd:PRK13651 252 I 252
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
962-1163 |
4.73e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 962 INLRIPA-GQTVVFvGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLreFDVDG------YRNRLGIVTQEQYVFAG-TV 1033
Cdd:PRK11144 17 VNLTLPAqGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKgiclppEKRRIGYVFQDARLFPHyKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 RDAIAYGRPDATDAQVERAAREVGahpmITALDNGYLHqvtaggrNLSAGQLQLLALARARLVDPDILLLDEATVALD-- 1111
Cdd:PRK11144 94 RGNLRYGMAKSMVAQFDKIVALLG----IEPLLDRYPG-------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlp 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1112 ------PATEavvqratlTLAARRTT--LIVAHGL-AIAEHADRIVVLEHGTVVEDGAHTE 1163
Cdd:PRK11144 163 rkrellPYLE--------RLAREINIpiLYVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
353-576 |
5.15e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.62 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKSTLAS----LATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGlvPEDAVLF-------- 420
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKaicgITKDNWHVTADRFRWNGIDLLKLSPRERRKIIG--REIAMIFqepsscld 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 421 -SGTIGANIAYGRPDATPE----QIATAARAAHIEEF-----------VNTLPdgYQtavgargltLSGGQRQRIALARA 484
Cdd:COG4170 104 pSAKIGDQLIEAIPSWTFKgkwwQRFKWRKKRAIELLhrvgikdhkdiMNSYP--HE---------LTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 485 LLHQPRLLIMDDPTSAVDAVIECGIQEVL-REAIADRTAVIFTRR--RSMLTLADRVAVLDSGRLLDVGTPDEVWERC-- 559
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLaRLNQLQGTSILLISHdlESISQWADTITVLYCGQTVESGPTEQILKSPhh 252
|
250
....*....|....*..
gi 1108176189 560 PRYRELLSPAPDLADDL 576
Cdd:COG4170 253 PYTKALLRSMPDFRQPL 269
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
344-555 |
6.58e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 344 VADRPVLREISLSVRAGETLAVVGAPGSGKSTL-ASLA-TRCYdvtQGAVRIGGQDVRELTLDSL-RSAIGLVPEDAVLF 420
Cdd:PRK03695 6 VAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLlARMAgLLPG---SGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 421 SGTIGANIAYGRPDATPeqiaTAARAAHIEEFVNT--LPDGYQTAVGarglTLSGGQRQRIALARALLH-------QPRL 491
Cdd:PRK03695 83 AMPVFQYLTLHQPDKTR----TEAVASALNEVAEAlgLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1108176189 492 LIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLTL--ADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLrhADRVWLLKQGKLLASGRRDEV 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
353-575 |
7.17e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.07 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKStLASLATRCY-----DVTQGAVRIGGQDVRELTLDSLRSAIGlvPEDAVLFSGTIGA- 426
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKS-VSSLAIMGLidypgRVMAEKLEFNGQDLQRISEKERRNLVG--AEVAMIFQDPMTSl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYGRPDATPEQIAT---AARAAHIEEFVNTLpdgyqTAVG----ARGL-----TLSGGQRQRIALARALLHQPRLLIM 494
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVhqgGNKKTRRQRAIDLL-----NQVGipdpASRLdvyphQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 495 DDPTSAVDAVIECGIQEVL-----REAIAdrtAVIFTRRRSMLT-LADRVAVLDSGRLLDVGTPDEVWeRCPRY---REL 565
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLlelqqKENMA---LVLITHDLALVAeAAHKIIVMYAGQVVETGKAHDIF-RAPRHpytQAL 253
|
250
....*....|
gi 1108176189 566 LSPAPDLADD 575
Cdd:PRK11022 254 LRALPEFAQD 263
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
958-1153 |
7.20e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 60.27 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCD---LREFDVDGYRNRLGIVTQEQYVFAG-TV 1033
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHHLLMDrTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1034 RDAIAYGRPDAtDAQVERAAREVGAhpmitALDN-GYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDP 1112
Cdd:PRK10908 97 YDNVAIPLIIA-GASGDDIRRRVSA-----ALDKvGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1108176189 1113 A-TEAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHG 1153
Cdd:PRK10908 171 AlSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDG 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
346-550 |
7.48e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKST-LASLATRCY-DVTQGAVRIGGqdvRELTLDSLRSaIGLVPEDAVLFSG- 422
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTlLNALAGRIQgNNFTGTILANN---RKPTKQILKR-TGFVTQDDILYPHl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TIGANIAYGR----PDATPEQIATAARAAHIEEFvnTLPDGYQTAVG---ARGLtlSGGQRQRIALARALLHQPRLLIMD 495
Cdd:PLN03211 156 TVRETLVFCSllrlPKSLTKQEKILVAESVISEL--GLTKCENTIIGnsfIRGI--SGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 496 DPTSAVDAVIECGIQEVLrEAIADRTAVIFTRRRS----MLTLADRVAVLDSGRLLDVG 550
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTL-GSLAQKGKTIVTSMHQpssrVYQMFDSVLVLSEGRCLFFG 289
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
334-548 |
9.86e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRpVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVR-ELTLDSLRSAIG- 411
Cdd:PRK11288 5 LSFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 ------LVPEdavlfsGTIGANIAYGRpdaTPEQIATAARAAHIEEFVNTL--------PDgyqTAVGarglTLSGGQRQ 477
Cdd:PRK11288 84 iyqelhLVPE------MTVAENLYLGQ---LPHKGGIVNRRLLNYEAREQLehlgvdidPD---TPLK----YLSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 478 RIALARALLHQPRLLIMDDPTSAVDAviecgiQE------VLREAIADRTAVIFTRRR--SMLTLADRVAVLDSGRLLD 548
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSA------REieqlfrVIRELRAEGRVILYVSHRmeEIFALCDAITVFKDGRYVA 220
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
653-839 |
1.08e-09 |
|
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: 60.89 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 653 DVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADV 732
Cdd:cd18584 25 GVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 733 EAIVAFLRTGLVVAVISVVTLVGILVALLAI--RARLVLLIftTMPVL----ALATWQFRRASnwtyRRARHRLGTVTAT 806
Cdd:cd18584 105 DALDGYFARYLPQLVLAAIVPLLILVAVFPLdwVSALILLV--TAPLIplfmILIGKAAQAAS----RRQWAALSRLSGH 178
|
170 180 190
....*....|....*....|....*....|...
gi 1108176189 807 LREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRR 839
Cdd:cd18584 179 FLDRLRGLPTLKLFGRARAQAARIARASEDYRR 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
346-522 |
1.13e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.50 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVrelTLDSLRSAIG-LVPEDAVLFSGTI 424
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHyLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 425 GANIA-----YGRPDATPEQIATAARAAHIEEfvntLPDGYqtavgargltLSGGQRQRIALARALLHQPRLLIMDDPTS 499
Cdd:PRK13539 91 AENLEfwaafLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|...
gi 1108176189 500 AVDAviecGIQEVLREAIADRTA 522
Cdd:PRK13539 157 ALDA----AAVALFAELIRAHLA 175
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
898-1136 |
1.43e-09 |
|
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: 62.46 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 898 IGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGtlRGEVVfdAVHYSYRTREVPA--------LAGINLRIPAG 969
Cdd:TIGR00954 403 VDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPG--RGIVE--YQDNGIKFENIPLvtpngdvlIESLSFEVPSG 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 970 QTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyRNRLGIVTQEQYVFAGTVRDAIAYgrPDATDAQV 1049
Cdd:TIGR00954 479 NNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1050 ERAAREvgaHPMITALDNGYL-HQVTAGG-----RN----LSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQ 1119
Cdd:TIGR00954 546 RRGLSD---KDLEQILDNVQLtHILEREGgwsavQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
250 260
....*....|....*....|...
gi 1108176189 1120 RA------TLTLAARRTTLIVAH 1136
Cdd:TIGR00954 623 RLcrefgiTLFSVSHRKSLWKYH 645
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
332-550 |
1.51e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 332 LSLEFQRVSfgyVADRPVLREISLSVRAGETLAVVGAPGSGKSTL-ASLATR-CYDVTQGAVRIGGQDVRELTldslrsa 409
Cdd:PRK09580 2 LSIKDLHVS---VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGReDYEVTGGTVEFKGKDLLELS------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 410 iglvPEDAvlfSGTiGANIAYGRPDATPEQ-----IATAARAAH----------------IEEFVNTL---PDGYQTAVg 465
Cdd:PRK09580 72 ----PEDR---AGE-GIFMAFQYPVEIPGVsnqffLQTALNAVRsyrgqepldrfdfqdlMEEKIALLkmpEDLLTRSV- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 466 arGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD----AVIECGIQEvLREaiADRTAVIFTRRRSMLTL--ADRVA 539
Cdd:PRK09580 143 --NVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDidalKIVADGVNS-LRD--GKRSFIIVTHYQRILDYikPDYVH 217
|
250
....*....|.
gi 1108176189 540 VLDSGRLLDVG 550
Cdd:PRK09580 218 VLYQGRIVKSG 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-577 |
1.81e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.19 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIggqDVRELTLD--SLRSA-IGLVPEDAvlfSGTIGA 426
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI---DDHPLHFGdySYRSQrIRMIFQDP---STSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 427 NIAYGRPDATPEQIATAARAAHIEEFVNT-------LPDgyqtAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTS 499
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPEQREKQIIEtlrqvglLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 500 AVDAVIECGIQEVLREaIADRTAVIF---TRRRSMLT-LADRVAVLDSGRLLDVGTPDEVwercpryreLLSPAPDLADD 575
Cdd:PRK15112 179 SLDMSMRSQLINLMLE-LQEKQGISYiyvTQHLGMMKhISDQVLVMHQGEVVERGSTADV---------LASPLHELTKR 248
|
..
gi 1108176189 576 LV 577
Cdd:PRK15112 249 LI 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
961-1173 |
1.83e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 961 GINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYdPT------HGTVRVDGCDLREFDVDGYR----NRLGIVTQEQYVFA 1030
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMVSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRD---------AIAYG-RPDATDAQVERAAREVGAHPMITALdNGYLHQvtaggrnLSAGQLQLLALARARLVDPDI 1100
Cdd:PRK15134 106 NPLHTlekqlyevlSLHRGmRREAARGEILNCLDRVGIRQAAKRL-TDYPHQ-------LSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1101 LLLDEATVALDpateAVVQRATLTLAAR------RTTLIVAHGLAIAEH-ADRIVVLEHGTVVEDGAHTELLAAGGH-YS 1172
Cdd:PRK15134 178 LIADEPTTALD----VSVQAQILQLLRElqqelnMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHpYT 253
|
.
gi 1108176189 1173 R 1173
Cdd:PRK15134 254 Q 254
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
349-502 |
1.88e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLD---SLRSA-IG-------LVP--- 414
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGfvfqsfmLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 --EDAVLFSGTIGANIAYGRPDATP--EQIATAARAAHieefvntLPdgyqtavgargLTLSGGQRQRIALARALLHQPR 490
Cdd:PRK10584 105 alENVELPALLRGESSRQSRNGAKAllEQLGLGKRLDH-------LP-----------AQLSGGEQQRVALARAFNGRPD 166
|
170
....*....|..
gi 1108176189 491 LLIMDDPTSAVD 502
Cdd:PRK10584 167 VLFADEPTGNLD 178
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
680-918 |
2.38e-09 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 60.04 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 680 VVQWGSAMVAG-------YTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVT 752
Cdd:cd18590 44 LFSLGSSLSAGlrgglfmCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 753 LVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFA 832
Cdd:cd18590 124 TLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 833 HSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAA 912
Cdd:cd18590 204 ALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNV 283
|
....*.
gi 1108176189 913 VAAGRI 918
Cdd:cd18590 284 GAAAKV 289
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
340-500 |
2.75e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGYVadrPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVT--QGAVRIGGQDVRELTL-DSLRSAIGLVPED 416
Cdd:PRK13549 14 TFGGV---KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIrDTERAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 AVLFSG-TIGANIAYGRpDATPEQI----ATAARAAHIEEFVNTLPDGYqTAVGArgltLSGGQRQRIALARALLHQPRL 491
Cdd:PRK13549 91 LALVKElSVLENIFLGN-EITPGGImdydAMYLRAQKLLAQLKLDINPA-TPVGN----LGLGQQQLVEIAKALNKQARL 164
|
....*....
gi 1108176189 492 LIMDDPTSA 500
Cdd:PRK13549 165 LILDEPTAS 173
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
966-1151 |
2.92e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 966 IPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVrvdgcdlrEFDVDgyrnrlgIVTQEQYV---FAGTVRDAIAYGRP 1042
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK-------ISYKPQYIkpdYDGTVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1043 DATDAQVERaarEVgAHPMitALDNGYLHQVTaggrNLSAGQLQLLALARARLVDPDILLLDEATVALDpateaVVQRAT 1122
Cdd:PRK13409 427 DLGSSYYKS---EI-IKPL--QLERLLDKNVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-----VEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 1108176189 1123 LTLAARR-------TTLIVAHGLAIAEH-ADRIVVLE 1151
Cdd:PRK13409 492 VAKAIRRiaeereaTALVVDHDIYMIDYiSDRLMVFE 528
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
969-1151 |
3.78e-09 |
|
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: 56.61 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 969 GQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDlrefdvdgyrnrlgivtqeqyvfagtvrdaiaygrpdatdaq 1048
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1049 veraarevgaHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLT---- 1124
Cdd:smart00382 40 ----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlll 109
|
170 180 190
....*....|....*....|....*....|....*.
gi 1108176189 1125 --LAARRTTLIVAH-------GLAIAEHADRIVVLE 1151
Cdd:smart00382 110 llKSEKNLTVILTTndekdlgPALLRRRFDRRIVLL 145
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
690-918 |
3.95e-09 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 59.48 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 690 GYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVL 769
Cdd:cd18574 67 SVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 770 LIFTTMPVLALATWQF----RRASnwtyRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLgvrgQ 845
Cdd:cd18574 147 LLLVIVPVVVLVGTLYgsflRKLS----RRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL----N 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 846 RLLALYYPFVALLCSLA----TTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18574 219 EKLGLGIGIFQGLSNLAlngiVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
334-577 |
4.19e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELTLDSL---RSAI 410
Cdd:PRK11831 8 VDMRGVSFTR-GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDAVLFSG-TIGANIAYGRPDAT--PEQIATAARAAHIEefvntlpdgyqtAVGARGLT------LSGGQRQRIAL 481
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPLREHTqlPAPLLHSTVMMKLE------------AVGLRGAAklmpseLSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAvIECG-----IQEvLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEVW 556
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDP-ITMGvlvklISE-LNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 1108176189 557 ERC-PRYRELLS-----------PAPDLADDLV 577
Cdd:PRK11831 233 ANPdPRVRQFLDgiadgpvpfryPAGDYHADLL 265
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
943-1111 |
4.90e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 943 VFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfDVDGYRNRLGIV 1022
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1023 TQEQYVFAG-TVRDAIAYgrpdatdaQVERAAREVGAHPMITALDNGYLHQVTAGgrNLSAGQLQLLALARARLVDPDIL 1101
Cdd:PRK13540 80 GHRSGINPYlTLRENCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLW 149
|
170
....*....|
gi 1108176189 1102 LLDEATVALD 1111
Cdd:PRK13540 150 LLDEPLVALD 159
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
959-1153 |
5.00e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.29 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---YRNR-LGIVTQEQYV---FAG 1031
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLlpdFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1032 TVRDAIAYGRPDATDAQVERAAREvgahpMITALdnGYLHQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVALD 1111
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALE-----MLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1108176189 1112 PATEAVVQRATLTLAARRTT--LIVAHGLAIAEHADRIVVLEHG 1153
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
348-546 |
7.48e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGLVPED----AVLFSG 422
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDrkrdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TIGANI----------AYGRPDATPEQIAtaaraahIEEFVNTL----PDGYQTAvgarGLtLSGGQRQRIALARALLHQ 488
Cdd:PRK10762 346 SVKENMsltalryfsrAGGSLKHADEQQA-------VSDFIRLFniktPSMEQAI----GL-LSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 489 PRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRR--SMLTLADRVAVLDSGRL 546
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEmpEVLGMSDRILVMHEGRI 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-544 |
9.86e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVR-ELTLDSLRSAIGLVPEDAVLFSG-TIGAN 427
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 428 IAYGRpdatpeqiataaraahieEFVNT---------------------LPDGYQTAVGarglTLSGGQRQRIALARALL 486
Cdd:PRK10762 100 IFLGR------------------EFVNRfgridwkkmyaeadkllarlnLRFSSDKLVG----ELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 487 HQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFT--RRRSMLTLADRVAVLDSG 544
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYIshRLKEIFEICDDVTVFRDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
347-545 |
1.14e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.50 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKST-LASLA--TRCYDVTQGAVRIGGQDVRElTLDSLRSAIGLVPEDAVLFsgt 423
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTlLKALAnrTEGNVSVEGDIHYNGIPYKE-FAEKYPGEIIYVSEEDVHF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 424 iganiaygrPDATPEQIATAARAAHIEEFVntlpdgyqtavgaRGltLSGGQRQRIALARALLHQPRLLIMDDPTSAVDA 503
Cdd:cd03233 96 ---------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1108176189 504 VIECGIQEVLREaIAD--RTAVIFTRRR---SMLTLADRVAVLDSGR 545
Cdd:cd03233 152 STALEILKCIRT-MADvlKTTTFVSLYQasdEIYDLFDKVLVLYEGR 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
350-553 |
1.27e-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: 59.07 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCY--DVTQGAVRIGGQDVRELTL-DSLRSAIG-------LVPEDAVL 419
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIViihqeltLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 420 FSGTIGANIAY-GRPDATPEQIATAA---RAAHIEEFVNTLPDGyqtavgarglTLSGGQRQRIALARALLHQPRLLIMD 495
Cdd:TIGR02633 97 ENIFLGNEITLpGGRMAYNAMYLRAKnllRELQLDADNVTRPVG----------DYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 496 DPTSAVDAVIECGIQEVLREAIADRTAVIFTRRR--SMLTLADRVAVLDSGRllDVGTPD 553
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlnEVKAVCDTICVIRDGQ--HVATKD 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-555 |
2.07e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKST-LASLATRCY----DVTqGAVRIGGQD----VRELTLDSLRSAiglvpEDAVL 419
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTlLKTIASNTDgfhiGVE-GVITYDGITpeeiKKHYRGDVVYNA-----ETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 420 F-SGTIGANIAYG----RPDATPEQIATAARAAHIEEFVNT---LPDGYQTAVG---ARGLtlSGGQRQRIALARALLHQ 488
Cdd:TIGR00956 150 FpHLTVGETLDFAarckTPQNRPDGVSREEYAKHIADVYMAtygLSHTRNTKVGndfVRGV--SGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 489 PRLLIMDDPTSAVDAVIECGIQEVLREA--IADRTAVIFTRRRSMLT--LADRVAVLDSGRLLDVGTPDEV 555
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSanILDTTPLVAIYQCSQDAyeLFDKVIVLYEGYQIYFGPADKA 298
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
942-1159 |
2.66e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVpALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfdvDGYRNRLGI 1021
Cdd:PRK15056 7 IVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYV---FAGTVRDAIAYGR---------PDATDAQVERAAREvgahpMITALDngYLHQVTAggrNLSAGQLQLLA 1089
Cdd:PRK15056 83 VPQSEEVdwsFPVLVEDVVMMGRyghmgwlrrAKKRDRQIVTAALA-----RVDMVE--FRHRQIG---ELSGGQKKRVF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1108176189 1090 LARARLVDPDILLLDEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGL-AIAEHADRIVVLEhGTVVEDG 1159
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLgSVTEFCDYTVMVK-GTVLASG 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
959-1165 |
3.37e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYdPTHGTVRVDGCDLREFDVDGYRNRLGIVTQEQY-VFAGTVRDAI 1037
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1038 AYGRPDATD-AQVERAAREVGAHPMITALDNGYLHQvtaggrnLSAGQLQLLALARARL-VDPDI------LLLDEATVA 1109
Cdd:PRK03695 91 TLHQPDKTRtEAVASALNEVAEALGLDDKLGRSVNQ-------LSGGEWQRVRLAAVVLqVWPDInpagqlLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1110 LDPATEAVVQRATLTLAAR-RTTLIVAHGLA-IAEHADRIVVLEHGTVVEDGAHTELL 1165
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
683-918 |
3.41e-08 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 56.37 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 683 WGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLdAFEDD---GDaqIVTAVTADV----EAIVAFLRTGLvvavISVVTLVG 755
Cdd:cd18573 59 FGRVYLLRIAGERIVARLRKRLFKSILRQDA-AFFDKnktGE--LVSRLSSDTsvvgKSLTQNLSDGL----RSLVSGVG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 756 ILVALLAIRARLVLLIFTTMPVLALATWQF-RRASNWTyRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHS 834
Cdd:cd18573 132 GIGMMLYISPKLTLVMLLVVPPIAVGAVFYgRYVRKLS-KQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 835 DDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVA 914
Cdd:cd18573 211 DEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGA 290
|
....
gi 1108176189 915 AGRI 918
Cdd:cd18573 291 SSRL 294
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
956-1187 |
3.59e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKS--------TLIKLVARfydpTHGTVRVDGCDLREFDVDGyRNRLGIVTQEQY 1027
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaalgILPAGVRQ----TAGRVLLDGKPVAPCALRG-RKIATIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 VF-------AGTVRDAIAYGRPdATDAQVERAAREVGAHPMITALDngyLHQVtaggrNLSAGQLQLLALARARLVDPDI 1100
Cdd:PRK10418 91 AFnplhtmhTHARETCLALGKP-ADDATLTAALEAVGLENAARVLK---LYPF-----EMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1101 LLLDEATVALDPATEAVVQRATLTLAARRT--TLIVAHGLAI-AEHADRIVVLEHGTVVEDGAHTELLAAGGH--YSRLW 1175
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVvARLADDVAVMSHGRIVEQGDVETLFNAPKHavTRSLV 241
|
250
....*....|..
gi 1108176189 1176 AAHTRLCSPEIT 1187
Cdd:PRK10418 242 SAHLALYGMELA 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-551 |
4.04e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.10 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 348 PVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVreLT-LDSLRSAIGLVPE-DAV--LFSGT 423
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTnISDVHQNMGYCPQfDAIddLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 424 IGANIaYGRPDATPeqiataarAAHIEEFVNTLPDGYQTAVGARGL--TLSGGQRQRIALARALLHQPRLLIMDDPTSAV 501
Cdd:TIGR01257 2031 EHLYL-YARLRGVP--------AEEIEKVANWSIQSLGLSLYADRLagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 502 DAVIECGIQEVLREAIADRTAVIFTrRRSM---LTLADRVAVLDSGRLLDVGT 551
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREGRAVVLT-SHSMeecEALCTRLAIMVKGAFQCLGT 2153
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-553 |
4.25e-08 |
|
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: 53.53 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 360 GETLAVVGAPGSGKSTLA-SLATRCYDVTQGAVRIGGQDVRELTLDSLRsaiglvpedavlfsgtiganiaygrpdatpe 438
Cdd:smart00382 2 GEVILIVGPPGSGKTTLArALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 439 qiataaraahieefvntlpdgyQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQE------V 512
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1108176189 513 LREAIADRTAVIFTRRRSMlTLADRVAVLDSGRLLDVGTPD 553
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEK-DLGPALLRRRFDRRIVLLLIL 148
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
70-309 |
4.82e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 55.94 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 70 TYLLTYVRRYYGGRIAHlvqhDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFD-VPNVLRHVLTLLLGV 148
Cdd:cd18577 64 SYIQTACWTITGERQAR----RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEkLGLLIQSLSTFIAGF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 149 A-----------VMTWLSVPlallavllvpvIGLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERE 217
Cdd:cd18577 140 IiafiyswkltlVLLATLPL-----------IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 218 TVKLVTASRALYAAQLRVARLNAhfgpLLQTLPALGQMAVFALGGW----MAAQGSITVGT-FVAFWACLTL---LARpa 289
Cdd:cd18577 209 IKRYSKALEKARKAGIKKGLVSG----LGLGLLFFIIFAMYALAFWygsrLVRDGEISPGDvLTVFFAVLIGafsLGQ-- 282
|
250 260
....*....|....*....|
gi 1108176189 290 cdLAGMLTIAQQARAGAVRV 309
Cdd:cd18577 283 --IAPNLQAFAKARAAAAKI 300
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
950-1154 |
4.89e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDL------REFDVdgyRNRLGIVT 1023
Cdd:PRK11831 14 SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsRLYTV---RKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1024 QEQYVFAG-TVRDAIAYgrpdatdaqverAAREvgaHpmiTALDNGYLHQV------TAGGR--------NLSAGQLQLL 1088
Cdd:PRK11831 91 QSGALFTDmNVFDNVAY------------PLRE---H---TQLPAPLLHSTvmmkleAVGLRgaaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDPATEAVVQR--ATLTLAARRTTLIVAHG----LAIAEHADRIV---VLEHGT 1154
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKliSELNSALGVTCVVVSHDvpevLSIADHAYIVAdkkIVAHGS 227
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
663-926 |
5.57e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 55.92 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 663 ALWWAALAgtatvVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAH--AQRLGLdaFEDDGDA--QIVTAVTADVEAIVAF 738
Cdd:cd18578 55 ALMFLVLA-----IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAilRQDIAW--FDDPENStgALTSRLSTDASDVRGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 739 LRTGLVVAVISVVTLV-GILVALlAIRARLVLLIFTTMPVLALAT-WQFRRASNWTyRRARHRLGTVTATLREYAAGLRI 816
Cdd:cd18578 128 VGDRLGLILQAIVTLVaGLIIAF-VYGWKLALVGLATVPLLLLAGyLRMRLLSGFE-EKNKKAYEESSKIASEAVSNIRT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 817 AQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGA-LVTYLLyieLLY 895
Cdd:cd18578 206 VASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQfFIVFMA---LIF 282
|
250 260 270
....*....|....*....|....*....|...
gi 1108176189 896 T--PIGELAQMFDDYQRAAVAAGRIRSLLSTRT 926
Cdd:cd18578 283 GaqSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
433-554 |
6.05e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 433 PDATPEQIATAARAAHIEEFVNTLPDGyqtavgargltLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEV 512
Cdd:NF033858 371 AAEIAARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1108176189 513 LREAIADRTAVIFTRRRSMLTLA--DRVAVLDSGRLLDVGTPDE 554
Cdd:NF033858 440 LIELSREDGVTIFISTHFMNEAErcDRISLMHAGRVLASDTPAA 483
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
92-278 |
6.06e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family 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. 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. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 55.72 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 92 LRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQ-ALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIG 170
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQnAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 171 LIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLP 250
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAA 236
|
170 180
....*....|....*....|....*...
gi 1108176189 251 ALGQMAVFALGGWMAAQGSITVGTFVAF 278
Cdd:cd18780 237 QLAIVLVLWYGGRLVIDGELTTGLLTSF 264
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
947-1181 |
6.17e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 947 VHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfdvdgyRNRLGIVTQEQ 1026
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRR------RSRQVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 Y-------------------------VF------AGTVRDAIAYGRPDATdAQVERAAREVGAhPMITALDNGYLHQvta 1075
Cdd:PRK10261 94 SaaqmrhvrgadmamifqepmtslnpVFtvgeqiAESIRLHQGASREEAM-VEAKRMLDQVRI-PEAQTILSRYPHQ--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1076 ggrnLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRT--TLIVAHGLA-IAEHADRIVVLEH 1152
Cdd:PRK10261 169 ----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGvVAEIADRVLVMYQ 244
|
250 260 270
....*....|....*....|....*....|.
gi 1108176189 1153 GTVVEDGAHTELLAAGGH-YSR-LWAAHTRL 1181
Cdd:PRK10261 245 GEAVETGSVEQIFHAPQHpYTRaLLAAVPQL 275
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
956-1161 |
8.96e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYdPtHGT----VRVDGCDLREFDV-DGYRNRLGIVTQE----- 1025
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-P-HGTyegeIIFEGEELQASNIrDTERAGIAIIHQElalvk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1026 -----QYVFAGtvRDAIAYGRPDaTDAQVERAA---REVGahpmitaLD-NGYLhQVtaggRNLSAGQLQLLALARARLV 1096
Cdd:PRK13549 96 elsvlENIFLG--NEITPGGIMD-YDAMYLRAQkllAQLK-------LDiNPAT-PV----GNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLAARRTTLI-VAHGL-AIAEHADRIvvlehgTVVEDGAH 1161
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIyISHKLnEVKAISDTI------CVIRDGRH 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
969-1171 |
9.14e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 969 GQTVVFVGSTGSGKSTLIKLVArFYDPT----HGTVRVDGcdlREFDVDGYRNRLGIVtQEQYVFAG--TVRDAI---AY 1039
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYV-QQDDLFIPtlTVREHLmfqAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1040 GRPDATDAQVERAAR------EVG----AHPMItaldngylhQVTAGGRNLSAGQLQLLALARARLVDPDILLLDEATVA 1109
Cdd:TIGR00955 126 LRMPRRVTKKEKRERvdevlqALGlrkcANTRI---------GVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1110 LDPATEAVVQRATLTLAARRTTLIVA-H--GLAIAEHADRIVVLEHGTVVEDGAHTEL---LAAGGHY 1171
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTiHqpSSELFELFDKIILMAEGRVAYLGSPDQAvpfFSDLGHP 264
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
942-1164 |
1.00e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.62 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTReVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVdgyRNRlGI 1021
Cdd:PRK11650 4 LKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADR-DI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTqeqyVFAG-------TVRDAIAYG---R--PDAT-DAQVERAAREVGAHPMitaLDNgylhqvtaGGRNLSAGQLQLL 1088
Cdd:PRK11650 79 AM----VFQNyalyphmSVRENMAYGlkiRgmPKAEiEERVAEAARILELEPL---LDR--------KPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDpATEAVVQRATLTLAARR---TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGAHTEL 1164
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD-AKLRVQMRLEIQRLHRRlktTSLYVTHDQVEAmTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
969-1151 |
1.07e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 969 GQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVrvdgcdlrEFDVDgyrnrlgIVTQEQYV---FAGTVRDAIAYGRPDAT 1045
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK-------ISYKPQYIspdYDGTVEEFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1046 DAQVERAarEVgAHPMitALDNGYLHQVtaggRNLSAGQLQLLALARARLVDPDILLLDEATVALDpateaVVQRATLTL 1125
Cdd:COG1245 431 GSSYYKT--EI-IKPL--GLEKLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-----VEQRLAVAK 496
|
170 180 190
....*....|....*....|....*....|....
gi 1108176189 1126 AARR-------TTLIVAHGLAIAEH-ADRIVVLE 1151
Cdd:COG1245 497 AIRRfaenrgkTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
946-1170 |
1.18e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 946 AVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKST-------LIKLVARFydpTHGTVRVDGCDLREFDVDGYRNR 1018
Cdd:PRK11022 10 SVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRV---MAEKLEFNGQDLQRISEKERRNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1019 LG----IVTQEQ-------YVFAGTVRDAIAYGRPDATDAQVERAA---REVGAHPMITALDNgYLHQvtaggrnLSAGQ 1084
Cdd:PRK11022 87 VGaevaMIFQDPmtslnpcYTVGFQIMEAIKVHQGGNKKTRRQRAIdllNQVGIPDPASRLDV-YPHQ-------LSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1085 LQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTT--LIVAHGLA-IAEHADRIVVLEHGTVVEDGAH 1161
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLAlVAEAAHKIIVMYAGQVVETGKA 238
|
....*....
gi 1108176189 1162 TELLAAGGH 1170
Cdd:PRK11022 239 HDIFRAPRH 247
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
331-502 |
1.23e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 331 RLSLEFQRVSFGYvADRPVLREISLSVRAGETLAVVGAPGSGKSTLaslatrcydvtqgavriggqdvreltldsLRSAI 410
Cdd:PRK15064 317 RNALEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTL-----------------------------LRTLV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPEDavlfSGTI----GANIAYGRPDatpeqiataaraaHIEEFVNTL------------PDGYQTAVGARGLTL--- 471
Cdd:PRK15064 367 GELEPD----SGTVkwseNANIGYYAQD-------------HAYDFENDLtlfdwmsqwrqeGDDEQAVRGTLGRLLfsq 429
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1108176189 472 ----------SGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:PRK15064 430 ddikksvkvlSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
958-1160 |
1.49e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFY--DPTHG--------TVRVDGCDLRefDVDGYRNRLGIVTQE-Q 1026
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLAR--DIRKSRANTGYIFQQfN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1027 YVFAGTVRDAIAYGRPDAT-----------DAQVERAAREVGAHPMITaldngYLHQVTAggrNLSAGQLQLLALARARL 1095
Cdd:PRK09984 97 LVNRLSVLENVLIGALGSTpfwrtcfswftREQKQRALQALTRVGMVH-----FAHQRVS---TLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1096 VDPDILLLDEATVALDPATEAVVQRATLTLAARR--TTLIVAHGLAIA-EHADRIVVLEHGTVVEDGA 1160
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYAlRYCERIVALRQGHVFYDGS 236
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
641-918 |
1.49e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 54.49 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 641 GLLPPLLIRHGIDVGIRRHVLSALWWAA----LAGTATVVIRWVVQWgsamVAGYTGEQVLFRLRSVVFAHAQRLGLDAF 716
Cdd:cd18568 18 GLALPLFTQIILDRVLVHKNISLLNLILigllIVGIFQILLSAVRQY----LLDYFANRIDLSLLSDFYKHLLSLPLSFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 717 E--DDGDaqIVTAVTADvEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYR 794
Cdd:cd18568 94 AsrKVGD--IITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 795 RARHRLGTVTATLREYAAGLRIAQAFRAEYR---GLQSYFAHSDDYRrlgVRGQRLLALYYPFVALLCSLATTLVLLDGA 871
Cdd:cd18568 171 EIFQANAEQQSFLVEALTGIATIKALAAERPirwRWENKFAKALNTR---FRGQKLSIVLQLISSLINHLGTIAVLWYGA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1108176189 872 REVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18568 248 YLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
975-1134 |
1.74e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 975 VGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDlrefdvdgyrnRLGIVTQEQYVFA-----GTV-------------RDA 1036
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKLRQDQFAFEeftvlDTVimghtelwevkqeRDR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1037 IaYGRPDATDAQVERAAR-EVGAHPMitaldNGYLHQVTAGGRNLSAG-----------------QLQLLaLARARLVDP 1098
Cdd:PRK15064 102 I-YALPEMSEEDGMKVADlEVKFAEM-----DGYTAEARAGELLLGVGipeeqhyglmsevapgwKLRVL-LAQALFSNP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1108176189 1099 DILLLDEATVALDPAT----EAVvqratltLAARRTTLIV 1134
Cdd:PRK15064 175 DILLLDEPTNNLDINTirwlEDV-------LNERNSTMII 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
350-558 |
1.76e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVREltlDSLRSAIGlvpedavlfsgtigANIA 429
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVC--------------PRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 430 Y-----GR---PDAT-PEQI---------ATAARAAHIEEFVNtlpdgyqtavgARGLT---------LSGGQRQRIALA 482
Cdd:NF033858 80 YmpqglGKnlyPTLSvFENLdffgrlfgqDAAERRRRIDELLR-----------ATGLApfadrpagkLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 483 RALLHQPRLLIMDDPTSAVDAviecgiqevL-R----EAIADrtavIFTRRRSMLTLA-----------DRVAVLDSGRL 546
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDP---------LsRrqfwELIDR----IRAERPGMSVLVataymeeaerfDWLVAMDAGRV 215
|
250
....*....|..
gi 1108176189 547 LDVGTPDEVWER 558
Cdd:NF033858 216 LATGTPAELLAR 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
325-555 |
1.93e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 325 PLSPEARLSLEFQrvsfgyVADRPV--LREISLSVRAGETLAVVGAPGSGKSTLAS----LATRCYDVTQGAVRIGGQDV 398
Cdd:PRK15093 2 PLLDIRNLTIEFK------TSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKaicgVTKDNWRVTADRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 399 RELTLDSLRSAIG-------LVPEDAVLFSGTIGANIAYGRPDATP-----EQIATAARAAhIEEFVNTLPDGYQTAVGA 466
Cdd:PRK15093 76 LRLSPRERRKLVGhnvsmifQEPQSCLDPSERVGRQLMQNIPGWTYkgrwwQRFGWRKRRA-IELLHRVGIKDHKDAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 467 RGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVL-REAIADRTAVIFTRR--RSMLTLADRVAVLDS 543
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHdlQMLSQWADKINVLYC 234
|
250
....*....|..
gi 1108176189 544 GRLLDVGTPDEV 555
Cdd:PRK15093 235 GQTVETAPSKEL 246
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-519 |
1.94e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 335 EFQRVSFGyVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQ-DVRelTLDSLRSAigLV 413
Cdd:PRK11147 321 EMENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA--YFDQHRAE--LD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 414 PEDAVLfsgtigANIAYGRPDATpeqiaTAARAAHI----EEFVNTlPDGYQTAVGArgltLSGGQRQRIALARALLHQP 489
Cdd:PRK11147 396 PEKTVM------DNLAEGKQEVM-----VNGRPRHVlgylQDFLFH-PKRAMTPVKA----LSGGERNRLLLARLFLKPS 459
|
170 180 190
....*....|....*....|....*....|
gi 1108176189 490 RLLIMDDPTSAVDavIEcgIQEVLREAIAD 519
Cdd:PRK11147 460 NLLILDEPTNDLD--VE--TLELLEELLDS 485
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
204-278 |
2.39e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 54.00 E-value: 2.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 204 GIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAF 278
Cdd:cd18567 189 GIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAF 263
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
31-297 |
2.55e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 53.67 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 31 TVIAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATY-LLTYVRRYYggrIAHLVQH-DLRM--DAFQALLRWDGR 106
Cdd:cd18555 15 QLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYgLFSFLRGYI---IIKLQTKlDKSLmsDFFEHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 107 QQDRWSSGQLIVRTtNDLQLVQALLFDvpNVLRHVLTLLLGV---AVMTWLSVPLALLAVLLVPVIGLIAHRSRRLLAAA 183
Cdd:cd18555 92 FFENRSSGDLLFRA-NSNVYIRQILSN--QVISLIIDLLLLViylIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 184 THCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERetvkLVTASRALYAAQL----RVARLNAHFGPLLQTLPALGQMAVFA 259
Cdd:cd18555 169 NQEEIVAQTKVQSYLTETLYGIETIKSLGSEKN----IYKKWENLFKKQLkafkKKERLSNILNSISSSIQFIAPLLILW 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 1108176189 260 LGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLT 297
Cdd:cd18555 245 IGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYN 282
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
922-1170 |
2.80e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 922 LSTRTPSSPAARpvgtlrGEVVFDAVHYSYRtrevPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVR 1001
Cdd:COG1129 241 LEDLFPKRAAAP------GEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1002 VDGcdlREFDV----DGYRNRLGIVT---QEQYVFAG-TVRDAIA------YGRPDATDAQVERAArevgAHPMITALDn 1067
Cdd:COG1129 311 LDG---KPVRIrsprDAIRAGIAYVPedrKGEGLVLDlSIRENITlasldrLSRGGLLDRRRERAL----AEEYIKRLR- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1068 gylhqVTAGG-----RNLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARrttlivahGLAI-- 1140
Cdd:COG1129 383 -----IKTPSpeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE--------GKAViv 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1108176189 1141 --------AEHADRIVVLEHGTVVEDGAHTEL-------LAAGGH 1170
Cdd:COG1129 450 isselpelLGLSDRILVMREGRIVGELDREEAteeaimaAATGGA 494
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
71-278 |
3.32e-07 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 53.32 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 71 YLLTYVrryyGGRIAHlvqhDLRMDAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQ-ALLFDVPNVLRHVlTLLLGVA 149
Cdd:cd18574 64 SLLSVV----GERVAA----RLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKsSFKQCVSQGLRSV-TQTVGCV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 150 V--------MTWLSVPLALLAVLLVPVIGliahrsrRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEEREtvkl 221
Cdd:cd18574 135 VslylispkLTLLLLVIVPVVVLVGTLYG-------SFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE---- 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 222 vtasRALYAAQL-RVARLNAHFG---PLLQTLP--ALGQM--AVFALGGWMAAQGSITVGTFVAF 278
Cdd:cd18574 204 ----LELYEEEVeKAAKLNEKLGlgiGIFQGLSnlALNGIvlGVLYYGGSLVSRGELTAGDLMSF 264
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
958-1159 |
4.64e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.62 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDG---------YRNRLGIVTQE--- 1025
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAlseaerrrlLRTEWGFVHQHprd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1026 ---QYVFAGT----------VRDaiaYG--RPDATD--AQVERAAREVGAHPmitaldngylhqvtaggRNLSAGQLQLL 1088
Cdd:PRK11701 101 glrMQVSAGGnigerlmavgARH---YGdiRATAGDwlERVEIDAARIDDLP-----------------TTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 1089 ALARARLVDPDILLLDEATVALDPATEA----VVQR--ATLTLAArrttLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQArlldLLRGlvRELGLAV----VIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
353-555 |
4.72e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 353 ISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV-----------------------RELT-LDSLrs 408
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvrtfqhvrlfREMTvIENL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 409 aigLVPE----DAVLFSGTIgANIAYGRPDAtpeqiATAARAAHIEEFVNTLPDGYQTAvgarGlTLSGGQRQRIALARA 484
Cdd:PRK11300 102 ---LVAQhqqlKTGLFSGLL-KTPAFRRAES-----EALDRAATWLERVGLLEHANRQA----G-NLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 485 LLHQPRLLIMDDP--------TSAVDAVIecgiqEVLREAIADRTAVIFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK11300 168 MVTQPEILMLDEPaaglnpkeTKELDELI-----AELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
17-278 |
4.73e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.98 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 17 RRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAI-AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMD 95
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLvQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 96 AFQALLRWDGRQQDRWSSGQLIVRTtNDLQLVQALLFD-VPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIAH 174
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGtALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 175 RSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPALGQ 254
Cdd:cd18782 160 LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSS 239
|
250 260
....*....|....*....|....
gi 1108176189 255 MAVFALGGWMAAQGSITVGTFVAF 278
Cdd:cd18782 240 LLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
349-516 |
5.01e-07 |
|
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: 53.98 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 349 VLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAvriggqdvreLTLDSlRSAIGLVPEDAVLFSGTIGANI 428
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR----------LTKPA-KGKLFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 429 AYgrPDATPEQIATAARAAHIEEFVNTLPDGY--QTAVGARGL-----TLSGGQRQRIALARALLHQPRLLIMDDPTSAV 501
Cdd:TIGR00954 536 IY--PDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGGWSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170
....*....|....*
gi 1108176189 502 DAVIECGIQEVLREA 516
Cdd:TIGR00954 614 SVDVEGYMYRLCREF 628
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
344-412 |
6.56e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 6.56e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 344 VADRPVLREISLSVRAGETLAVVGAPGSGKSTLAS-LATR-CYDVTQGAVRIGGQDVRELTLDsLRSAIGL 412
Cdd:CHL00131 17 VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKvIAGHpAYKILEGDILFKGESILDLEPE-ERAHLGI 86
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
347-546 |
6.86e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGLVPED--------- 416
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyay 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 417 -AVLFSGTIgANI-AYGRPDATPEQIATAARAAHIEEFVNTLPDGYQTAVGarglTLSGGQRQRIALARALLHQPRLLIM 494
Cdd:PRK10982 341 lDIGFNSLI-SNIrNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 495 DDPTSAVDAVIECGIQEVLRE-AIADRTAVIFTRRR-SMLTLADRVAVLDSGRL 546
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
350-515 |
8.23e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTL----ASLATRcyDVTQGA-VRIGGQDVR---ELTLDSLRS---------AIGL 412
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITG--DKSAGShIELLGRTVQregRLARDIRKSrantgyifqQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 413 VPEDAVLFSGTIGA--NIAYGRPDA---TPEQIATAARAAhieefvntlpdgyqTAVG------ARGLTLSGGQRQRIAL 481
Cdd:PRK09984 98 VNRLSVLENVLIGAlgSTPFWRTCFswfTREQKQRALQAL--------------TRVGmvhfahQRVSTLSGGQQQRVAI 163
|
170 180 190
....*....|....*....|....*....|....
gi 1108176189 482 ARALLHQPRLLIMDDPTSAVDAVIECGIQEVLRE 515
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRD 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
916-1156 |
9.37e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 916 GRIRSLLSTRTPSSPaarpvgtlrGEVVFDAVHYSYRT-REVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYD 994
Cdd:COG3845 239 GREVLLRVEKAPAEP---------GEVVLEVENLSVRDdRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 995 PTHGTVRVDGCDLREFDVD-------GY----RNRLGIVTqeqyvfAGTVRDAIAYGRPDATD---------AQVERAAR 1054
Cdd:COG3845 310 PASGSIRLDGEDITGLSPRerrrlgvAYipedRLGRGLVP------DMSVAENLILGRYRRPPfsrggfldrKAIRAFAE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1055 EvgahpMITALDngylhqVTAGG-----RNLSAGQLQLLALARARLVDPDILLLDEATVALDP-ATEAVVQRatltLAAR 1128
Cdd:COG3845 384 E-----LIEEFD------VRTPGpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgAIEFIHQR----LLEL 448
|
250 260 270
....*....|....*....|....*....|....*...
gi 1108176189 1129 RttlivAHGLA----------IAEHADRIVVLEHGTVV 1156
Cdd:COG3845 449 R-----DAGAAvllisedldeILALSDRIAVMYEGRIV 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
950-1169 |
9.63e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREfdvDGYRNRlgivtqeqyvf 1029
Cdd:NF033858 8 SHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRA----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 agtVRDAIAY-----GR---PDAT--------------DAQvERAARevgahpmITALdngylhqVTAGG---------R 1078
Cdd:NF033858 74 ---VCPRIAYmpqglGKnlyPTLSvfenldffgrlfgqDAA-ERRRR-------IDEL-------LRATGlapfadrpaG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1079 NLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAvvQRATL--TLAARRT--TLIVAhgLAI---AEHADRIVVLE 1151
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QFWELidRIRAERPgmSVLVA--TAYmeeAERFDWLVAMD 211
|
250
....*....|....*...
gi 1108176189 1152 HGTVVEDGAHTELLAAGG 1169
Cdd:NF033858 212 AGRVLATGTPAELLARTG 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
950-1166 |
1.04e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.43 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 950 SYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNR-LGIVTQEQYV 1028
Cdd:PRK10895 12 AYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 FAG-TVRD---AIAYGRPDATDAQVERAAREVGAHPMITALDNGYlhqvtagGRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:PRK10895 90 FRRlSVYDnlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1105 EATVALDPATEAVVQRATLTLaaRRTTLivahGLAIAEH--------ADRIVVLEHGTVVEDGAHTELLA 1166
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL--RDSGL----GVLITDHnvretlavCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
346-503 |
1.05e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 346 DRPVLREISLSVRAGETLAVVGAPGSGKSTLAS-LATRcydVTQGAVRIGGQDVRELTLD-SLRSAIGLVPE-------- 415
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER---VTTGVITGGDRLVNGRPLDsSFQRSIGYVQQqdlhlpts 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 416 ---DAVLFSgtiganiAYGRpdaTPEQIATAARAAHIEEFVNTLP-DGYQTA-VGARGLTLSGGQRQRIALARALLHQPR 490
Cdd:TIGR00956 852 tvrESLRFS-------AYLR---QPKSVSKSEKMEYVEEVIKLLEmESYADAvVGVPGEGLNVEQRKRLTIGVELVAKPK 921
|
170
....*....|....
gi 1108176189 491 LLI-MDDPTSAVDA 503
Cdd:TIGR00956 922 LLLfLDEPTSGLDS 935
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
945-1165 |
1.35e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 945 DAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVA-RFYDPTH-------GTVRVDGCDLREFDVDGYR 1016
Cdd:PRK13547 5 DHLHVARRHRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1017 NRLGIVTQE-QYVFAGTVRDAIAYGR-PDATDA-QVERAAREVGAHPMITAldngylHQVTAGGRN---LSAGQLQLLAL 1090
Cdd:PRK13547 83 RLRAVLPQAaQPAFAFSAREIVLLGRyPHARRAgALTHRDGEIAWQALALA------GATALVGRDvttLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1091 ARA---------RLVDPDILLLDEATVALDPATEAVVQRATLTLAA--RRTTLIVAHGLAI-AEHADRIVVLEHGTVVED 1158
Cdd:PRK13547 157 ARVlaqlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLaARHADRIAMLADGAIVAH 236
|
....*..
gi 1108176189 1159 GAHTELL 1165
Cdd:PRK13547 237 GAPADVL 243
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
17-309 |
1.37e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 51.68 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 17 RRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAI-AADHRPLAPWAVVLVAAAGATYLLTYVRRYYGGRIAHLVQHDLRMD 95
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIpSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 96 AFQALLR-----WDGRQqdrwsSGQLIVRTtNDLQLVQALLFDV-PNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVI 169
Cdd:cd18570 81 YFKHLLKlplsfFETRK-----TGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 170 GLIAHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTL 249
Cdd:cd18570 155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 250 PALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
340-544 |
1.45e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 340 SFGYVAdrpVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVRELT-LDSLRSAIGLV-PEDA 417
Cdd:PRK09700 14 SFGPVH---ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIyQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 418 VLFSGTIGANIAYGR-----------PDATPEQIataaRAAHIEEFVNTLPDgYQTAVGarglTLSGGQRQRIALARALL 486
Cdd:PRK09700 91 VIDELTVLENLYIGRhltkkvcgvniIDWREMRV----RAAMMLLRVGLKVD-LDEKVA----NLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 487 HQPRLLIMDDPTSAV-DAVIEcGIQEVLREAIADRTAVIFTRRR--SMLTLADRVAVLDSG 544
Cdd:PRK09700 162 LDAKVIIMDEPTSSLtNKEVD-YLFLIMNQLRKEGTAIVYISHKlaEIRRICDRYTVMKDG 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
463-555 |
1.86e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 463 AVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRR--RSMLTLADRVAV 540
Cdd:NF000106 137 AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQymEEAEQLAHELTV 216
|
90
....*....|....*
gi 1108176189 541 LDSGRLLDVGTPDEV 555
Cdd:NF000106 217 IDRGRVIADGKVDEL 231
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
641-918 |
2.60e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 50.67 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 641 GLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDG 720
Cdd:cd18782 18 GLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 721 DAQIVTAVtADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATWQFRRASNWTYRRARHRL 800
Cdd:cd18782 98 VGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEAS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 801 GTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVIS 880
Cdd:cd18782 177 AKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELT 256
|
250 260 270
....*....|....*....|....*....|....*...
gi 1108176189 881 VGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18782 257 LGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
347-579 |
2.75e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 347 RPVLREISLSVRAGETLAVVGAPGSGKSTL---------ASLATRCYDVTqGAVRIGGQDVREL---TLDSLRSAIGLVP 414
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARVT-GDVTLNGEPLAAIdapRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 415 EDAVLFSgtIGANIAYGRPDATPEQIATAARAAHIEEFVNTLPDGyQTAVGARGLTLSGGQRQRIALARALLH------- 487
Cdd:PRK13547 93 QPAFAFS--AREIVLLGRYPHARRAGALTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 488 --QPRLLIMDDPTSAVDAVIECGIQEVLREAIAD-RTAVIFTRRRSMLTL--ADRVAVLDSGRLLDVGTPDEVW-----E 557
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAArhADRIAMLADGAIVAHGAPADVLtpahiA 249
|
250 260
....*....|....*....|..
gi 1108176189 558 RCPRYRELLSPAPDLADDLVVA 579
Cdd:PRK13547 250 RCYGFAVRLVDAGDGVPPVIVP 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
957-1156 |
3.06e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVArfydpthGTVRVDgcdlrefdvDG---YRNRLGIVTQEQ----YVf 1029
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLD---------DGriiYEQDLIVARLQQdpprNV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AGTVRDAIAYGRPDATDA--QVERAAREVGAHPMITALD------------NGY-----LHQVTAG-GRN-------LSA 1082
Cdd:PRK11147 80 EGTVYDFVAEGIEEQAEYlkRYHDISHLVETDPSEKNLNelaklqeqldhhNLWqlenrINEVLAQlGLDpdaalssLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1083 GQLQLLALARARLVDPDILLLDEATVALDpaTEAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHGTVV 1156
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLD--IETIEWLEGFLKTFQGSIIFISHDRSfIRNMATRIVDLDRGKLV 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
953-1159 |
3.58e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 953 TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGC---DLREFDVDGYRNRLGIVTQEQYVF 1029
Cdd:PRK10261 334 TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1030 AG---TVRDAI-------AYGRPDATDAQVERAAREVGAHPMITALdngYLHQvtaggrnLSAGQLQLLALARARLVDPD 1099
Cdd:PRK10261 414 LDprqTVGDSImeplrvhGLLPGKAAAARVAWLLERVGLLPEHAWR---YPHE-------FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1100 ILLLDEATVALDPATEAvvQRATLTLAARR----TTLIVAHGLAIAEH-ADRIVVLEHGTVVEDG 1159
Cdd:PRK10261 484 VIIADEAVSALDVSIRG--QIINLLLDLQRdfgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
17-303 |
3.60e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 50.25 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 17 RRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATY-LLTYVRRYYggrIAHLVQH-DLRM 94
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQiLLSAVRQYL---LDYFANRiDLSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 95 --DAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLI 172
Cdd:cd18568 78 lsDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 173 AHRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQEERETVKLVTASRALYAAQLRVARLNAHFGPLLQTLPAL 252
Cdd:cd18568 158 TLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 253 GQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQAR 303
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETR 288
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
957-1162 |
3.67e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 957 PALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVA--RFYDPTHGTVRVDGCDLREFDVDGyRNRLGIVTQEQY------- 1027
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAFQYpveipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1028 ---VFAGTVRDAI-------AYGRPDATDAQVERAAR-EVGAHPMITALDNGYlhqvtAGGRNLSAGQLQLLALararlv 1096
Cdd:PRK09580 94 snqFFLQTALNAVrsyrgqePLDRFDFQDLMEEKIALlKMPEDLLTRSVNVGF-----SGGEKKRNDILQMAVL------ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1097 DPDILLLDEATVALDPATEAVVQRATLTLA-ARRTTLIVAHGLAIAEH--ADRIVVLEHGTVVEDGAHT 1162
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHYQRILDYikPDYVHVLYQGRIVKSGDFT 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
956-1157 |
3.83e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyrnrlgivtqEQYVFAGTvRD 1035
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG--------------------QEMRFAST-TA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1036 AIAYGrpdatdaqVERAAREVGAHPMITALDNGYLHQV-TAGG----------------------------RNLSAGQLQ 1086
Cdd:PRK11288 76 ALAAG--------VAIIYQELHLVPEMTVAENLYLGQLpHKGGivnrrllnyeareqlehlgvdidpdtplKYLSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1087 LLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLA-IAEHADRIVVLEHGTVVE 1157
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEeIFALCDAITVFKDGRYVA 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
961-1175 |
3.95e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.03 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 961 GINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRL------GIVT----QEQYVFA 1030
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGIKTeltaLENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 GTVRDaiaygrpDATDAQVERAAREVGAHpmitaldnGYLHqVTAggRNLSAGQLQLLALARARLVDPDILLLDEATVAL 1110
Cdd:PRK13538 99 QRLHG-------PGDDEALWEALAQVGLA--------GFED-VPV--RQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1108176189 1111 DpaTEAVVQRATLtlaarrttlivahglaIAEHADR--IVVLEhgtvvedgAHTELLAAGGHYSRLW 1175
Cdd:PRK13538 161 D--KQGVARLEAL----------------LAQHAEQggMVILT--------THQDLPVASDKVRKLR 201
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
955-1027 |
4.66e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 4.66e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 955 EVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARF--YDPTHGTVRVDGCDLREFDVDgYRNRLGIVTQEQY 1027
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAFQY 92
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
942-1111 |
5.51e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 942 VVFDAVHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlrefdvdgyRNRLGI 1021
Cdd:PRK09544 5 VSLENVSVSFGQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1022 VTQEQYVFAG---TVRDAIAYgRPDATDAQVERAAREVGAHpmitaldngylHQVTAGGRNLSAGQLQLLALARARLVDP 1098
Cdd:PRK09544 72 VPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAG-----------HLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 1108176189 1099 DILLLDEATVALD 1111
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
72-318 |
1.14e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 48.99 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 72 LLTYVRRYYGGRIAHLVQHDLRMDAFQALLRwdgrqQDR-W------SSGQLIVRTTNDLQLVQALLFDV-PNVLRHVLT 143
Cdd:cd18578 67 IAYFLQGYLFGIAGERLTRRLRKLAFRAILR-----QDIaWfddpenSTGALTSRLSTDASDVRGLVGDRlGLILQAIVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 144 LLLGVA-----------VMTWLSVPLALLAVLLVPVIGLIAHRSRRLLAAATHCAQEhkaavtgvvdaAVCGIRVVKAFG 212
Cdd:cd18578 142 LVAGLIiafvygwklalVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASE-----------AVSNIRTVASLT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 213 QEEretvKLVTASRALYAAQLRVARLNAHFGPLL----QTLPALGQMAVFALGGWMAAQGSITVGT-FVAFWAcLTLLAR 287
Cdd:cd18578 211 LED----YFLEKYEEALEEPLKKGLRRALISGLGfglsQSLTFFAYALAFWYGGRLVANGEYTFEQfFIVFMA-LIFGAQ 285
|
250 260 270
....*....|....*....|....*....|.
gi 1108176189 288 PACDLAGMLTIAQQARAGAVRVLELIDSRPT 318
Cdd:cd18578 286 SAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1080-1170 |
1.46e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1080 LSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQR--ATLTLAARRTTLIVAHGLAIAEH-ADRIVVLEHGTVV 1156
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRllTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTV 238
|
90
....*....|....
gi 1108176189 1157 EDGAHTELLAAGGH 1170
Cdd:PRK15093 239 ETAPSKELVTTPHH 252
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
216-851 |
1.61e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 49.49 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 216 RETVKLVTASRALYAAQLRVArlnAHFGPlLQTLPALGQMAVFALGGwmaaqgsitvgtfvafWACLTLLARPACDLAGM 295
Cdd:COG3321 774 RQPVRFADAVEALLADGVRVF---LEVGP-GPVLTGLVRQCLAAAGD----------------AVVLPSLRRGEDELAQL 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 296 LT-IAQQARAGAvrvlelidsrptLVDGTKPLSPEARlslefQRVSF-GYVADRPVLREISLSVRAGETLAVVGAPGSGK 373
Cdd:COG3321 834 LTaLAQLWVAGV------------PVDWSALYPGRGR-----RRVPLpTYPFQREDAAAALLAAALAAALAAAAALGALL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 374 STLASLATRCYDVTQGAVRIGGQDVRELTLDSLRSAIGLVPEDAVLFSGTIGANIAygRPDATPEQIATAARAAHIEEFV 453
Cdd:COG3321 897 LAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAA--AAALAAAEAGALLLLAAAAAAA 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 454 NTLPDGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAVIFTRRRSMLT 533
Cdd:COG3321 975 AAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAA 1054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 534 LADRVAVLDSGRLLDVGTPDEVWERCPRYRELLSPAPDLADDLVVAERSPVCRPVAGLGTKAAQHTNVHNPGPHDHPPGP 613
Cdd:COG3321 1055 AAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAA 1134
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 614 DPLRRLLREFRGPLALSLLLVAVQTCAGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTG 693
Cdd:COG3321 1135 AAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALA 1214
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 694 EQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFT 773
Cdd:COG3321 1215 ALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAA 1294
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 774 TMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALY 851
Cdd:COG3321 1295 AAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAA 1372
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
964-1158 |
1.71e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 964 LRIPA-GQTVVFVGSTGSGKSTLIKLVA--------RFYDPTHGTVRVD---GCDLREFDVDGYRNRLGIVTQEQYV--- 1028
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVdli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 ---FAGTVRDAIaygrpDATDaqvERAAREVgahpMITALD-NGYLHQVTAggrNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:cd03236 100 pkaVKGKVGELL-----KKKD---ERGKLDE----LVDQLElRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1105 EATVALDpateaVVQRATltlAARrttliVAHGLaiAEHADRIVVLEHGTVVED 1158
Cdd:cd03236 165 EPSSYLD-----IKQRLN---AAR-----LIREL--AEDDNYVLVVEHDLAVLD 203
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
641-916 |
1.92e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 47.90 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 641 GLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDG 720
Cdd:cd18783 18 ALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 721 DAQIVTAVtADVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIF----TTMPVLALATWQFRRASNWTYRRA 796
Cdd:cd18783 98 AGVLTKHM-QQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLafsaLIALIILAFLPPFRRRLQALYRAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 797 RHRLgtvtATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRA 876
Cdd:cd18783 177 GERQ----AFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFA 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1108176189 877 GVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAG 916
Cdd:cd18783 253 GSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVR 292
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
965-1150 |
2.08e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 965 RIPA---GQTVVFVGSTGSGKSTLIKLVA--------RFYD-PTHGTV--RVDGCDLREFDVDGYRNRLGIVTQEQYV-- 1028
Cdd:PRK13409 92 GLPIpkeGKVTGILGPNGIGKTTAVKILSgelipnlgDYEEePSWDEVlkRFRGTELQNYFKKLYNGEIKVVHKPQYVdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 ----FAGTVRDAIaygrpDATDaqvER-AAREVgahpmITALD-NGYLHQVTaggRNLSAGQLQLLALARARLVDPDILL 1102
Cdd:PRK13409 172 ipkvFKGKVRELL-----KKVD---ERgKLDEV-----VERLGlENILDRDI---SELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 1103 LDEATVALDpateaVVQRATLT-----LAARRTTLIVAHGLAIAEH-ADRIVVL 1150
Cdd:PRK13409 236 FDEPTSYLD-----IRQRLNVArlireLAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
231-309 |
2.08e-05 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 47.86 E-value: 2.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 231 AQLRVARLNAHFGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARAGAVRV 309
Cdd:cd18569 216 AQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
325-503 |
2.64e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 325 PLSPearLSLEFQRVSfgYVADRP--------------VLREISLSVRAGETLAVVGAPGSGKSTL----ASLATRCYdv 386
Cdd:PLN03140 862 PFTP---LAMSFDDVN--YFVDMPaemkeqgvtedrlqLLREVTGAFRPGVLTALMGVSGAGKTTLmdvlAGRKTGGY-- 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 387 TQGAVRIGGQDVRELTLdslrSAIGLVPEDAVLFSG--TIGANIAYGRPDATPEQIATAARAAHIEEF-----VNTLPDg 459
Cdd:PLN03140 935 IEGDIRISGFPKKQETF----ARISGYCEQNDIHSPqvTVRESLIYSAFLRLPKEVSKEEKMMFVDEVmelveLDNLKD- 1009
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1108176189 460 yqTAVGARGLT-LSGGQRQRIALARALLHQPRLLIMDDPTSAVDA 503
Cdd:PLN03140 1010 --AIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
444-502 |
2.80e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 444 ARAAHIEEFVNTLPDGYQTAVGarglTLSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATK----TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-500 |
3.60e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 350 LREISLSVRAGETLAVVGAPGSGKSTL----------ASlatrcYDvtqGAVRIGGQDVRELTL-DSLRSAI-------G 411
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLmkvlsgvyphGS-----YE---GEILFDGEVCRFKDIrDSEALGIviihqelA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 412 LVPEdavLfsgTIGANIAYGRPDATPEQI---ATAARAAHIEEFVNtLPDGYQTAVGARGLtlsgGQRQRIALARALLHQ 488
Cdd:NF040905 89 LIPY---L---SIAENIFLGNERAKRGVIdwnETNRRARELLAKVG-LDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170
....*....|..
gi 1108176189 489 PRLLIMDDPTSA 500
Cdd:NF040905 158 VKLLILDEPTAA 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
953-1134 |
3.61e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 953 TREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVA-RFYDPTH-GTVRVDGCDLREFDVdgyrNRLGIVTQEQYVFA 1030
Cdd:PLN03211 78 IQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNFtGTILANNRKPTKQIL----KRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1031 G-TVRDAIAYGR----PDATDAQVE-RAAREVGAHPMITALDNGYLHQVTAggRNLSAGQLQLLALARARLVDPDILLLD 1104
Cdd:PLN03211 154 HlTVRETLVFCSllrlPKSLTKQEKiLVAESVISELGLTKCENTIIGNSFI--RGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|
gi 1108176189 1105 EATVALDpATEAVVQRATLTLAARRTTLIV 1134
Cdd:PLN03211 232 EPTSGLD-ATAAYRLVLTLGSLAQKGKTIV 260
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
956-1161 |
5.88e-05 |
|
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: 47.13 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYdpTHGT----VRVDGCDLREFDV-DGYRNRLGIVTQE----- 1025
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY--PHGTwdgeIYWSGSPLKASNIrDTERAGIVIIHQEltlvp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1026 -----QYVFAGtvrDAIAYGRPDATDAQVERAAREVGAHPMITALDngylhqVTAGGRNLSAGQLQLLALARARLVDPDI 1100
Cdd:TIGR02633 92 elsvaENIFLG---NEITLPGGRMAYNAMYLRAKNLLRELQLDADN------VTRPVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 1101 LLLDEATVALDPATEAVVQRATLTLAARRTTLI-VAHGL-AIAEHADRIvvlehgTVVEDGAH 1161
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAHGVACVyISHKLnEVKAVCDTI------CVIRDGQH 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
314-504 |
9.06e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 314 DSRPTLVDGtkplspEARLSLEFQRVSFGyvaDRPVLREISLSVRAGETLAVVGAPGSGKSTLASLAT----RCY--DVT 387
Cdd:PRK10938 249 SARHALPAN------EPRIVLNNGVVSYN---DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYsnDLT 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 388 Q-GAVRIGGQdvrelTLDSLRSAIGLVPED------------AVLFSG---TIGanIAYGRPDAtpeQIATAARAAHIEE 451
Cdd:PRK10938 320 LfGRRRGSGE-----TIWDIKKHIGYVSSSlhldyrvstsvrNVILSGffdSIG--IYQAVSDR---QQKLAQQWLDILG 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 452 FVNTLPDgyqtavgARGLTLSGGQrQRIAL-ARALLHQPRLLIMDDPTSAVDAV 504
Cdd:PRK10938 390 IDKRTAD-------APFHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPL 435
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
963-1150 |
1.02e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 963 NLRIP-AGQTVVFVGSTGSGKSTLIKLVA--------RFY-DPTHGTV--RVDGCDLREFDVDGYRNRLGIVTQEQYV-- 1028
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSgelkpnlgDYDeEPSWDEVlkRFRGTELQDYFKKLANGEIKVAHKPQYVdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1029 ----FAGTVRDAIaygrpDATDaqvER-AAREVgahpmITALDNGYL--HQVtaggRNLSAGQLQLLALARARLVDPDIL 1101
Cdd:COG1245 172 ipkvFKGTVRELL-----EKVD---ERgKLDEL-----AEKLGLENIldRDI----SELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1102 LLDEATVALDpateaVVQRATltlAAR---------RTTLIVAHGLAIAEH-ADRIVVL 1150
Cdd:COG1245 235 FFDEPSSYLD-----IYQRLN---VARlirelaeegKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
352-542 |
1.42e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 44.71 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 352 EISLSVRAG-----ETLAVVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDV----RELTLDSLRSAiglvpeDAVLFSG 422
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKADYEGTV------RDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 423 TIGA-NIAYGRPD-ATPEQIATAaraahIEEFVNTLpdgyqtavgargltlSGGQRQRIALARALLHQPRLLIMDDPTSA 500
Cdd:cd03237 86 TKDFyTHPYFKTEiAKPLQIEQI-----LDREVPEL---------------SGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1108176189 501 VDAVIECGIQEVLREAI--ADRTAVIFTRRRSMLT-LADRVAVLD 542
Cdd:cd03237 146 LDVEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDyLADRLIVFE 190
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
333-555 |
1.77e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 333 SLEFQRVSFgYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLAS--------LATRCYDVTQGAVRIGGQDVRELTLD 404
Cdd:PRK10938 3 SLQISQGTF-RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARalagelplLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 405 S-LRSAIGLVPEDAVLFSGTIGANIAYGRPDatPEQIATAARAAHIEEFVNTlpdgyqtavgaRGLTLSGGQRQRIALAR 483
Cdd:PRK10938 82 EwQRNNTDMLSPGEDDTGRTTAEIIQDEVKD--PARCEQLAQQFGITALLDR-----------RFKYLSTGETRKTLLCQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1108176189 484 ALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAIADRTAV--IFTRRRSMLTLADRVAVLDSGRLLDVGTPDEV 555
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLvlVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
642-897 |
1.88e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 44.91 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 642 LLPPLLIRHGIDvgirrhvlsalwwaALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVV----------------F 705
Cdd:cd18560 13 VLAPLFLGRAVN--------------ALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLyrrvqqnayrelslktF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 706 AHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGL-----VVAVISVVTLV-----GILVALLAIRARLVLLIFTtm 775
Cdd:cd18560 79 AHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVfylvpTLLELIVVSVVfafhfGAWLALIVFLSVLLYGVFT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 776 pvLALATW--QFRRASNWTYRRARHRlgtVTATLREYAAglriAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYP 853
Cdd:cd18560 157 --IKVTEWrtKFRRAANKKDNEAHDI---AVDSLLNFET----VKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1108176189 854 FVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTP 897
Cdd:cd18560 228 GQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQP 271
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
704-918 |
2.42e-04 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 44.41 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 704 VFAHAQRLGLDAFEDDGDAQIVTAVTAdVEAIVAFLRTGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVLALATW 783
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDTVARVRE-LESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 784 ----QFRRASNwtyrrARHRLGTV-TATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALL 858
Cdd:cd18588 160 lvtpILRRRLE-----EKFQRGAEnQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLI 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 859 CSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18588 235 QKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
334-506 |
3.48e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 334 LEFQRVSFGYVADRPVLREISLSVRAGETLAVVGAPGSGKSTLASLATRCYDVTQGAVriggqdvreltldsLRSA---I 410
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAkvrM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 411 GLVPE---DAVLFSGTIGANIAYGRPDAtPEQiataARAAHIEEFVNTLPDGYQTAvgargLTLSGGQRQRIALARALLH 487
Cdd:PLN03073 575 AVFSQhhvDGLDLSSNPLLYMMRCFPGV-PEQ----KLRAHLGSFGVTGNLALQPM-----YTLSGGQKSRVAFAKITFK 644
|
170 180
....*....|....*....|....
gi 1108176189 488 QPRLLIMDDPTS-----AVDAVIE 506
Cdd:PLN03073 645 KPHILLLDEPSNhldldAVEALIQ 668
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
661-918 |
3.89e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 44.00 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 661 LSALWWAALAGTATVVIRWVVQwgsaMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVAFLR 740
Cdd:cd18589 36 TAAITVMSLLTIASAVSEFVCD----LIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 741 TGLVVAVISVVTLVGILVALLAIRARLVLLIFTTMPVL-----ALATWQFRRAsnwtyRRARHRLGTVTATLREYAAGLR 815
Cdd:cd18589 112 ENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLllvpkFVGKFQQSLA-----VQVQKSLARANQVAVETFSAMK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 816 IAQAFRAEYRGLQSYFAHSDDYRRLgvrgQRLLALYYP---FVALLCSLATTL-VLLDGAREVRAGVISVGALVTYLLYi 891
Cdd:cd18589 187 TVRSFANEEGEAQRYRQRLQKTYRL----NKKEAAAYAvsmWTSSFSGLALKVgILYYGGQLVTAGTVSSGDLVTFVLY- 261
|
250 260
....*....|....*....|....*...
gi 1108176189 892 ELLYTPIGE-LAQMFDDYQRAAVAAGRI 918
Cdd:cd18589 262 ELQFTSAVEvLLSYYPSVMKAVGSSEKI 289
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
916-1136 |
4.46e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 916 GRIRSLLSTRTPSSPAARPVGTLR---------GEVVFDA--VHYSYRTREVpaLAGINLRIPAGQTVVFVGSTGSGKST 984
Cdd:PRK11147 283 GRVRALKALRRERSERREVMGTAKmqveeasrsGKIVFEMenVNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 985 LIKLVARFYDPTHGTVRVdGCDLREFDVDGYRNRLgivTQEQyvfagTVRDAIAYGRPDATDAQVERaarevgaHPMita 1064
Cdd:PRK11147 361 LLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAEL---DPEK-----TVMDNLAEGKQEVMVNGRPR-------HVL--- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1065 ldnGYLHQ-----------VTAggrnLSAGQLQLLALARARLVDPDILLLDEATVALDPAT----EAVVQRATLTLaarr 1129
Cdd:PRK11147 422 ---GYLQDflfhpkramtpVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETlellEELLDSYQGTV---- 490
|
....*..
gi 1108176189 1130 ttLIVAH 1136
Cdd:PRK11147 491 --LLVSH 495
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
458-542 |
4.88e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 458 DGYQTAVGARGLTLSGGQRQRIALARALLHQPRLLIMDDPTSAVDAVIECGIQEVLREAI--ADRTAVIFTRRRSMLT-L 534
Cdd:cd03222 59 DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDyL 138
|
....*...
gi 1108176189 535 ADRVAVLD 542
Cdd:cd03222 139 SDRIHVFE 146
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
972-1123 |
6.97e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 41.96 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 972 VVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREF--------DVDGYRNrlGIVTQEqyvFAGT-VRDAIAYGRP 1042
Cdd:pfam06414 14 ILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELhphyrelqAADPKTA--SEYTQP---DASRwVEKLLQHAIE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1043 DATDAQVERAAR--EVGAHPMITALDNGYLHQV--TAGGRNLSagqlQLLALAR-------ARLVDPDIllLDEATVALD 1111
Cdd:pfam06414 89 NGYNIILEGTLRspDVAKKIARALKAAGYRVEVaaVAAPPELS----WLGVLDRyeeevaeGRYVPKEH--HDEAFNGLR 162
|
170
....*....|..
gi 1108176189 1112 PATEAVVQRATL 1123
Cdd:pfam06414 163 ESLRALERRKLL 174
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
24-310 |
7.10e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 42.89 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 24 FGAALAGTVIAVLVPLVTKRVIDDAIAadHRP---LAPWAVVLVAAAGATYLLTYVRRYyggriahLVQH-----DLRM- 94
Cdd:cd18783 8 AIASLILHVLALAPPIFFQIVIDKVLV--HQSystLYVLTIGVVIALLFEGILGYLRRY-------LLLVattriDARLa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 95 -DAFQALLRWDGRQQDRWSSGQLIVRTTNDLQLVQALLFDVPNVLRHVLTLLLGVAVMTWLSVPLALLAVLLVPVIGLIA 173
Cdd:cd18783 79 lRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 174 HRSRRLLAAATHCAQEHKAAVTGVVDAAVCGIRVVKAFGQE-ERETVKLVTASRALyAAQLRVARLNAHFGPLLQTLPAL 252
Cdd:cd18783 159 LAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEpRQRREWDERVARAI-RARFAVGRLSNWPQTLTGPLEKL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1108176189 253 GQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPACDLAGMLTIAQQARaGAVRVL 310
Cdd:cd18783 238 MTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEAR-LSVRML 294
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
661-918 |
7.36e-04 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 43.03 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 661 LSALWWAALAgtATVVIRWVVQ---WGSAmvagytGEQVLFRLRSVVFAHAQRLGLDAFEDDGDAQIVTAVTADVEAIVA 737
Cdd:cd18558 60 LYAYYYLIIG--AIVLITAYIQgsfWGLA------AGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 738 FLRTGLVVAVISVVTL-VGILVALlaIRA-RLVLLIFTTMPVLALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLR 815
Cdd:cd18558 132 GIGDKIGVIFQNIATFgTGFIIGF--IRGwKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 816 IAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLY 895
Cdd:cd18558 210 TVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGA 289
|
250 260
....*....|....*....|...
gi 1108176189 896 TPIGELAQMFDDYQRAAVAAGRI 918
Cdd:cd18558 290 FSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
639-901 |
1.06e-03 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 42.49 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 639 CAGLLPPLLIRHGIDVgirrhvLSALWWAALAGTATVVIRWVVQWGSA--------MVAGYTGEQVLFRLRSVVFAHAQR 710
Cdd:cd18582 10 LLNVAVPFLLKYAVDA------LSAPASALLAVPLLLLLAYGLARILSslfnelrdALFARVSQRAVRRLALRVFRHLHS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 711 LGLDAFEDDGDAQIVTAVTADVEAIVAFLRTGL---------VVAVISVVT-LVGILVALLAIRARLVLLIFTtmpvLAL 780
Cdd:cd18582 84 LSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLfnilptileLLLVCGILWyLYGWSYALITLVTVALYVAFT----IKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 781 ATW--QFRRASNWTYRRARHRLG-------TVtatlreyaaglriaQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALY 851
Cdd:cd18582 160 TEWrtKFRREMNEADNEANAKAVdsllnyeTV--------------KYFNNEEYEAERYDKALAKYEKAAVKSQTSLALL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1108176189 852 YPFVALLCSLATTLVLLDGAREVRAGVISVGALV---TYLLYielLYTPIGEL 901
Cdd:cd18582 226 NIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFVlvnTYLLQ---LYQPLNFL 275
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
958-1106 |
1.09e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 958 ALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRNRL-GIVTQE-QYVFAGTVRD 1035
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtGIENIElKGLMMGLTKE 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1108176189 1036 AIAygrpDATDAQVERAarEVGAhpmitaldngYLHQVTaggRNLSAGQLQLLALARARLVDPDILLLDEA 1106
Cdd:PRK13545 119 KIK----EIIPEIIEFA--DIGK----------FIYQPV---KTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
17-301 |
1.50e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 42.15 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 17 RRDLLLGFGAALAGTVIAVLVPLVTKRVIDDAIAADHRPLAPWAVVLVAAAGATYLL-TYVRRYYGGRIAHLVQHDLRMD 95
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLaGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 96 AFQALLRWDGRQQDRWSSGQLIVRTTNDL--------QLVQALLfDVPNVLRHVLTLLlgvaVMTWLSVPLALLAVLLVP 167
Cdd:cd18779 81 FLEHLLRLPYRFFQQRSTGDLLMRLSSNAtirelltsQTLSALL-DGTLVLGYLALLF----AQSPLLGLVVLGLAALQV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 168 VIGLIAHRSRRLLAAATHCAQehkAAVTGVVDAAVCGIRVVKAFGQEERetvklvTASR--ALYAAQLRVA----RLNAH 241
Cdd:cd18779 156 ALLLATRRRVRELMARELAAQ---AEAQSYLVEALSGIETLKASGAEDR------ALDRwsNLFVDQLNASlrrgRLDAL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 242 FGPLLQTLPALGQMAVFALGGWMAAQGSITVGTFVAFWACLTLLARPacdLAGMLTIAQQ 301
Cdd:cd18779 227 VDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAP---LASLVGTAQQ 283
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1080-1164 |
2.01e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.12 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1080 LSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAARRTTLIV-----AHGLAIaehADRIVVLEHGT 1154
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVvsselAEVLGL---SDRVLVIGEGK 480
|
90
....*....|
gi 1108176189 1155 VVEDGAHTEL 1164
Cdd:TIGR02633 481 LKGDFVNHAL 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
471-502 |
2.16e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|..
gi 1108176189 471 LSGGQRQRIALARALLHQPRLLIMDDPTSAVD 502
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
956-1153 |
2.45e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 956 VPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGcdlREFDVDGYRNR----LGIVTQE------ 1025
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQElnlipq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1026 ----QYVFAGtvRDAI-AYGRPDATDAQVEraarevgAHPMITALDNGYLHQVTAGgrNLSAGQLQLLALARARLVDPDI 1100
Cdd:PRK10762 94 ltiaENIFLG--REFVnRFGRIDWKKMYAE-------ADKLLARLNLRFSSDKLVG--ELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1108176189 1101 LLLDEATVAL-DPATEAVVQRATLTLAARRTTLIVAHGLA-IAEHADRIVVLEHG 1153
Cdd:PRK10762 163 IIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKeIFEICDDVTVFRDG 217
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
640-903 |
2.50e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 41.38 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 640 AGLLPPLLIRHGIDVGIRRHVLSALWWAALAGTATVVIRWVVQWGSAMVAGYTGEQVLFRLRSVVFAHAQRLGLDAFEDD 719
Cdd:cd18779 17 LGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 720 GDAQIVTAVTADVeAIVAFLRTGLVVAVISVVTLVGILVALLAIRARL--VLLIFTTMPVLALAtwqfrrasnWTYRRAR 797
Cdd:cd18779 97 STGDLLMRLSSNA-TIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLglVVLGLAALQVALLL---------ATRRRVR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 798 HRLGTVTAT-------LREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVALLCSLATTLVLLDG 870
Cdd:cd18779 167 ELMARELAAqaeaqsyLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVG 246
|
250 260 270
....*....|....*....|....*....|...
gi 1108176189 871 AREVRAGVISVGALVTYLLYIELLYTPIGELAQ 903
Cdd:cd18779 247 AWQVLDGQLSLGTMLALNALAGAFLAPLASLVG 279
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
365-401 |
2.98e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.04 E-value: 2.98e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1108176189 365 VVGAPGSGKSTLASLATRCYDVTQGAVRIGGQDVREL 401
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFREL 52
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1078-1136 |
3.55e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 3.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1108176189 1078 RNLSAGQLQLLALARARLVDPDILLLDEATVALDpaTEAVVQRATLTLAARRTTLIVAH 1136
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1075-1178 |
6.35e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1075 AGGR---NLSAGQLQLLALARARLVDPDILLLDEATVALDPATEAVVQRATLTLAAR-RTTLIVAHGLAIAEH-ADRIVV 1149
Cdd:NF000106 137 AAGRaaaKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTV 216
|
90 100 110
....*....|....*....|....*....|
gi 1108176189 1150 LEHGTVVEDGAHTEL-LAAGGHYSRLWAAH 1178
Cdd:NF000106 217 IDRGRVIADGKVDELkTKVGGRTLQIRPAH 246
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
959-986 |
6.42e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 6.42e-03
10 20
....*....|....*....|....*...
gi 1108176189 959 LAGINLRIPAGQTVVFVGSTGSGKSTLI 986
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
778-1177 |
8.82e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 40.63 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 778 LALATWQFRRASNWTYRRARHRLGTVTATLREYAAGLRIAQAFRAEYRGLQSYFAHSDDYRRLGVRGQRLLALYYPFVAL 857
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 858 LCSLATTLVLLDGAREVRAGVISVGALVTYLLYIELLYTPIGELAQMFDDYQRAAVAAGRIRSLLSTRTPSSPAARPVGT 937
Cdd:COG3321 941 ALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAA 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 938 LRGEVVFDAVHYSYRTREVPALAGINLRIPAGQTVVFVGSTGSGKSTLIKLVARFYDPTHGTVRVDGCDLREFDVDGYRN 1017
Cdd:COG3321 1021 LLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALA 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1018 RLGIVTQEQYVFAGTVRDAIAYGRPDATDAQVERAAREVGAHPMITALDNGYLHQVTAGGRNLSAGQLQLLALARARLVD 1097
Cdd:COG3321 1101 ALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALA 1180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1108176189 1098 PDILLLDEATVALDPATEAVVQRATLTLAARRTTLIVAHGLAIAEHADRIVVLEHGTVVEDGAHTELLAAGGHYSRLWAA 1177
Cdd:COG3321 1181 LAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA 1260
|
|
| |
