|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
116-696 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 613.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 116 WKLFWHFLHPHLLALGAAIVLALGAALVNVQIPLLLGQLVEIVAKytrdhmGSFVSESRKLSVQLLLLYGVQGLLTFGYL 195
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLA------GGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 196 VLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPR 275
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 276 LTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGR 355
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 356 GIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEYMALSP 435
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 436 VIPLTGGYcIPNKDIRGSITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL 515
Cdd:COG1132 323 EIPDPPGA-VPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 516 DGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLS 595
Cdd:COG1132 400 DGVDIRDLTLESLRRQ-IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 596 GGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTH 675
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570 580
....*....|....*....|.
gi 27753995 676 EELLKKGGLYSELIRRQTLDA 696
Cdd:COG1132 559 EELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
133-427 |
6.55e-165 |
|
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: 475.88 E-value: 6.55e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHMGSFVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKA 212
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 213 LFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGT 292
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 293 LMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMV 372
Cdd:cd18574 161 LYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 373 LGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18574 241 LGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-689 |
1.06e-159 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 478.06 E-value: 1.06e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 19 SLQSLRFQTFSAARSSDDRLSShllrtvaqlrvqlrahlprappaSHWSPSAWCWVGGtlvvpAVLWQHPRLCLIALCEA 98
Cdd:TIGR00958 84 SLSSLRALAFWEALDPAVRVAL-----------------------GLWSWFVWSYGAA-----LPAAALWAVLSSAGASE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 99 KESPPAQPTRAPELrfnWKLFwHFLHPHLLALGAAIVLALGAALVNVQIPLLLGQLVEIVakytrdhMGSFVSESRKLSV 178
Cdd:TIGR00958 136 KEAEQGQSETADLL---FRLL-GLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTL-------GGDKGPPALASAI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 179 QLLLLYGVQGLLTFG-----YLVLLSHIGERMamdmRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVIS 253
Cdd:TIGR00958 205 FFMCLLSIASSVSAGlrggsFNYTMARINLRI----REDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 254 QGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEK 333
Cdd:TIGR00958 281 VLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 334 REEERYQAELESC--CCKAEELGRgiALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLS 411
Cdd:TIGR00958 361 GEASRFKEALEETlqLNKRKALAY--AGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLS 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 412 VLFGQVVRGLSAGARVFEYMALSPVIPLTGGYCIPNkdIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQS 491
Cdd:TIGR00958 439 YVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLN--LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPS 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 492 GGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREAN 571
Cdd:TIGR00958 517 GSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQV-ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAAN 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 572 AHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEalDRASAGRTVLVIAHR 651
Cdd:TIGR00958 596 AHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHR 673
|
650 660 670
....*....|....*....|....*....|....*...
gi 27753995 652 LSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 689
Cdd:TIGR00958 674 LSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
120-692 |
4.19e-156 |
|
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: 464.17 E-value: 4.19e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 120 WHFLHPHLLALGAAIVLALGAALVNVQIPLLLGQLVeivakytrDHmgSFVSESRKLSVQ----LLLLYGVQGLLTFGYL 195
Cdd:TIGR02204 10 WPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMI--------DH--GFSKDSSGLLNRyfafLLVVALVLALGTAARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 196 VLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPR 275
Cdd:TIGR02204 80 YLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 276 LTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEELGR 355
Cdd:TIGR02204 160 LTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE----KAYEAAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 356 G-----IALFQGLSNIAFNCMVlGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEY 430
Cdd:TIGR02204 236 QrirtrALLTAIVIVLVFGAIV-GVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 431 MALSPVIPLTGGYCIPNKDIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA 510
Cdd:TIGR02204 315 LQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 511 GSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGER 590
Cdd:TIGR02204 395 GRILLDGVDLRQLDPAELR-ARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 591 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVC 670
Cdd:TIGR02204 474 GVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIV 553
|
570 580
....*....|....*....|..
gi 27753995 671 EAGTHEELLKKGGLYSELIRRQ 692
Cdd:TIGR02204 554 AQGTHAELIAKGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-693 |
1.20e-155 |
|
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: 467.77 E-value: 1.20e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 19 SLQSLRfqtfSAARSSDDRLSSHLLRTVAQlRVQLRAHLPRAPPAS----------HWSPSAWCWVGG------TLVVPA 82
Cdd:COG2274 32 SLEELR----EALGVSRDGLSLLGLLRAAR-RLGLRARGVRLDLEElaelplpailHWDGNHFVVLEGvdgdkvTIADPA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 83 vlwQHPRLCLIALCEAKES-------PPAQPTRAPELRFNWKLFWHFLHPHLLALGAAIVLALGAALVNVQIPLLLGQLV 155
Cdd:COG2274 107 ---TGRRKLSLEEFAESWTgvalllePTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 156 EIVAkytrdhmgsfVSESRK----LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTG 231
Cdd:COG2274 184 DRVL----------PNQDLStlwvLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 232 QLVSRlttdVQEFKSSFKLVISQGLRSCTQVIGSLVSLSML---SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQ 308
Cdd:COG2274 254 DLASR----FRDVESIREFLTGSLLTALLDLLFVLIFLIVLffySPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 309 IARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCcKAEELGRGIALFQGLSNIAFNCMV-LGTLFIGGSLVAGQQ 387
Cdd:COG2274 330 SAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL-NARFKLRRLSNLLSTLSGLLQQLAtVALLWLGAYLVIDGQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 388 LKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEYMALsPVIPLTGGYCIPNKDIRGSITFQNVTFSYPcRP 467
Cdd:COG2274 409 LTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL-PPEREEGRSKLSLPRLKGDIELENVSFRYP-GD 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTI 547
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSGTI 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 548 MENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 627
Cdd:COG2274 566 RENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAE 645
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 628 SERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQT 693
Cdd:COG2274 646 TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
454-692 |
6.51e-145 |
|
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: 422.72 E-value: 6.51e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvI 533
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 613
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 614 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 692
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
116-692 |
7.38e-132 |
|
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: 401.79 E-value: 7.38e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 116 WKLFWHFLHPHLLALGAAIVLALGAALVNVQIPLLLgqlveivaKYTRDHMGSFVSESRKLSVQLLL--LYGVQGLLTFG 193
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALL--------KPLLDDGFGGRDRSVLWWVPLVVigLAVLRGICSFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 194 YLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSS----FKLVISQGLrsctQVIGSLVSL 269
Cdd:TIGR02203 74 STYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdaFIVLVRETL----TVIGLFIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 270 SMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCK 349
Cdd:TIGR02203 150 LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 350 AEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFE 429
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 430 YMAlSPVIPLTGGYCIPNkdIRGSITFQNVTFSYPCRpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPE 509
Cdd:TIGR02203 310 LLD-SPPEKDTGTRAIER--ARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 510 AGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKL-DASDEEVYTAAREANAHEFISSFPDGYSTVVG 588
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQ-VALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 589 ERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQ 668
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|....
gi 27753995 669 VCEAGTHEELLKKGGLYSELIRRQ 692
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
454-688 |
5.09e-122 |
|
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: 363.86 E-value: 5.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvI 533
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 613
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 614 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSEL 688
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
101-692 |
1.13e-121 |
|
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: 376.47 E-value: 1.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 101 SPPAQPTRAPELRFNWKLFWHFLHPHLLALGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHMGSFVsesrkLSVQL 180
Cdd:COG5265 6 AMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLV-----VPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 181 LLLYGVQGLLT--FGYL--VLLSHIGERMamdMRK-AL--FSSLLRQDIAFFDAKKTGQLvSRlttdvqefkssfklVIS 253
Cdd:COG5265 81 LLAYGLLRLLSvlFGELrdALFARVTQRA---VRRlALevFRHLHALSLRFHLERQTGGL-SR--------------DIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 254 QGLRSctqvIGSLVSLSMLS--P---RLTLMLAV--------------VTPALMGVGTLMGSGLR-KLSRQCQEQIARAT 313
Cdd:COG5265 143 RGTKG----IEFLLRFLLFNilPtllEIALVAGIllvkydwwfalitlVTVVLYIAFTVVVTEWRtKFRREMNEADSEAN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 314 GVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDL 393
Cdd:COG5265 219 TRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 394 MsfLVASQTVQRSMA--SLSVLFGQVVRGLSAGARVFEYMALSPVI-------PLTGGycipnkdiRGSITFQNVTFSY- 463
Cdd:COG5265 299 V--LVNAYLIQLYIPlnFLGFVYREIRQALADMERMFDLLDQPPEVadapdapPLVVG--------GGEVRFENVSFGYd 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 464 PCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLF 543
Cdd:COG5265 369 PERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR-AAIGIVPQDTVLF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 544 ATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 623
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 624 LDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 692
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
454-692 |
6.44e-116 |
|
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: 348.07 E-value: 6.44e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 533
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR-RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 613
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 614 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 692
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
115-692 |
1.66e-107 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 338.92 E-value: 1.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 115 NWKLF---WHFLHPHLLALGAAIV-LALGAALVNVQIPLLLGQLVEIVAKYTRDHMgsfvsesRKLSVQLLLLYGVQGLL 190
Cdd:PRK11176 9 TWQTFrrlWPTIAPFKAGLIVAGVaLILNAASDTFMLSLLKPLLDDGFGKADRSVL-------KWMPLVVIGLMILRGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 191 TFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLS 270
Cdd:PRK11176 82 SFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 271 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYqaelESCCCKA 350
Cdd:PRK11176 162 YYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRF----DKVSNRM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 351 EELGRGIALFQGLSN-----IAFNCMVLgTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGA 425
Cdd:PRK11176 238 RQQGMKMVSASSISDpiiqlIASLALAF-VLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 426 RVFEYMALSPVIPlTGGYCIpnKDIRGSITFQNVTFSYPCR--PGfnvLKDFTLKLPSGKIVALVGQSGGGKTTVASLLE 503
Cdd:PRK11176 317 TLFAILDLEQEKD-EGKRVI--ERAKGDIEFRNVTFTYPGKevPA---LRNINFKIPAGKTVALVGRSGSGKSTIANLLT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 504 RFYDPEAGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATTIMENIRFGKLDA-SDEEVYTAAREANAHEFISSFPDG 582
Cdd:PRK11176 391 RFYDIDEGEILLDGHDLRDYTLASLRNQV-ALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 583 YSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSII 662
Cdd:PRK11176 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIL 549
|
570 580 590
....*....|....*....|....*....|
gi 27753995 663 VMANGQVCEAGTHEELLKKGGLYSELIRRQ 692
Cdd:PRK11176 550 VVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
129-683 |
2.24e-107 |
|
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: 337.89 E-value: 2.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 129 ALGAAIVLALGAALVNVQIPLLLGQLVE--IVAKYTRDHMGSFVsesrklsVQLLLLYGVQGLLTFGYLVLLSHIGERMA 206
Cdd:COG4988 18 WLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLSALLPLL-------GLLLAVLLLRALLAWLRERAAFRAAARVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 207 MDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPA 286
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 287 LMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAElesccckAEELGRG------IALf 360
Cdd:COG4988 171 IPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEA-------SEDFRKRtmkvlrVAF- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 361 qgLSN-----IAFNCMVLGTLFIGGSLVAGQqlkggdlMSFLVAsqtvqrsmasLSVL-----FGQVVR----------- 419
Cdd:COG4988 243 --LSSavlefFASLSIALVAVYIGFRLLGGS-------LTLFAA----------LFVLllapeFFLPLRdlgsfyharan 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 420 GLSAGARVFEYMALSPVIPLTGGYCIPNKDIrGSITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVA 499
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 500 SLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSF 579
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAAL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 580 PDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAH 659
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
|
570 580
....*....|....*....|....
gi 27753995 660 SIIVMANGQVCEAGTHEELLKKGG 683
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
204-691 |
8.81e-105 |
|
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: 331.35 E-value: 8.81e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 204 RMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVv 283
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLAL- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 284 tpALMGVGTLMGSGLRKLSRQCQEQIARATG----VADEALGNVRTVRAFAMEKREEERYQAeLESCCCKAEE-LGRGIA 358
Cdd:COG4987 164 --GLLLAGLLLPLLAARLGRRAGRRLAAARAalraRLTDLLQGAAELAAYGALDRALARLDA-AEARLAAAQRrLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 359 LFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEYMALSPVIP 438
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 439 LTGGYCIPNKDirGSITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGH 518
Cdd:COG4987 321 EPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 519 DLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQ 598
Cdd:COG4987 398 DLRDLDEDDLR-RRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|...
gi 27753995 679 LKKGGLYSELIRR 691
Cdd:COG4987 557 LAQNGRYRQLYQR 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
452-683 |
4.53e-102 |
|
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: 312.24 E-value: 4.53e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQ 531
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 vIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:cd03254 79 -IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGG 683
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
265-705 |
6.89e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 303.42 E-value: 6.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 265 SLVSLSMLSP-------RLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAmekreee 337
Cdd:PRK13657 140 TLVALVVLLPlalfmnwRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYN------- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 338 RYQAELESCCCKAEELGRG-------IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL-VASQTVQRsmas 409
Cdd:PRK13657 213 RIEAETQALRDIADNLLAAqmpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGR---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 410 LSVLFGQVVRGLSAGARVFEYMALSPVIPLTG--GYCIPNKDIRGSITFQNVTFSYP-CRPGfnvLKDFTLKLPSGKIVA 486
Cdd:PRK13657 289 LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRdpPGAIDLGRVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 487 LVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTA 566
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR-RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 567 AREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVL 646
Cdd:PRK13657 445 AERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTF 524
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 647 VIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ--TLDASLTSTPPAE 705
Cdd:PRK13657 525 IIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQgmLQEDERRKQPAAE 585
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
454-692 |
1.69e-93 |
|
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: 290.16 E-value: 1.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYpcRP-GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQV 532
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 iGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQP 612
Cdd:cd03252 79 -GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 613 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 692
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
448-669 |
5.62e-88 |
|
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: 275.50 E-value: 5.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 448 KDIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSW 527
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 528 LRGQViGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARA 607
Cdd:cd03248 86 LHSKV-SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 608 LIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 669
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
133-427 |
1.26e-84 |
|
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: 269.04 E-value: 1.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVEIVakYTRDHMGSFVsesrKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKA 212
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTI--IKGGDLDVLN----ELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 213 LFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGT 292
Cdd:cd18557 75 LFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 293 LMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMV 372
Cdd:cd18557 155 IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 373 LGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18557 235 LLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
119-690 |
3.84e-82 |
|
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: 275.28 E-value: 3.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 119 FWHFLHPHLLALGAAIVLALGAALVNVQIPLLLGQLVEI-VAKYTRDHMGSFVsesRKLSVQLLLLYGVQGLLTFGYLVL 197
Cdd:TIGR03796 141 LLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIfVDEILVQGRQDWL---RPLLLGMGLTALLQGVLTWLQLYY 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 198 LSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTD--VQEFKSSfklVISQGLRSCTQVIGSLVSLSMLSPR 275
Cdd:TIGR03796 218 LRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNdqVAEFLSG---QLATTALDAVMLVFYALLMLLYDPV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 276 LTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEER---YQAELEScccKAEE 352
Cdd:TIGR03796 295 LTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRwagYQAKLLN---AQQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 353 LGRGIALFQGLSNI--AFNCMVLgtLFIGGSLVAGQQLKGGDLmsflVASQTVqrsMASLS------VLFGQVVRGLSAG 424
Cdd:TIGR03796 372 LGVLTQILGVLPTLltSLNSALI--LVVGGLRVMEGQLTIGML----VAFQSL---MSSFLepvnnlVGFGGTLQELEGD 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 425 ARVFEYMALSPVIPL------TGGYCIPNKDIRGSITFQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTV 498
Cdd:TIGR03796 443 LNRLDDVLRNPVDPLleepegSAATSEPPRRLSGYVELRNITFGYS-PLEPPLIENFSLTLQPGQRVALVGGSGSGKSTI 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 499 ASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISS 578
Cdd:TIGR03796 522 AKLVAGLYQPWSGEILFDGIPREEIPREVLANSV-AMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITS 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 579 FPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsaGRTVLVIAHRLSTVRAA 658
Cdd:TIGR03796 601 RPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDC 678
|
570 580 590
....*....|....*....|....*....|..
gi 27753995 659 HSIIVMANGQVCEAGTHEELLKKGGLYSELIR 690
Cdd:TIGR03796 679 DEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
454-668 |
3.73e-80 |
|
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: 252.69 E-value: 3.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvI 533
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIrfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPT 613
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 614 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQ 668
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
125-705 |
2.86e-76 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 256.57 E-value: 2.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 125 PHLLALGAAIVLALGAALVNVQIPLLLgqlveivaKYTRDHMgsfVSESR-------KLSVQLLLLYGVQGLLTFGYLVL 197
Cdd:PRK10790 20 PWRKPLGLAVLMLWVAAAAEVSGPLLI--------SYFIDNM---VAKGNlplglvaGLAAAYVGLQLLAAGLHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 198 LSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLT 277
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 278 LMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEER--------YQAELescccK 349
Cdd:PRK10790 169 LVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERmgeasrshYMARM-----Q 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 350 AEELgRGIALFQGLSniAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL---------VASQTVQRSMASLSVLfgqvvrg 420
Cdd:PRK10790 244 TLRL-DGFLLRPLLS--LFSALILCGLLMLFGFSASGTIEVGVLYAFIsylgrlnepLIELTTQQSMLQQAVV------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 421 lsAGARVFEYMAlSP-------VIPLTGGycipnkdirgSITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGG 493
Cdd:PRK10790 314 --AGERVFELMD-GPrqqygndDRPLQSG----------RIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 494 GKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKlDASDEEVYTAAREANAH 573
Cdd:PRK10790 379 GKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR-QGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 574 EFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS 653
Cdd:PRK10790 457 ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLS 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 27753995 654 TVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQTLDASLTSTPPAE 705
Cdd:PRK10790 537 TIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREE 588
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
130-692 |
2.49e-73 |
|
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: 251.03 E-value: 2.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVeivakytrdhmGSFVSES-RKLSVQLLLLYGVQGLLTFGY-----LVLLsHIGE 203
Cdd:TIGR03797 138 LLAILAMGLLGTLLGMLVPIATGILI-----------GTAIPDAdRSLLVQIALALLAAAVGAAAFqlaqsLAVL-RLET 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 204 RMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRlttdVQEFKSSFKLVISQGLRSCTQVIGSLVSLSML---SPRLTLML 280
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASR----AMGISQIRRILSGSTLTTLLSGIFALLNLGLMfyySWKLALVA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 281 AVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERY------QAELEScccKAEELG 354
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWaklfsrQRKLEL---SAQRIE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 355 RGIALFqglsNIAFNCMVLGTLF-IGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVrglsagARVFEYMAL 433
Cdd:TIGR03797 359 NLLTVF----NAVLPVLTSAALFaAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISIL------AVIPLWERA 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 434 SPV---IPLTGGYCIPNKDIRGSITFQNVTFSYPCRpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA 510
Cdd:TIGR03797 429 KPIleaLPEVDEAKTDPGKLSGAIEVDRVTFRYRPD-GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPES 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 511 GSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIrFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGER 590
Cdd:TIGR03797 508 GSVFYDGQDLAGLDVQAVRRQ-LGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEG 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 591 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRtvLVIAHRLSTVRAAHSIIVMANGQVC 670
Cdd:TIGR03797 586 GGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVV 663
|
570 580
....*....|....*....|..
gi 27753995 671 EAGTHEELLKKGGLYSELIRRQ 692
Cdd:TIGR03797 664 QQGTYDELMAREGLFAQLARRQ 685
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
189-706 |
1.51e-71 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 243.47 E-value: 1.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 189 LLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQefkssfKLVISQGLRSCT----QVIG 264
Cdd:PRK10789 51 LLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVD------RVVFAAGEGVLTlvdsLVMG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 265 SLVSLSM---LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQA 341
Cdd:PRK10789 125 CAVLIVMstqISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 342 ELESCCCKAEELGRGIALFQ-------GLSNIafncmvlgtLFIGGS--LVAGQQLKGGDLMSFLVASQTVQRSMASLSV 412
Cdd:PRK10789 205 DAEDTGKKNMRVARIDARFDptiyiaiGMANL---------LAIGGGswMVVNGSLTLGQLTSFVMYLGLMIWPMLALAW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 413 LFGQVVRGLSAGARVFEYMALSPVIpLTGGYCIPNKdiRGSITFQNVTFSYP--CRPgfnVLKDFTLKLPSGKIVALVGQ 490
Cdd:PRK10789 276 MFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEG--RGELDVNIRQFTYPqtDHP---ALENVNFTLKPGQMLGICGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 491 SGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREA 570
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 571 NAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAH 650
Cdd:PRK10789 429 SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 651 RLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQTLDASLTSTPPAEK 706
Cdd:PRK10789 509 RLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDAPEIRE 564
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
133-427 |
2.68e-71 |
|
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: 233.95 E-value: 2.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHmGSFVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKA 212
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDI-EIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 213 LFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGT 292
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 293 LMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMV 372
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 373 LGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
176-681 |
8.36e-71 |
|
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: 241.19 E-value: 8.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDiAFFDAKKTGQLVSRLTTdVQEFKSSfklvisqg 255
Cdd:COG4618 62 LTLLALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAA-LRGGGGAAAQALRDLDT-LRQFLTG-------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 lrsctQVIGS----------LVSLSMLSPRLTLMlavvtpALMGVGTLMGSGL------RKLSRQCQEQIARATGVADEA 319
Cdd:COG4618 132 -----PGLFAlfdlpwapifLAVLFLFHPLLGLL------ALVGALVLVALALlnerltRKPLKEANEAAIRANAFAEAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 320 LGNVRTVRAFAMEKREEERYQAElescccKAEELGRGI------ALFQGLS---NIAFNCMVLGTlfiGGSLVAGQQLKG 390
Cdd:COG4618 201 LRNAEVIEAMGMLPALRRRWQRA------NARALALQArasdraGGFSALSkflRLLLQSAVLGL---GAYLVIQGEITP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 391 GDLM--SFLVAsqtvqRSMASLSVLFG---QVVRGLSAGARVFEYMALSPVIPLTggycIPNKDIRGSITFQNVTFSYPC 465
Cdd:COG4618 272 GAMIaaSILMG-----RALAPIEQAIGgwkQFVSARQAYRRLNELLAAVPAEPER----MPLPRPKGRLSVENLTVVPPG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 --RPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLrGQVIGFISQEPVLF 543
Cdd:COG4618 343 skRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-GRHIGYLPQDVELF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 544 ATTIMENI-RFGklDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:COG4618 419 DGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 623 ALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKK 681
Cdd:COG4618 497 NLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
452-669 |
3.81e-69 |
|
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: 225.55 E-value: 3.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQ 531
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 669
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
176-681 |
1.35e-67 |
|
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: 231.85 E-value: 1.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDaKKTGQLVSRLTTdVQEFKSSFKLVisqG 255
Cdd:TIGR01842 48 LTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRRGS-GDGLQALRDLDQ-LRQFLTGPGLF---A 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKRE 335
Cdd:TIGR01842 123 FFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 336 EERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGdlmSFLVASQTVQRSMASLSVLFG 415
Cdd:TIGR01842 203 TKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPG---MMIAGSILVGRALAPIDGAIG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 416 ---QVVRGLSAGARVFEYMALSP----VIPLtggyciPNKdiRGSITFQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALV 488
Cdd:TIGR01842 280 gwkQFSGARQAYKRLNELLANYPsrdpAMPL------PEP--EGHLSVENVTIVPP-GGKKPTLRGISFSLQAGEALAII 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 489 GQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLrGQVIGFISQEPVLFATTIMENI-RFGKlDASDEEVYTAA 567
Cdd:TIGR01842 351 GPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF-GKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 568 REANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVL 646
Cdd:TIGR01842 429 KLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVV 508
|
490 500 510
....*....|....*....|....*....|....*
gi 27753995 647 VIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKK 681
Cdd:TIGR01842 509 VITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
452-674 |
9.77e-66 |
|
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: 216.59 E-value: 9.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG 530
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QvIGFISQEPVLFATTIMENIR-FGKldASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALI 609
Cdd:cd03244 79 R-ISIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 610 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGT 674
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
132-664 |
2.73e-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: 225.24 E-value: 2.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 132 AAIVLALGAALVNVQIPLLLGQ---LVEIVAKYTRDhmGSFVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMD 208
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQawlLARVVDGLISA--GEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 209 MRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQgLRSCtqVIGSLVSLSML---SPRLTLMLAVVTP 285
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQ-LVLA--VIVPLAILAAVfpqDWISGLILLLTAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 286 ALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAElesccckAEELGRG------IAL 359
Cdd:TIGR02857 156 LIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRS-------SEEYRERtmrvlrIAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 360 fqgLSNIAFNcmVLGTL-------FIGGSLVAGQQLKGGDLMSFLVASQTVQrSMASLSVLFGQVVRGLSAGARVFEYMA 432
Cdd:TIGR02857 229 ---LSSAVLE--LFATLsvalvavYIGFRLLAGDLDLATGLFVLLLAPEFYL-PLRQLGAQYHARADGVAAAEALFAVLD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 433 LSPViPLTGGYCIPNKDIRgSITFQNVTFSYPCRPgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGS 512
Cdd:TIGR02857 303 AAPR-PLAGKAPVTAAPAS-SLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 513 VTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGT 592
Cdd:TIGR02857 379 IAVNGVPLADADADSWRDQ-IAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 593 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVM 664
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
197-652 |
2.67e-64 |
|
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: 222.62 E-value: 2.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 197 LLSH-IGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPR 275
Cdd:TIGR02868 75 LVGHdAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 276 LTLMLAvvtpALMGVGTLMGSGLRKLSRQCQEQIARA-----TGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 350
Cdd:TIGR02868 155 AALILA----AGLLLAGFVAPLVSLRAARAAEQALARlrgelAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 351 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEY 430
Cdd:TIGR02868 231 RRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 431 MALSP-----VIPLTGGYciPNKDIRgsITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF 505
Cdd:TIGR02868 311 LDAAGpvaegSAPAAGAV--GLGKPT--LELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 506 YDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYST 585
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDT 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 586 VVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 652
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
176-689 |
6.25e-64 |
|
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: 225.77 E-value: 6.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQG 255
Cdd:TIGR01193 198 ISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLF 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LRSCTQVIGSLVsLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEkre 335
Cdd:TIGR01193 278 LDMWILVIVGLF-LVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSE--- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 336 EERYQ---AELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSF--LVASQT-------- 402
Cdd:TIGR01193 354 AERYSkidSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFnaLLSYFLtpleniin 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 403 VQRSMASLSVlfgqvvrglsAGARVFE-YMALSPVIplTGGYCIPNKDIRGSITFQNVTFSYpcrpGF--NVLKDFTLKL 479
Cdd:TIGR01193 434 LQPKLQAARV----------ANNRLNEvYLVDSEFI--NKKKRTELNNLNGDIVINDVSYSY----GYgsNILSDISLTI 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 480 PSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFG-KLDA 558
Cdd:TIGR01193 498 KMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR-QFINYLPQEPYIFSGSILENLLLGaKENV 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 559 SDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR 638
Cdd:TIGR01193 577 SQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 27753995 639 ASAgRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 689
Cdd:TIGR01193 657 LQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
474-695 |
2.69e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 213.17 E-value: 2.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 474 DFTLklPSGKIVALVGQSGGGKTTVASLLERFYdPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRF 553
Cdd:PRK11174 370 NFTL--PAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 554 GKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQ 633
Cdd:PRK11174 446 GNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 634 EALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQTLD 695
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
133-427 |
7.23e-60 |
|
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: 203.48 E-value: 7.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVEIVakytrdHMGSFVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKA 212
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAA------LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 213 LFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGT 292
Cdd:cd18576 75 LYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 293 LMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMV 372
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 373 LGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18576 235 VAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
133-427 |
9.95e-60 |
|
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: 203.16 E-value: 9.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVEIVAkytrdHMGSFVSESRklSVQLLLLYGV-QGLLTFGYLVLLSHIGERMAMDMRK 211
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVV-----ADGSREAFYR--AVLLLLLLSVlSGLFSGLRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 212 ALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVG 291
Cdd:cd18572 74 DLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 292 TLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCM 371
Cdd:cd18572 154 KVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 372 VLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18572 234 QVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
132-427 |
2.30e-56 |
|
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: 194.01 E-value: 2.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 132 AAIVLALGAALvNVQIPLLLGQLVEIVAKYTRDHMGSFVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRK 211
Cdd:cd18780 1 GTIALLVSSGT-NLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 212 ALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVG 291
Cdd:cd18780 80 RLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 292 TLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCM 371
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 372 VLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18780 240 IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
130-427 |
2.57e-56 |
|
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: 194.23 E-value: 2.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHMGS--FVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAM 207
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 208 DMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVsLSM-LSPRLTLMLAVVTPA 286
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFI-IAFiYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 287 LMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEELGRGIALFQGLSNI 366
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE----KARKAGIKKGLVSGLGLG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 367 AFNCMVLGT----LFIGGSLVAGQQLKGGD----LMSFLVASQTVQRSMASLSVLfgqvVRGLSAGARV 427
Cdd:cd18577 236 LLFFIIFAMyalaFWYGSRLVRDGEISPGDvltvFFAVLIGAFSLGQIAPNLQAF----AKARAAAAKI 300
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
336-692 |
7.87e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 200.44 E-value: 7.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 336 EERYQAELESCCCKAEELGRGIALFQGLSN---IAFNCM-VLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLS 411
Cdd:PRK11160 219 EDRYRQQLEQTEQQWLAAQRRQANLTGLSQalmILANGLtVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 412 VLF---GQVVrglSAGARVFEYMALSPVIPLTGGYCIPNKdiRGSITFQNVTFSYPCRPgFNVLKDFTLKLPSGKIVALV 488
Cdd:PRK11160 299 GAFqhlGQVI---ASARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 489 GQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAR 568
Cdd:PRK11160 373 GRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR-QAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQ 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 569 EANAHEFISSfPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVI 648
Cdd:PRK11160 452 QVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 27753995 649 AHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 692
Cdd:PRK11160 531 THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
180-716 |
2.67e-55 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 205.65 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 180 LLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 259
Cdd:PTZ00265 103 LVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 260 TQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLrKLSRQCQEQIARAT-GVADEALGNVRTVRAFAMEKREEER 338
Cdd:PTZ00265 183 SAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV-KINKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 339 YQAElESCCCK-------AEELGrgIALFQG--LSNIAFNcMVLGTLFIGGSLVAGQ---QLKGGDLMSFLVAsqtVQRS 406
Cdd:PTZ00265 262 FNLS-EKLYSKyilkanfMESLH--IGMINGfiLASYAFG-FWYGTRIIISDLSNQQpnnDFHGGSVISILLG---VLIS 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 407 MASLSVLFGQV---VRGLSAGARVFEYMALSPVIPLTG-GYCIPnkDIRgSITFQNVTFSYPCRPGFNVLKDFTLKLPSG 482
Cdd:PTZ00265 335 MFMLTIILPNIteyMKSLEATNSLYEIINRKPLVENNDdGKKLK--DIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEG 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 483 KIVALVGQSGGGKTTVASLLERFYDPEAGSVTL-DGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFG-----KL 556
Cdd:PTZ00265 412 KTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK-IGVVSQDPLLFSNSIKNNIKYSlyslkDL 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 557 DA----------------------------------------------------SDEEVYTAAREANAHEFISSFPDGYS 584
Cdd:PTZ00265 491 EAlsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 585 TVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSII 662
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIF 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 663 VMANGQ-----------------------------------------------VCEAGTHEELLK-KGGLYSELIRRQTL 694
Cdd:PTZ00265 651 VLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKnKNGIYYTMINNQKV 730
|
650 660
....*....|....*....|..
gi 27753995 695 DASLTSTPPAEKPEDPKSCQSK 716
Cdd:PTZ00265 731 SSKKSSNNDNDKDSDMKSSAYK 752
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
201-690 |
6.49e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 201.41 E-value: 6.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 201 IGERMAMDMRKALFSSLLRQDIAFFDAKKT--GQLVSRLTTDVQEFKSsfklvisqGLRSCTQVIGSLVSLSMLSPRLTL 278
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKT--------GLVNNIVIFTHFIVLFLVSMVMSF 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 279 MLAVVTPALMgVGTLMgSGLRKLSrqCQEQIARATGVADEALGNVRTVRAFAMEKR---------EEERYQAE------L 343
Cdd:PTZ00265 965 YFCPIVAAVL-TGTYF-IFMRVFA--IRARLTANKDVEKKEINQPGTVFAYNSDDEifkdpsfliQEAFYNMNtviiygL 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 344 ESCCCKAEELGRGIALFQGLSNIAFNCMVLG-----TLFI-------GGSLVAGQQLKGGDLMSFLVASQTVQRSMASLS 411
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGfsqsaQLFInsfaywfGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 412 VLFGQVVRGLSAGARVFEYMALSPVIPL--TGGYCIPNK-DIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALV 488
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIRIKNKnDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 489 GQSGGGKTTVASLLERFYD------------------------------------------------------PEAGSVT 514
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKIL 1280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 515 LDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTL 594
Cdd:PTZ00265 1281 LDGVDICDYNLKDLR-NLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSL 1359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 595 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEAL--DRASAGRTVLVIAHRLSTVRAAHSIIVMAN----GQ 668
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGS 1439
|
570 580
....*....|....*....|....
gi 27753995 669 VCEA-GTHEELLK-KGGLYSELIR 690
Cdd:PTZ00265 1440 FVQAhGTHEELLSvQDGVYKKYVK 1463
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
130-427 |
6.43e-52 |
|
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: 181.85 E-value: 6.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHMGSFVSesrklsVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVP------LAIIGLFLLRGLASYLQTYLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEELGRGIALFQGLSN---- 365
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANE----RLRRLSMKIARARALSSplme 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 366 IAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
86-698 |
3.02e-50 |
|
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: 190.54 E-value: 3.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 86 QHPRLCLIALCEAKESPPA--QPTRAPELRFNWKLFWHFLHphllALGAAIVLALgaalvnvqIPLLLGQLVEIVAK--- 160
Cdd:TIGR00957 920 HHGSSAELQKAEAKEETWKlmEADKAQTGQVELSVYWDYMK----AIGLFITFLS--------IFLFVCNHVSALASnyw 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 161 ---YTRDHMGSFVSESRKLSVQLLLLYGV-QGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSR 236
Cdd:TIGR00957 988 lslWTDDPMVNGTQNNTSLRLSVYGALGIlQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNR 1067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 237 LTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPrltlMLAVVTPALMGVGTLMGSGLRKLSRQCQ--EQIARATG 314
Cdd:TIGR00957 1068 FSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATP----IAAVIIPPLGLLYFFVQRFYVASSRQLKrlESVSRSPV 1143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 315 VA--DEALGNVRTVRAFamEKREEERYQAEL-----ESCCCKAEELGRGIALfqGLSNIAfNCMVL-GTLFiggSLVAGQ 386
Cdd:TIGR00957 1144 YShfNETLLGVSVIRAF--EEQERFIHQSDLkvdenQKAYYPSIVANRWLAV--RLECVG-NCIVLfAALF---AVISRH 1215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 387 QLKGGdLMSFLVA-SQTVQRSMASLSVLFGQVVRGLSAGARVFEYMALSPVIPLTGGYCIPNKDI--RGSITFQNVTFSY 463
Cdd:TIGR00957 1216 SLSAG-LVGLSVSySLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWppRGRVEFRNYCLRY 1294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 464 pcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVL 542
Cdd:TIGR00957 1295 --REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK-ITIIPQDPVL 1371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 543 FATTIMENIR-FGKLdaSDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 621
Cdd:TIGR00957 1372 FSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 622 SALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRrqtlDASL 698
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK----DAGL 1522
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
130-407 |
5.62e-50 |
|
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: 175.91 E-value: 5.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHmgsfVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE----TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCcckaEELGRGIALFQGLSNIA-- 367
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEA----LKAGIKKAVANGLSFGItq 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 27753995 368 --FNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSM 407
Cdd:pfam00664 233 fiGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
130-427 |
1.73e-49 |
|
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: 175.05 E-value: 1.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKytRDHMGSFVsesrKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIP--AGDLSLLL----WIALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFN 369
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 370 CMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
454-681 |
7.65e-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: 168.66 E-value: 7.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVi 533
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPV--LFATTIMENIRFG--KLDASDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQRLAIA 605
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 606 RALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 681
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
130-427 |
1.73e-47 |
|
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: 169.54 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKytrdhmGSFVSesrKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSA------GGSSG---GLLALLVALFLLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFN 369
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 370 CMVLGTLFIGGSLVAGQQLKGGDLMSFLV-ASQTVQrSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18551 232 LALLVVLGVGGARVASGALTVGTLVAFLLyLFQLIT-PLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
454-678 |
2.58e-45 |
|
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: 161.58 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD-----PEAGSVTLDGHDLRTL--NPS 526
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 WLRGQViGFISQEPVLFATTIMENIRFG-KL------DASDEEVYTAAREANAHEFISSFPDGYStvvgergttLSGGQK 599
Cdd:cd03260 78 ELRRRV-GMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 600 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 678
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
454-681 |
4.64e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.00 E-value: 4.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgqVI 533
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT-TIMENIRF-GKL-DASDEEvytaaREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIK 610
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfARLyGLPRKE-----ARERIDELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 611 QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKK 681
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
132-397 |
1.16e-44 |
|
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: 161.83 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 132 AAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHMGsfvsesrKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMR 210
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIdSVIGGGLRELLW-------LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 211 KALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGV 290
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 291 GTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNC 370
Cdd:cd18542 156 SYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGL 235
|
250 260
....*....|....*....|....*..
gi 27753995 371 MVLGTLFIGGSLVAGQQLKGGDLMSFL 397
Cdd:cd18542 236 QIVLVLWVGGYLVINGEITLGELVAFI 262
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
454-669 |
6.93e-44 |
|
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: 155.45 E-value: 6.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYP--CRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQ 531
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 vIGFISQEPVLFATTIMENIrfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQ 611
Cdd:cd03246 78 -VGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTVRAAHSIIVMANGQV 669
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
454-669 |
1.84e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 155.74 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVi 533
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIRFGKLDASDEevytaAREANAHEFISSFpdGYSTVVGERGTT-LSGGQKQRLAIARALIKQP 612
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFPFQLRERK-----FDRERALELLERL--GLPPDILDKPVErLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 613 TVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH--RLSTvRAAHSIIVMANGQV 669
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
452-674 |
3.07e-43 |
|
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: 155.26 E-value: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSY-PCRPgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG 530
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QvIGFISQEPVLFATTIMENI-RFGKLdaSDEEVYTAAReanahefissfpdgystvVGERGTTLSGGQKQRLAIARALI 609
Cdd:cd03369 83 S-LTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 610 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGT 674
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
132-425 |
3.21e-43 |
|
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: 157.65 E-value: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 132 AAIVLALGAALVnvqipLLLGQLVeivaKYTRDHmgSFVSESRKLS----VQLLLLYGVQGLLTFGYLVLLSHIGERMAM 207
Cdd:cd18575 1 ALIALLIAAAAT-----LALGQGL----RLLIDQ--GFAAGNTALLnrafLLLLAVALVLALASALRFYLVSWLGERVVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 208 DMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPAL 287
Cdd:cd18575 70 DLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 288 MGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIA 367
Cdd:cd18575 150 VLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 368 FNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRglSAGA 425
Cdd:cd18575 230 VFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQR--AAGA 285
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
454-673 |
5.68e-43 |
|
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: 153.24 E-value: 5.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlRGQVI 533
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIrfgkldasdeevytaareanahefissfpdgystvvgerGTTLSGGQKQRLAIARALIKQPT 613
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 614 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAG 673
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
454-679 |
6.32e-43 |
|
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: 162.77 E-value: 6.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPG--FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR-- 529
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 GQVIGFISQEPV--LF-----ATTIMENIR-FGKLDASD--EEVYTAAREAN-AHEFISSFPDgystvvgergtTLSGGQ 598
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRlHGLLSRAErrERVAELLERVGlPPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTH 675
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....
gi 27753995 676 EELL 679
Cdd:COG1123 490 EEVF 493
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
454-669 |
2.73e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.89 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDLRTLNP---S 526
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSErelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 WLRGQVIGFISQEPVLFAT-TIMENI----RFGKLDAsdeevytAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQR 601
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSR-------KERRERARELLERV--GLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 602 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 669
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
454-668 |
8.28e-42 |
|
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: 151.08 E-value: 8.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLL--ErfYDPEAGSVTLDGHdlrtlnpswlr 529
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 gqvIGFISQEPVLFATTIMENIRFGKldASDEEVYTAAREANA-HEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARAL 608
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK--PFDEERYEKVIKACAlEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 609 IKQPTVLILDEATSALDAES-----ERVVQEALdraSAGRTVLVIAHRLSTVRAAHSIIVMANGQ 668
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
456-668 |
8.43e-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: 151.08 E-value: 8.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 456 FQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPsWLRGQVIGF 535
Cdd:cd03225 2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL-KELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 536 ISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQ 611
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 668
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
472-622 |
2.04e-41 |
|
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: 147.79 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLF-ATTIMEN 550
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFpRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 551 IRFGkldASDEEVYTAAREANAHEFISSF--PDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:pfam00005 80 LRLG---LLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
454-683 |
3.45e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 150.39 E-value: 3.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRGQvI 533
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQ-I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT-TIMENIR-FGKL-DASDEEVYTAAREAnAHEF-ISSFPDgystvvgERGTTLSGGQKQRLAIARALI 609
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRyFAELyGLFDEELKKRIEEL-IELLgLEEFLD-------RRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 610 KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGG 683
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
120-437 |
7.52e-41 |
|
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: 151.84 E-value: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 120 WHFLHPHLLALGAAIVLALGAALVNvqiPL---LLGQLVEIVAKYTRDHMgsfVSESRKLSVQLLLLYGVQGLLTFGYLV 196
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVF---PVfaiLFSKLISVFSLPDDDEL---RSEANFWALMFLVLAIVAGIAYFLQGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 197 LLSHIGERMAMDMRKALFSSLLRQDIAFFDAKK--TGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVsLSM-LS 273
Cdd:cd18578 75 LFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI-IAFvYG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 274 PRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEEL 353
Cdd:cd18578 154 WKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 354 GRGIALFQGLSN-IAFNCMVLGtLFIGGSLVAGQQLKGGD----LMSFLVASQTVQRSMAslsvLFGQVVRGLSAGARVF 428
Cdd:cd18578 234 ALISGLGFGLSQsLTFFAYALA-FWYGGRLVANGEYTFEQffivFMALIFGAQSAGQAFS----FAPDIAKAKAAAARIF 308
|
....*....
gi 27753995 429 EYMALSPVI 437
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
454-707 |
1.80e-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: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA---GSVTLDGHDLRTLNPsWLRG 530
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-ALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIAR 606
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGG 683
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260
....*....|....*....|....
gi 27753995 684 LYSELIRRQTLDASLTSTPPAEKP 707
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
454-681 |
1.12e-39 |
|
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: 146.19 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVA---SLLERfydPEAGSVTLDGHDLRTLNPSWLR 529
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 G--QVIGFISQEPVLFAT-TIMENIRFG-KLDASDEevytAAREANAHEFI-----SSFPDGYSTvvgergtTLSGGQKQ 600
Cdd:cd03258 79 KarRRIGMIFQHFNLLSSrTVFENVALPlEIAGVPK----AEIEERVLELLelvglEDKADAYPA-------QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEE 677
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....
gi 27753995 678 LLKK 681
Cdd:cd03258 228 VFAN 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
454-673 |
1.39e-39 |
|
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: 145.73 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL--RG 530
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEPVL-------FATTIMENIRFGKLDASDEEVYTAAREA-----NAHEFISSFPDgystvvgergtTLSGGQ 598
Cdd:cd03257 82 KEIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAG 673
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
130-427 |
3.96e-39 |
|
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: 146.39 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHMGSFVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQA---ELESCCCKAEELGrGIA--LFQGLS 364
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEineELYKASFKAQFYS-GLLmpIMNFIN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 365 NIAFncmvLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18547 240 NLGY----VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
454-669 |
5.39e-39 |
|
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: 143.40 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDLRTLNPSWL- 528
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 --RGQVIGFISQEPVLFAT-TIMENIRFGKLDASDEevyTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIA 605
Cdd:cd03255 78 afRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVP---KKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 606 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 669
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
133-427 |
1.30e-38 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. 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. 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 144.76 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVE-IVAKYTRDhmgsfvsesrKLSVQLLLLygvqGLLTFGYLV-------LLSHIGER 204
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDgIVIEKSQD----------KFSRAIIIM----GLLAIASSVaagirggLFTLAMAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 205 MAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVT 284
Cdd:cd18784 67 LNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 285 PALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESccckAEELGRGIALFQG-- 362
Cdd:cd18784 147 PLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKD----TYKLKIKEALAYGgy 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 363 --LSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18784 223 vwSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
454-691 |
2.02e-38 |
|
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: 143.26 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 533
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVL-FATTIMENI---------RFGKLDASDEE-VYTAAREANAHEFIssfpdgystvvgERG-TTLSGGQKQR 601
Cdd:COG1120 78 AYVPQEPPApFGLTVRELValgryphlgLFGRPSAEDREaVEEALERTGLEHLA------------DRPvDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 602 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|...
gi 27753995 679 LKkgglySELIRR 691
Cdd:COG1120 226 LT-----PELLEE 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
454-669 |
3.71e-38 |
|
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: 139.46 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRGQvI 533
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRR-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT-TIMENIRfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQP 612
Cdd:cd03230 76 GYLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 613 TVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 669
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
454-695 |
6.89e-38 |
|
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: 142.18 E-value: 6.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGF-NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDlrTLNPS--WLRG 530
Cdd:TIGR04520 1 IEVENVSFSYP--ESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEEnlWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEE----VYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRL 602
Cdd:TIGR04520 77 KKVGMVFQNPdnQFVGATVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 603 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
250
....*....|....*
gi 27753995 681 KGglysELIRRQTLD 695
Cdd:TIGR04520 226 QV----ELLKEIGLD 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
454-679 |
8.05e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.06 E-value: 8.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVA---SLLERfydPEAGSVTLDGHDLRTLNPSWLR 529
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 G--QVIGFISQEPVLFAT-TIMENIRF----GKLDAsdeevytAAREANAHEFISsfpdgystVVG--ERGTT----LSG 596
Cdd:COG1135 79 AarRKIGMIFQHFNLLSSrTVAENVALpleiAGVPK-------AEIRKRVAELLE--------LVGlsDKADAypsqLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 597 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAG 673
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
....*.
gi 27753995 674 THEELL 679
Cdd:COG1135 224 PVLDVF 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
455-668 |
1.15e-37 |
|
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: 137.76 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 455 TFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIG 534
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 535 FISQepvlfattimenirfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPTV 614
Cdd:cd00267 77 YVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 615 LILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTV-RAAHSIIVMANGQ 668
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
454-680 |
1.88e-37 |
|
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: 140.32 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYP-CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQV 532
Cdd:COG1124 2 LEVRNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 iGFISQEPVL-------FATTIMENIRFGKLDASDEEVYTAAREAN-AHEFISSFPDgystvvgergtTLSGGQKQRLAI 604
Cdd:COG1124 82 -QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 605 ARALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEE 677
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVAD 225
|
...
gi 27753995 678 LLK 680
Cdd:COG1124 226 LLA 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
454-666 |
4.92e-37 |
|
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: 137.99 E-value: 4.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYP-CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqv 532
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFA-TTIMENIRFGkLDASDeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVALG-LELQG--VPKAEARERAEELLELV--GLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMAN 666
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
186-683 |
7.82e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 148.97 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 186 VQGLLTFG----------YLVLLS-HIGERMamdmRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQ 254
Cdd:PLN03232 955 VYALLGFGqvavtftnsfWLISSSlHAAKRL----HDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 255 GLRSCTQVIGSLVSLSMLSprlTLMLAVVTPALM---GVGTLMGSGLRKLSRQcqEQIARATGVAD--EALGNVRTVRAF 329
Cdd:PLN03232 1031 FMNQLWQLLSTFALIGTVS---TISLWAIMPLLIlfyAAYLYYQSTSREVRRL--DSVTRSPIYAQfgEALNGLSSIRAY 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 330 AMEKReeeryqaelesccckaeelgrgIALFQGLS---NIAFNcmvLGTLFIGGSLVAGQQLKGGdLMSFLVASQTV--- 403
Cdd:PLN03232 1106 KAYDR----------------------MAKINGKSmdnNIRFT---LANTSSNRWLTIRLETLGG-VMIWLTATFAVlrn 1159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 404 -----QRSMAS-----------LSVLFGQVVR-------GLSAGARVFEYMALspviPLTGGYCIPNK------DIRGSI 454
Cdd:PLN03232 1160 gnaenQAGFAStmglllsytlnITTLLSGVLRqaskaenSLNSVERVGNYIDL----PSEATAIIENNrpvsgwPSRGSI 1235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 455 TFQNVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 533
Cdd:PLN03232 1236 KFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR-RVL 1312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIR-FGklDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQP 612
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNIDpFS--EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 613 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGG 683
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
190-689 |
4.65e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 146.66 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 190 LTFGYLV---LLSHIGeRMAMDMRKALFSSLLRQDIAF-FDAKK---TGQLVSRLTTDVQEFKSSFKLVisQGLRSCTQV 262
Cdd:PLN03232 351 VTFGVLCesqYFQNVG-RVGFRLRSTLVAAIFHKSLRLtHEARKnfaSGKVTNMITTDANALQQIAEQL--HGLWSAPFR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 263 IgsLVSLSMLSPRL---TLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERY 339
Cdd:PLN03232 428 I--IVSMVLLYQQLgvaSLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRI 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 340 QAelesccCKAEELgrgiALF---QGLSniAFNCMVLGTLFIGGSLVAGQQ--LKGGDL-----MSFLVASQTVQRSMAS 409
Cdd:PLN03232 506 QG------IRNEEL----SWFrkaQLLS--AFNSFILNSIPVVVTLVSFGVfvLLGGDLtparaFTSLSLFAVLRSPLNM 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 410 LSVLFGQVVRGLSAGARVFEYM-----ALSPVIPLTGGycIPnkdirgSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKI 484
Cdd:PLN03232 574 LPNLLSQVVNANVSLQRIEELLlseerILAQNPPLQPG--AP------AISIKNGYFSWDSKTSKPTLSDINLEIPVGSL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 485 VALVGQSGGGKTT-VASLLERFYDPEAGSVTLdghdlrtlnpswlRGQViGFISQEPVLFATTIMENIRFGKldASDEEV 563
Cdd:PLN03232 646 VAIVGGTGEGKTSlISAMLGELSHAETSSVVI-------------RGSV-AYVPQVSWIFNATVRENILFGS--DFESER 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 564 YTAAREANA--HEfISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRAS 640
Cdd:PLN03232 710 YWRAIDVTAlqHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDEL 788
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 27753995 641 AGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 689
Cdd:PLN03232 789 KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
454-667 |
9.39e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.60 E-value: 9.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqv 532
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFA-TTIMENIRFGkLDASDeeVYTAAREANAHEFIS---------SFPDgystvvgergtTLSGGQKQRL 602
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALG-LELRG--VPKAERRERARELLElvglagfedAYPH-----------QLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 603 AIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH------RLSTvRaahsIIVMANG 667
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLAD-R----VVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
454-668 |
9.48e-36 |
|
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: 133.08 E-value: 9.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL-RGQV 532
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFAT-TIMENIRFGkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQ 611
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 612 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQ 668
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
185-690 |
1.49e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 145.27 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 185 GVQGLLTFG---------YLVLLSHIgeRMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQG 255
Cdd:PLN03130 957 LIYALLSFGqvlvtllnsYWLIMSSL--YAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMF 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LRSCTQVIGSLVSLSMLSprlTLMLAVVTPALM---GVGTLMGSGLRKLSRQcqEQIARATGVAD--EALGNVRTVRAFA 330
Cdd:PLN03130 1035 LGQIFQLLSTFVLIGIVS---TISLWAIMPLLVlfyGAYLYYQSTAREVKRL--DSITRSPVYAQfgEALNGLSTIRAYK 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 331 MEKReeeryqaelesccckaeelgrgIALFQGLS---NIAFncmvlgTLF-IGGSLVAGQQLKG-GDLMSFLVASQTV-- 403
Cdd:PLN03130 1110 AYDR----------------------MAEINGRSmdnNIRF------TLVnMSSNRWLAIRLETlGGLMIWLTASFAVmq 1161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 404 ------QRSMAS-----------LSVLFGQVVR-------GLSAGARVFEYMALSPVIPLT--GGYCIPNKDIRGSITFQ 457
Cdd:PLN03130 1162 ngraenQAAFAStmglllsyalnITSLLTAVLRlaslaenSLNAVERVGTYIDLPSEAPLVieNNRPPPGWPSSGSIKFE 1241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 458 NVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFI 536
Cdd:PLN03130 1242 DVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR-KVLGII 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQEPVLFATTImeniRFgKLDA----SDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQP 612
Cdd:PLN03130 1319 PQAPVLFSGTV----RF-NLDPfnehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 613 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL-KKGGLYSELIR 690
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSAFSKMVQ 1472
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
457-680 |
1.83e-35 |
|
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: 136.72 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA---GSVTLDGHDLRTLNPS---WLR 529
Cdd:COG0444 5 RNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKelrKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 GQVIGFISQEPvlFA---------TTIMENIRFGKlDASDEEVYTAAREA-------NAHEFISSFPdgystvvGErgtt 593
Cdd:COG0444 85 GREIQMIFQDP--MTslnpvmtvgDQIAEPLRIHG-GLSKAEARERAIELlervglpDPERRLDRYP-------HE---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 594 LSGGQKQRLAIARALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRA-AHSIIVMAN 666
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMYA 226
|
250
....*....|....
gi 27753995 667 GQVCEAGTHEELLK 680
Cdd:COG0444 227 GRIVEEGPVEELFE 240
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
458-669 |
1.05e-34 |
|
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: 130.84 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 458 NVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPSWLRGQVIGFIS 537
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 538 QEP--VLFATTIMENIRFGK--LDASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIARALIKQPT 613
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLkeLDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 614 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 669
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
454-690 |
2.54e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.45 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYP--CRPGfnvLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLNPS--W-L 528
Cdd:PRK13635 6 IRVEHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEEtvWdV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RGQViGFISQEP--VLFATTIMENIRFG------KLDASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQ 600
Cdd:PRK13635 80 RRQV-GMVFQNPdnQFVGATVQDDVAFGlenigvPREEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESErvvQEALD-----RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTH 675
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
250
....*....|....*
gi 27753995 676 EELLKKGglySELIR 690
Cdd:PRK13635 225 EEIFKSG---HMLQE 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
454-678 |
2.81e-34 |
|
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: 131.15 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQV- 532
Cdd:cd03256 1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 -IGFISQEPVLFA-TTIMENIRFGKLdasdeevytaareaNAHEFISSFPDGYS-----------TVVG------ERGTT 593
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRL--------------GRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 594 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVC 670
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
....*...
gi 27753995 671 EAGTHEEL 678
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
454-673 |
3.78e-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: 129.56 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGqvI 533
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERRN--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT-TIMENIRFG------KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 606
Cdd:cd03259 75 GMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAG 673
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
132-427 |
4.26e-34 |
|
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: 132.14 E-value: 4.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 132 AAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHMgsfvsesRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMR 210
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIdEGIANGDLSYI-------LRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 211 KALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGV 290
Cdd:cd18548 76 KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 291 GTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNC 370
Cdd:cd18548 156 VFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 371 MVLGTLFIGGSLVAGQQLKGGDLMSFL-VASQTVQrSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18548 236 AIVAILWFGGHLINAGSLQVGDLVAFInYLMQILM-SLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
454-679 |
4.63e-34 |
|
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: 130.50 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 533
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-RKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFA-TTIMENIrfgKLDASDEEVYTAAREANAHEFIS-------SFPDGYSTvvgergtTLSGGQKQRLAIA 605
Cdd:cd03295 78 GYVIQQIGLFPhMTVEENI---ALVPKLLKWPKEKIRERADELLAlvgldpaEFADRYPH-------ELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 606 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRL-STVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
454-673 |
6.48e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.40 E-value: 6.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRg 530
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQE-PVLFATTIMENIRF-----GKldaSDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQ 600
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAE-SERVVqEALDRASA-GRTVLVIAHRLSTVRAA-HSIIVMANGQVCEAG 673
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRrGTTVLIATHDLELVDRMpKRVLELEDGRLVRDE 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
454-680 |
1.01e-33 |
|
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: 129.16 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--Q 531
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEPVLF-ATTIMENIRFG---KLDASDEEVYTAARE----ANAHEFISSFPdgystvvGErgttLSGGQKQRLA 603
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLRGAEDLYP-------AE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 604 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLK 680
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
453-678 |
1.32e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.14 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGqv 532
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFA-TTIMENIRFG----KLDAsdeevytAAREANAHE---------FISSFPDgystvvgergtTLSGGQ 598
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFGlrmrGVPK-------AEIRARVAEllelvglegLADRYPH-----------QLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS---TVraAHSIIVMANGQVCEAG 673
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
....*
gi 27753995 674 THEEL 678
Cdd:COG3842 219 TPEEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
457-673 |
1.63e-33 |
|
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: 126.78 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFI 536
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-RKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQepvlfattIMEniRFGKLDASDEEVytaareanahefissfpdgystvvgergTTLSGGQKQRLAIARALIKQPTVLI 616
Cdd:cd03214 79 PQ--------ALE--LLGLAHLADRPF----------------------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 617 LDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAG 673
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
454-679 |
1.69e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.05 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTT-VASLLeRFYDPEAGSVTLDGHDLRtlnpswLRGQV 532
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPR------RARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVL---FATTIMENIR---------FGKLDASDEEvytAAREA----NAHEFISsfpdgysTVVGErgttLSG 596
Cdd:COG1121 77 IGYVPQRAEVdwdFPITVRDVVLmgrygrrglFRRPSRADRE---AVDEAlervGLEDLAD-------RPIGE----LSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 597 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEaGT 674
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GP 221
|
....*
gi 27753995 675 HEELL 679
Cdd:COG1121 222 PEEVL 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
454-669 |
2.29e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.64 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--Q 531
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEPVLFA-TTIMENIRFGKLDA-----------SDEEVytaareANAHEFISSfpdgystvVG------ERGTT 593
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRLGRtstwrsllglfPPEDR------ERALEALER--------VGladkayQRADQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 594 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
452-690 |
3.07e-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: 128.49 E-value: 3.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYP--CRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR 529
Cdd:cd03288 18 GEIKIHDLCVRYEnnLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 GQvIGFISQEPVLFATTIMENIRfGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALI 609
Cdd:cd03288 95 SR-LSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 610 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL-KKGGLYSEL 688
Cdd:cd03288 173 RKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
..
gi 27753995 689 IR 690
Cdd:cd03288 253 VR 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
445-680 |
3.42e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.96 E-value: 3.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 445 IPNKDIrgSITFQNVTFSYPcrPGF-NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTL 523
Cdd:PRK13632 1 IKNKSV--MIKVENVSFSYP--NSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 524 NPSWLRGQvIGFISQEP--VLFATTIMENIRFG----KLDASD--EEVYTAAREANAHEFISSFPDgystvvgergtTLS 595
Cdd:PRK13632 77 NLKEIRKK-IGIIFQNPdnQFIGATVEDDIAFGlenkKVPPKKmkDIIDDLAKKVGMEDYLDKEPQ-----------NLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 596 GGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAG 673
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
....*..
gi 27753995 674 THEELLK 680
Cdd:PRK13632 225 KPKEILN 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
454-679 |
5.06e-33 |
|
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: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTV---ASLLERfydPEAGSVTLDGHDL----RTLNPs 526
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdskKDINK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 wLRGQvIGFISQEPVLFA-TTIMENIRFG-----KLdaSDEEVYTAAREANAH----EFISSFPDgystvvgergtTLSG 596
Cdd:COG1126 75 -LRRK-VGMVFQQFNLFPhLTVLENVTLApikvkKM--SKAEAEERAMELLERvglaDKADAYPA-----------QLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 597 GQKQRLAIARALIKQPTVLILDEATSALDAEserVVQEALD--R--ASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCE 671
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAReVADRVVFMDGGRIVE 216
|
....*...
gi 27753995 672 AGTHEELL 679
Cdd:COG1126 217 EGPPEEFF 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
454-680 |
5.49e-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: 127.40 E-value: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRG 530
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QvIGFISQEPVLF-ATTIMENIRFG---KLDASDEEVYTAAREA----NAHEFISSFPdgystvvGErgttLSGGQKQRL 602
Cdd:COG1127 83 R-IGMLFQGGALFdSLTVFENVAFPlreHTDLSEAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 603 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELL 679
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
.
gi 27753995 680 K 680
Cdd:COG1127 231 A 231
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
130-427 |
2.41e-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: 126.83 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHMGSFVsesrklsVQLLLLYGVQGLLTFGYLVLLSHIGERMAMD 208
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSALWPLV-------LLLLALGVAEAVLSFLRRYLAGRLSLGVEHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 209 MRKALFSSLLRQDIAFFDAKKTGQLVSRLTTD---VQEFKSSFKLVISQGLrsctQVIGSLVSLSMLSPRLTLMLAVVTP 285
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDlslVQRFLAFGPFLLGNLL----TLVVGLVVMLVLSPPLALVALASLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 286 ALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEER--------YQAELEscccKAEELGRGI 357
Cdd:cd18543 150 PLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRfeaaarrlRATRLR----AARLRARFW 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 358 ALFQGLSNIAfncmVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18543 226 PLLEALPELG----LAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
471-681 |
2.44e-32 |
|
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: 125.14 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGqvIGFISQEPVLFA-TTIME 549
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRD--ISYVPQNYALFPhMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 550 NIRFG--KLDASDEEVYTAAREanahefISSFPdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 627
Cdd:cd03299 91 NIAYGlkKRKVDKKEIERKVLE------IAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 628 SERVVQEALDRA--SAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 681
Cdd:cd03299 164 TKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
130-410 |
5.83e-32 |
|
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: 125.99 E-value: 5.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDhmgsfVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLT-----ASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFN 369
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 370 CMVLGTLFIGGSLVAGQQLKGGDLMSFL---------------VASqTVQRSMASL 410
Cdd:cd18541 236 LSFLIVLWYGGRLVIRGTITLGDLVAFNsylgmliwpmmalgwVIN-LIQRGAASL 290
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
468-680 |
1.20e-31 |
|
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: 123.32 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIG--FisQEPVLFAT 545
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrtF--QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 -TIMENIR--------FGKLDASDEEVYTAAREAnAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 616
Cdd:cd03219 90 lTVLENVMvaaqartgSGLLLARARREEREARER-AEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 617 LDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLK 680
Cdd:cd03219 167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
197-427 |
2.63e-31 |
|
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: 123.99 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 197 LLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRL 276
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 277 TLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRG 356
Cdd:cd18590 139 TLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 357 IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18590 219 RAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
454-678 |
3.37e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.84 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDL--RTLNPS 526
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 WLRGQViGFISQEPVLFATTIMENIRFG-----KLDAS--DEEVYTAAREANA-HEfissfpdgystvVGER----GTTL 594
Cdd:COG1117 89 ELRRRV-GMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSelDEIVEESLRKAALwDE------------VKDRlkksALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 595 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAG 673
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFG 235
|
....*
gi 27753995 674 THEEL 678
Cdd:COG1117 236 PTEQI 240
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
453-680 |
8.66e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.10 E-value: 8.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASL---LERfydPEAGSVTLDGHDLRTLNPSWLR 529
Cdd:COG1118 2 SIEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 GqvIGFISQEPVLFA-TTIMENIRFG--KLDASDEEvytaaREANAHEFISSFP-DGYstvvGER-GTTLSGGQKQRLAI 604
Cdd:COG1118 76 R--VGFVFQHYALFPhMTVAENIAFGlrVRPPSKAE-----IRARVEELLELVQlEGL----ADRyPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 605 ARALIKQPTVLILDEATSALDA----ESERVVQEALDRasAGRTVLVIAH-RLSTVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
.
gi 27753995 680 K 680
Cdd:COG1118 223 D 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
456-673 |
9.29e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.95 E-value: 9.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 456 FQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlrtlNPSWLRGQVIGF 535
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 536 ISQEPVL---FATTIMENIR---------FGKLDASDEEvytAAREAnaHEF--ISSFPDgystvvgERGTTLSGGQKQR 601
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglFRRLSKADKA---KVDEA--LERvgLSELAD-------RQIGELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 602 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAG 673
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
454-679 |
1.13e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGqvI 533
Cdd:COG3840 2 LRLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP--V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFA-TTIMENIRFG-----KLDASD-EEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 606
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 607 ALIKQPTVLILDEATSALD----AESERVVQEAldRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 679
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGLTVLMVTHDPEDAaRIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
454-669 |
1.22e-30 |
|
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: 119.56 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL--RTLNPSWLRGQ 531
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 ViGFISQEPVLFA-TTIMENIRFGK---LDASDEEVYTAAREANAH----EFISSFPDgystvvgergtTLSGGQKQRLA 603
Cdd:cd03262 78 V-GMVFQQFNLFPhLTVLENITLAPikvKGMSKAEAEERALELLEKvglaDKADAYPA-----------QLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 604 IARALIKQPTVLILDEATSALDAEserVVQEALD----RASAGRTVLVIAHRLSTVR-AAHSIIVMANGQV 669
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPE---LVGEVLDvmkdLAEEGMTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
130-409 |
3.85e-30 |
|
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: 120.57 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHMGSFvsesrKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMD 208
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLL-----LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 209 MRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALM 288
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 289 GVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEER--------YQAELESccCKAEELGRgiALF 360
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEfdeinqeyRKANLKS--IKLFALFR--PLV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 361 QGLSNIAfncmVLGTLFIGGSLVAGQQLKGGDLMSFL------------VASQ--TVQRSMAS 409
Cdd:cd18544 232 ELLSSLA----LALVLWYGGGQVLSGAVTLGVLYAFIqyiqrffrpirdLAEKfnILQSAMAS 290
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-427 |
5.08e-30 |
|
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: 120.33 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHmgsfvSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL-----GLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAelescccKAEELGRGI--ALFqgLSNIA 367
Cdd:cd18778 156 GAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA-------LSRRYRKAQlrAMK--LWAIF 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 368 FNCMV----LGT---LFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18778 227 HPLMEfltsLGTvlvLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
468-679 |
1.18e-29 |
|
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: 117.15 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL--RGqvIGFISQEPVLFAT 545
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERarAG--IGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 -TIMENIRFG-------KLDASDEEVYTAareanahefissFPdgystVVGER----GTTLSGGQKQRLAIARALIKQPT 613
Cdd:cd03224 90 lTVEENLLLGayarrraKRKARLERVYEL------------FP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 614 VLILDEATSALdaeSERVVQEALDR----ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELL 679
Cdd:cd03224 153 LLLLDEPSEGL---APKIVEEIFEAirelRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
457-679 |
1.99e-29 |
|
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: 123.26 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPG--------FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFyDPEAGSVTLDGHDLRTLNPSWL 528
Cdd:COG4172 279 RDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RG-----QVIgFisQEPvlFAT---------TIMENIRFGKLDASDEEVYTAAREANA-------------HEFissfpd 581
Cdd:COG4172 358 RPlrrrmQVV-F--QDP--FGSlsprmtvgqIIAEGLRVHGPGLSAAERRARVAEALEevgldpaarhrypHEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 582 gystvvgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV 655
Cdd:COG4172 427 -------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*
gi 27753995 656 RA-AHSIIVMANGQVCEAGTHEELL 679
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-427 |
3.33e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 118.38 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHMGSFVSESRKLS-VQLLL--------LYGVQGLLTFGYLVLLSH 200
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGPDpLALLLlaaaalvgIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 201 IGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLML 280
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 281 AVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALF 360
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 361 QGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-427 |
4.02e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 117.61 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHmgsfvSESRKLSVQLLLLYGVQGLLTF-----GYLvlLSHIGER 204
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPG-----GNTSLLLLLVLGLAGAYVLSALlgilrGRL--LARLGER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 205 MAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVT 284
Cdd:cd18563 74 ITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 285 PALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLS 364
Cdd:cd18563 154 PLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 365 NIafnCMVLGTLFI---GGSLVAGQQLKGGDLMSFLV-ASQTVQRsMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18563 234 TF---LTSLGTLIVwyfGGRQVLSGTMTLGTLVAFLSyLGMFYGP-LQWLSRLNNWITRALTSAERI 296
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
118-689 |
5.69e-29 |
|
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: 124.25 E-value: 5.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 118 LFWHFLHphllalgAAIVLALGAALVNVQiPLLLGQlveIVAKYTRDHmgsfvSESRK----LSVQLLLLYGVQGLLTFG 193
Cdd:TIGR01271 78 FFWRFVF-------YGILLYFGEATKAVQ-PLLLGR---IIASYDPFN-----APEREiayyLALGLCLLFIVRTLLLHP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 194 YLVLLSHIGermaMDMRKALFSSLLRQDIAF----FDAKKTGQLVSRLTTDVQEFKSS-----FKLVISQGLRSCTQVIG 264
Cdd:TIGR01271 142 AIFGLHHLG----MQMRIALFSLIYKKTLKLssrvLDKISTGQLVSLLSNNLNKFDEGlalahFVWIAPLQVILLMGLIW 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 265 SLVSLSMLSPRLTLMLAVVTPAlmGVGTLMGSGLRKLSRQCQEQIAratgVADEALGNVRTVRAF----AMEKREEERYQ 340
Cdd:TIGR01271 218 ELLEVNGFCGLGFLILLALFQA--CLGQKMMPYRDKRAGKISERLA----ITSEIIENIQSVKAYcweeAMEKIIKNIRQ 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 341 AELEsccckaeeLGRGIALFQGLSNIAFncMVLGTLFIGGSLVAGQQLKGGDLMS-FLVASQTVQRSMASLSVLFGQVVR 419
Cdd:TIGR01271 292 DELK--------LTRKIAYLRYFYSSAF--FFSGFFVVFLSVVPYALIKGIILRRiFTTISYCIVLRMTVTRQFPGAIQT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 420 GL-SAGA-------------RVFEYMALSPVIPLTGGYC---------------------IPNKDirGSITFQNvtFSYP 464
Cdd:TIGR01271 362 WYdSLGAitkiqdflckeeyKTLEYNLTTTEVEMVNVTAswdegigelfekikqnnkarkQPNGD--DGLFFSN--FSLY 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 465 CRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHdlrtlnpswlrgqvIGFISQEPVLFA 544
Cdd:TIGR01271 438 VTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMP 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENIRFGKldASDEEVYTAAREA-NAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 623
Cdd:TIGR01271 501 GTIKDNIIFGL--SYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 624 LDAESER-VVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 689
Cdd:TIGR01271 579 LDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
453-678 |
7.01e-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: 115.51 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPswlRGQV 532
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFA-TTIMENIRFG-KLDASDEEVYTAAREANAHEFI-----SSFPDGYSTvvgergtTLSGGQKQRLAIA 605
Cdd:cd03296 76 VGFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 606 RALIKQPTVLILDEATSALDA----ESERVVQEALDRASAgRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHV-TTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
194-397 |
8.39e-29 |
|
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: 116.80 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 194 YLVLLSHIGERMamdmRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLS 273
Cdd:cd18589 60 YNITMSRIHSRL----QGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 274 PRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESC--CCKAE 351
Cdd:cd18589 136 PKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTyrLNKKE 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27753995 352 ELGRGIALF-QGLSNIAfncMVLGTLFIGGSLVAGQQLKGGDLMSFL 397
Cdd:cd18589 216 AAAYAVSMWtSSFSGLA---LKVGILYYGGQLVTAGTVSSGDLVTFV 259
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
454-669 |
1.19e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP--SWLRGq 531
Cdd:COG1129 5 LEMRGISKSFG---GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 vIGFISQEPVLFAT-TIMENI-------RFGKLDasDEEVYTAAREA----NAHefISsfPDgysTVVGErgttLSGGQK 599
Cdd:COG1129 81 -IAIIHQELNLVPNlSVAENIflgreprRGGLID--WRAMRRRARELlarlGLD--ID--PD---TPVGD----LSVAQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 600 QRLAIARALIKQPTVLILDEATSAL-DAESER---VVQEaLdrASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLtEREVERlfrIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
454-678 |
1.29e-28 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 114.14 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVI 533
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAAR-QSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT-TIMENIRF-GKLDAsdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:cd03263 78 GYCPQFDALFDElTVREHLRFyARLKG----LPKSEIKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
454-669 |
1.91e-28 |
|
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: 111.75 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVI 533
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQepvlfattimenirfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPT 613
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 614 VLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
472-679 |
2.08e-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: 115.05 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL---RGQVIGFISQEPVLFA-TTI 547
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKKISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 548 MENIRFGkLD---ASDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:cd03294 120 LENVAFG-LEvqgVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 621 TSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:cd03294 188 FSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
116-397 |
4.76e-28 |
|
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: 114.47 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 116 WKLFwhflhphLLALGAAIVlalgAALVNVQIPLLLGQLVEIVAkyTRDHMGSFVsesrKLSVQLLLLYGVQGLLTFgYL 195
Cdd:cd18549 1 KKLF-------FLDLFCAVL----IAALDLVFPLIVRYIIDDLL--PSKNLRLIL----IIGAILLALYILRTLLNY-FV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 196 VLLSHI-GERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTD---VQEFksSFK----LVIsqglrSCTQVIGSLV 267
Cdd:cd18549 63 TYWGHVmGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDlfdISEL--AHHgpedLFI-----SIITIIGSFI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 268 SLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAE----L 343
Cdd:cd18549 136 ILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGndrfL 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 344 ESCcckaEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL 397
Cdd:cd18549 216 ESK----KKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFL 265
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
453-690 |
5.36e-28 |
|
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: 121.21 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYpCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHdlrtlnpswlrgqv 532
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFATTIMENIRFGKldASDEEVYTAAREANAH-EFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:TIGR00957 701 VAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 612 PTVLILDEATSALDAESERVVQEAL---DRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSEL 688
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
..
gi 27753995 689 IR 690
Cdd:TIGR00957 859 LR 860
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
454-678 |
6.81e-28 |
|
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: 112.33 E-value: 6.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGqvI 533
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-PPHKRP--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFA-TTIMENIRFG----KLDASD--EEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 606
Cdd:cd03300 75 NTVFQNYALFPhLTVFENIAFGlrlkKLPKAEikERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
454-674 |
7.20e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 115.28 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPC-RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDLRTLNPSWLR 529
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 G--QVIGFISQEPVLFAT-TIMENIRFG-KLDASDEevytAAREANAHEF-----ISSFPDGYSTvvgergtTLSGGQKQ 600
Cdd:PRK11153 79 KarRQIGMIFQHFNLLSSrTVFDNVALPlELAGTPK----AEIKARVTELlelvgLSDKADRYPA-------QLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGT 674
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
129-427 |
1.18e-27 |
|
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: 113.33 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 129 ALGAAIVLALGAALVNVQIPLLLGQLVE--IVAKytrdHMGSFVsesrKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMA 206
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDeyIPNG----DLSGLL----IIALLFLALNLVNWVASRLRIYLMAKVGQRIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 207 MDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVqefkSSFKLVISQGLrscTQVIGSLVSLSM-------LSPRLTLM 279
Cdd:cd18545 73 YDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDV----NSLSDLLSNGL---INLIPDLLTLVGiviimfsLNVRLALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 280 LAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQaELESCCCKAEElgRGIAL 359
Cdd:cd18545 146 TLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFD-ELNRENRKANM--RAVRL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 360 FQGLSNIAFNCMVLGT---LFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18545 223 NALFWPLVELISALGTalvYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
171-678 |
1.26e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 119.88 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 171 SESRKLSVQLLLLygVQGLLTFGYLVLLSHIGERM-AMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFK 249
Cdd:PTZ00243 996 SAATYLYVYLGIV--LLGTFSVPLRFFLSYEAMRRgSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLP 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 250 LVISQGLRSCTQVIGSLVSLSMLSPrltLMLAVVTPALMGVGTLMG---SGLRKLSRQCQEQIARATGVADEALGNVRTV 326
Cdd:PTZ00243 1074 MSYLYLLQCLFSICSSILVTSASQP---FVLVALVPCGYLYYRLMQfynSANREIRRIKSVAKSPVFTLLEEALQGSATI 1150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 327 RAFAMEK---REEERYQAELESCCCKAEELGRGIAL-FQGLSNIAFNCMVLgTLFIGGSLVAGQQLKGGDLMSFLVASQT 402
Cdd:PTZ00243 1151 TAYGKAHlvmQEALRRLDVVYSCSYLENVANRWLGVrVEFLSNIVVTVIAL-IGVIGTMLRATSQEIGLVSLSLTMAMQT 1229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 403 --------------------VQR-----------SMASLSVLFGQVVRGLSAGARVFEYMALSPVIPLTGGyciPNKDIR 451
Cdd:PTZ00243 1230 tatlnwlvrqvatveadmnsVERllyytdevpheDMPELDEEVDALERRTGMAADVTGTVVIEPASPTSAA---PHPVQA 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG 530
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QvIGFISQEPVLFATTIMENIR-FgkLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALI 609
Cdd:PTZ00243 1385 Q-FSMIPQDPVLFDGTVRQNVDpF--LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 610 KQPTVLIL-DEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PTZ00243 1462 KKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
204-689 |
1.31e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 119.84 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 204 RMAMDMRKALFSSLLRQDIAFFDAKK----TGQLVSRLTTDVQEFKSsfklvISQGLRSC----TQVIGSLV----SLSM 271
Cdd:PLN03130 367 RVGFRLRSTLVAAVFRKSLRLTHEGRkkftSGKITNLMTTDAEALQQ-----ICQQLHTLwsapFRIIIAMVllyqQLGV 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 272 LSPRLTLMLAVVTPAlmgvGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKReeerYQAELESCccKAE 351
Cdd:PLN03130 442 ASLIGSLMLVLMFPI----QTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENS----FQSKVQTV--RDD 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 352 ELG--RGIALfqgLSniAFNCMVLGTLFIGGSLVA--GQQLKGGDLmsflvasqTVQRSMASLSV-------------LF 414
Cdd:PLN03130 512 ELSwfRKAQL---LS--AFNSFILNSIPVLVTVVSfgVFTLLGGDL--------TPARAFTSLSLfavlrfplfmlpnLI 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 415 GQVVRGLSAGARVFEYM-----ALSPVIPLTGGycIPnkdirgSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVG 489
Cdd:PLN03130 579 TQAVNANVSLKRLEELLlaeerVLLPNPPLEPG--LP------AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVG 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 490 QSGGGKTTVAS-LLERFYDPEAGSVTLdghdlrtlnpswlRGQViGFISQEPVLFATTIMENIRFGKldASDEEVYTAAR 568
Cdd:PLN03130 651 STGEGKTSLISaMLGELPPRSDASVVI-------------RGTV-AYVPQVSWIFNATVRDNILFGS--PFDPERYERAI 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 569 EANA-HEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVL 646
Cdd:PLN03130 715 DVTAlQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRqVFDKCIKDELRGKTRV 794
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 27753995 647 VIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 689
Cdd:PLN03130 795 LVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
468-677 |
2.17e-27 |
|
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: 111.67 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL--RGQVIGFisQEPVLFAT 545
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarLGIARTF--QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 -TIMENI-----------------RFGKLDASDEEVYTAAREAnAHEFissfpdGYSTVVGERGTTLSGGQKQRLAIARA 607
Cdd:COG0411 94 lTVLENVlvaaharlgrgllaallRLPRARREEREARERAEEL-LERV------GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 608 LIKQPTVLILDEATSAL-DAESERVVQ--EALdRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEE 677
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
457-679 |
2.45e-27 |
|
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: 110.84 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFI 536
Cdd:COG0410 7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQEPVLFAT-TIMENIRFG--------KLDASDEEVYTAareanahefissFPdgystVVGER----GTTLSGGQKQRLA 603
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGayarrdraEVRADLERVYEL------------FP-----RLKERrrqrAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 604 IARALIKQPTVLILDEATSALdaeSERVVQE---ALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIRRlNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAEL 223
|
.
gi 27753995 679 L 679
Cdd:COG0410 224 L 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
454-683 |
2.72e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.13 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrTLNPSWLRGQVI 533
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEP--VLFATTIMENIRFGKLDASDEEVYTAAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 612 PTVLILDEATSALDAESE----RVVQEAldRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGG 683
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
453-669 |
3.10e-27 |
|
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: 109.18 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRPG---FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLL--ERFYDPEAGSVTLDGHDLRtlnPSW 527
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 528 LRGQvIGFISQEPVLFAT-TIMENIRFgkldasdeevytAAREanahefissfpdgystvvgeRGttLSGGQKQRLAIAR 606
Cdd:cd03213 80 FRKI-IGYVPQDDILHPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLST--VRAAHSIIVMANGQV 669
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
457-678 |
3.58e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.90 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPGF-----NVLK---DFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 528
Cdd:COG4608 11 RDLKKHFPVRGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGREL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RG-----QVIgFisQEPvlFA---------TTIMENIRFGKLdASDEEVYTAAREA-------------NAHEFissfpd 581
Cdd:COG4608 91 RPlrrrmQMV-F--QDP--YAslnprmtvgDIIAEPLRIHGL-ASKAERRERVAELlelvglrpehadrYPHEF------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 582 gystvvgergttlSGGQKQRLAIARALIKQPTVLILDEATSALD----AEserVV------QEALdrasaGRTVLVIAHR 651
Cdd:COG4608 159 -------------SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHD 217
|
250 260
....*....|....*....|....*...
gi 27753995 652 LSTVR-AAHSIIVMANGQVCEAGTHEEL 678
Cdd:COG4608 218 LSVVRhISDRVAVMYLGKIVEIAPRDEL 245
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
471-678 |
5.02e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 109.92 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT-TIME 549
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 550 NIRFGkLDAsdeevyTAAREANAHEFISS-FPdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD--- 625
Cdd:TIGR03410 95 NLLTG-LAA------LPRRSRKIPDEIYElFP-VLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQpsi 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 626 -AESERVVQEAldRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:TIGR03410 167 iKDIGRVIRRL--RAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
454-682 |
5.93e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 5.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 533
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR-KHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEP--VLFATTIMENIRFG------KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIA 605
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGlenhavPYDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 606 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKG 682
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-411 |
6.23e-27 |
|
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: 111.42 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEiVAKYTRDhMGSFVsesrKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDM 209
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIID-DALPQGD-LGLLV----LLALGMVAVAVASALLGVVQTYLSARIGQGVMYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 210 RKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMG 289
Cdd:cd18550 75 RVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 290 VGTLMGSGLRKLSRQCQEQIARATGVADEAL--GNVRTVRAFAMEKREEERYQAElesccckAEELGR--------GIAL 359
Cdd:cd18550 155 PTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARR-------SRELRDlgvrqalaGRWF 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 360 FQGLSnIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSF--------------LVASQTVQRSMASLS 411
Cdd:cd18550 228 FAALG-LFTAIGPALVYWVGGLLVIGGGLTIGTLVAFtallgrlygpltqlLNIQVDLMTSLALFE 292
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
454-669 |
7.09e-27 |
|
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: 108.82 E-value: 7.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGkIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVI 533
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLR-RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT-TIMENIRF----GKLDASDEEvytaAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARAL 608
Cdd:cd03264 75 GYLPQEFGVYPNfTVREFLDYiawlKGIPSKEVK----ARVDEVLELV-----NLGDRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 609 IKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
454-673 |
2.01e-26 |
|
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: 107.58 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrGQVI 533
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFA-TTIMENIRFG-----KLDASDEE-VYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 606
Cdd:cd03298 73 SMLFQENNLFAhLTVEQNVGLGlspglKLTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 607 ALIKQPTVLILDEATSALD-AESERVVQEALD-RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAG 673
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpALRAEMLDLVLDlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
454-681 |
2.96e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.05 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVi 533
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEP--VLFATTIMENIRFGKL------DASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIA 605
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVnmgldkDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 606 RALIKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKK 681
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
454-661 |
3.15e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.79 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLErfydPEAGSVTLDGHDLRTLNPSWLR 529
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 gqVIGFISQEPVLFAT-TIMENIRF----GKLDASDEEVYTAAREAN----AHEFISsfpdgystvvgergtTLSGGQKQ 600
Cdd:COG4133 76 --RLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGlaglADLPVR---------------QLSAGQKR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSI 661
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
198-689 |
4.00e-26 |
|
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: 115.39 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 198 LSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRL- 276
Cdd:TIGR01271 949 LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIf 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 277 --TLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVAdeaLGNVRTVRAFAMEKREEERYQAELESCCCKAEELG 354
Cdd:TIGR01271 1029 iaAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITS---LKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYL 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 355 RGIALFQGLSNIAFNCMVLGTLFIGgslVAGQQLKGGDL-----MSFLVASqTVQRSMASlSVLFGQVVRGLSagaRVFE 429
Cdd:TIGR01271 1106 STLRWFQMRIDIIFVFFFIAVTFIA---IGTNQDGEGEVgiiltLAMNILS-TLQWAVNS-SIDVDGLMRSVS---RVFK 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 430 YMALSPVIPLTGG----------YCIPNKDIR------GSITFQNVTFSYpCRPGFNVLKDFTLKLPSGKIVALVGQSGG 493
Cdd:TIGR01271 1178 FIDLPQEEPRPSGgggkyqlstvLVIENPHAQkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGS 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 494 GKTTVASLLERFYDPEaGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENirfgkLDA----SDEEVYTAARE 569
Cdd:TIGR01271 1257 GKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWR-KAFGVIPQKVFIFSGTFRKN-----LDPyeqwSDEEIWKVAEE 1329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 570 ANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIA 649
Cdd:TIGR01271 1330 VGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE 1409
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 27753995 650 HRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 689
Cdd:TIGR01271 1410 HRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
454-669 |
3.92e-25 |
|
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: 104.03 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRg 530
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEPVLFAT-TIMENIRFgkldaSDEEVYTAAREANahEFISSFPD--GYSTVVGERGTTLSGGQKQRLAIARA 607
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVAF-----ALEVTGVPPREIR--KRVPAALElvGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 608 LIKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTV-RAAHSIIVMANGQV 669
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
454-682 |
8.71e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 8.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL------RTLNP 525
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 526 swLRGQV-IGFISQEPVLFATTIMENIRFGKLD--ASDEEVYTAAREANA-----HEFISSFPdgystvvgergTTLSGG 597
Cdd:PRK13634 83 --LRKKVgIVFQFPEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIElvglpEELLARSP-----------FELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 598 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGT 674
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGT 229
|
....*...
gi 27753995 675 HEELLKKG 682
Cdd:PRK13634 230 PREIFADP 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
452-678 |
1.84e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.54 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTvasLLeR----FYDPEAGSVTLDGHDLRTLNPSw 527
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 528 LRGqvIGFISQEPVLF-ATTIMENIRFG----KLDAS--DEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQ 600
Cdd:COG3839 74 DRN--IAMVFQSYALYpHMTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESeRV--------VQEALdrasaGRTVLVIAHRLstVRA---AHSIIVMANGQV 669
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQ--VEAmtlADRIAVMNDGRI 212
|
....*....
gi 27753995 670 CEAGTHEEL 678
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
453-707 |
1.92e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLrGQV 532
Cdd:PRK11231 2 TLRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL-ARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVlfattIMENIR---------------FGKLDASDEEVYTAAREANAhefISSFPDgystvvgERGTTLSGG 597
Cdd:PRK11231 78 LALLPQHHL-----TPEGITvrelvaygrspwlslWGRLSAEDNARVNQAMEQTR---INHLAD-------RRLTDLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 598 QKQRLAIARALIKQPTVLILDEATSALD----AESERVVQEaldRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEA 672
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMRE---LNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQ 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 27753995 673 GTHEELLKKgglysELIRRQ-TLDASLTSTPPAEKP 707
Cdd:PRK11231 220 GTPEEVMTP-----GLLRTVfDVEAEIHPEPVSGTP 250
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
454-679 |
2.00e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLR--TLNPSWLRgQ 531
Cdd:PRK09493 2 IEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEPVLFA-TTIMENIRFGKLD---ASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIARA 607
Cdd:PRK09493 78 EAGMVFQQFYLFPhLTALENVMFGPLRvrgASKEEAEKQARELLAKVGLAERAHHYPS-------ELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 608 LIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRAAHS-IIVMANGQVCEAGTHEELL 679
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLI 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
454-679 |
2.53e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDlrTLNPSWLRG--Q 531
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGirK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEP--VLFATTIMENIRFGKLDAS------DEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLA 603
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGPENLClppieiRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 604 IARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
467-667 |
2.55e-24 |
|
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: 101.64 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 467 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSV----TLDGHDLRTLNPSWLRGQViGFISQEPVL 542
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSV-AYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 543 FATTIMENIRFGKldASDEEVYTAAREA-NAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 621
Cdd:cd03290 91 LNATVEENITFGS--PFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27753995 622 SALDAE-SERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANG 667
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
453-680 |
2.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL--RTLNPSWL 528
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RGQViGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISsfpdgYSTVVGERGTTLSGGQKQRLAI 604
Cdd:PRK13637 82 RKKV-GLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMNIVGLD-----YEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 605 ARALIKQPTVLILDEATSALDAESErvvQEALDRASA-----GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKElhkeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREV 232
|
..
gi 27753995 679 LK 680
Cdd:PRK13637 233 FK 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
472-684 |
2.69e-24 |
|
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: 105.19 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLK----LPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLNPSWLRGQV------IGFISQEPV 541
Cdd:TIGR02142 9 LGDFSLDadftLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG---RTLFDSRKGIFLppekrrIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 542 LFA-TTIMENIRFGKLDASDEevYTAAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:TIGR02142 86 LFPhLSVRGNLRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 621 TSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGGL 684
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
454-673 |
2.80e-24 |
|
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: 101.56 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGqvI 533
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFA-TTIMENIRFG-KL-----DASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIAR 606
Cdd:cd03301 75 AMVFQNYALYPhMTVYDNIAFGlKLrkvpkDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHrlSTVRA---AHSIIVMANGQVCEAG 673
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTH--DQVEAmtmADRIAVMNDGQIQQIG 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
471-691 |
3.00e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.07 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLL---ERfYDPEAGSVTLDGHDLRTLNPS--WLRGQVIGFisQEPV---- 541
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPDerARAGIFLAF--QYPVeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 542 ----LFATTIMENIRFGKLDASD--EEVYTAAREAN-AHEFISSFpdgystvVGErgtTLSGGQKQRLAIARALIKQPTV 614
Cdd:COG0396 92 vsvsNFLRTALNARRGEELSAREflKLLKEKMKELGlDEDFLDRY-------VNE---GFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 615 LILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRAAHSIIVMANGQVCEAGTHE---ELLKKGglYSEL 688
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElalELEEEG--YDWL 239
|
...
gi 27753995 689 IRR 691
Cdd:COG0396 240 KEE 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
454-699 |
3.61e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGS---VTLDGHDLrTLNPSWLRG 530
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITL-TAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAH----EFISSFPdgystvvgergTTLSGGQKQRL 602
Cdd:PRK13640 84 EKVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADvgmlDYIDSEP-----------ANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 603 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
250
....*....|....*....
gi 27753995 681 KgglySELIRRQTLDASLT 699
Cdd:PRK13640 233 K----VEMLKEIGLDIPFV 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
468-679 |
3.76e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.14 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSV-----TLDGHdlRTLNPSW-----LRGQViGFIS 537
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSQQKglirqLRQHV-GFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 538 QEPVLFA-TTIMENIRFGKL---DASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIARALIKQPT 613
Cdd:PRK11264 92 QNFNLFPhRTVLENIIEGPVivkGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 614 VLILDEATSALDAEserVVQEALDR----ASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK11264 165 VILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALF 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
457-691 |
5.23e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPsWLRGQVIGFI 536
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQEPVL-FATTIMENIRFGKL------DASDEEVYTAAREANAHEFISSFpdgYstvvgergTTLSGGQKQRLAIARALI 609
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGRAphglsrAEDDALVAAALAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 610 ------KQPTVLILDEATSALD-AESERVVQEALDRA-SAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
250
....*....|.
gi 27753995 681 KgglysELIRR 691
Cdd:PRK13548 231 P-----ETLRR 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
453-676 |
7.57e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 7.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDL---RTLNPS 526
Cdd:COG4161 2 SIQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLET---PDSGQLNIAGHQFdfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 ---WLRGQViGFISQE----PVLfatTIMENI--------RFGKLDASDEEVYTAAReANAHEFISSFPdgystvvgerg 591
Cdd:COG4161 76 airLLRQKV-GMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMKLLAR-LRLTDKADRFP----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 592 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVR-AAHSIIVMANGQV 669
Cdd:COG4161 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARkVASQVVYMEKGRI 219
|
....*..
gi 27753995 670 CEAGTHE 676
Cdd:COG4161 220 IEQGDAS 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
472-673 |
8.16e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 100.06 E-value: 8.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLP---SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLN--------PSWLRGqvIGFISQEP 540
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFdsrkkinlPPQQRK--IGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 541 VLFA-TTIMENIRFGKLDASDEEvytaaREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 619
Cdd:cd03297 85 ALFPhLNVRENLAFGLKRKRNRE-----DRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 620 ATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 673
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
458-694 |
8.17e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.69 E-value: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 458 NVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG-QVIGFI 536
Cdd:PRK13639 6 DLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQEP--VLFATTIMENIRFGKLDA--SDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQP 612
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAVGMEGFEN-------KPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 613 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKKgglySELIR 690
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD----IETIR 232
|
....
gi 27753995 691 RQTL 694
Cdd:PRK13639 233 KANL 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
472-652 |
1.01e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.40 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDL--RTLNPSWLRGQvIGFISQEPVLFA 544
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRR-IGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENIRFG------KLDAsDEEVYTAAREAnahefisSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 618
Cdd:PRK14243 105 KSIYDNIAYGaringyKGDM-DELVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190
....*....|....*....|....*....|....
gi 27753995 619 EATSALDAESERVVQEALDRASAGRTVLVIAHRL 652
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
458-678 |
1.39e-23 |
|
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: 101.47 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 458 NVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHdlrtlnpswlrgqvIGFIS 537
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 538 QEPVLFATTIMENIRFGKldASDEEVYTAAREA-NAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 616
Cdd:cd03291 105 QFSWIMPGTIKENIIFGV--SYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 617 LDEATSALDAESERVVQEA-LDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
454-673 |
1.52e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 99.36 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSY-PCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQV 532
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEAR-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFA-TTIMENIR-FGKLDASDEEVYTAAREanahEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIK 610
Cdd:cd03266 80 LGFVSDSTGLYDrLTARENLEyFAGLYGLKGDELTARLE----ELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 611 QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 673
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
453-700 |
3.05e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPcrPGFNV----LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrTLNPS-- 526
Cdd:PRK13641 2 SIKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGnk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 ---WLRGQViGFISQ--EPVLFATTIMENIRFGKLD--ASDEEvytaAREAnAHEFISSFpdGYSTVVGERGT-TLSGGQ 598
Cdd:PRK13641 79 nlkKLRKKV-SLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDE----AKEK-ALKWLKKV--GLSEDLISKSPfELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHE 676
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPK 230
|
250 260
....*....|....*....|....
gi 27753995 677 ELLKKgglySELIRRQTLDASLTS 700
Cdd:PRK13641 231 EIFSD----KEWLKKHYLDEPATS 250
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
472-679 |
3.24e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG---QVIGFISQEPVLFA-TTI 547
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 548 MENIRFG------KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALIKQPTVLILDEAT 621
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 622 SALDAESERVVQEALDRASAG--RTVLVIAHRL-STVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
391-663 |
3.38e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.50 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 391 GDLMsflvasQTVQrsmaslsvLFGQVVRGLS-------------AGA-RVFEYM-ALSPVIPLTGGYCIPNKDIRGSIT 455
Cdd:COG4178 299 GGLM------QAAS--------AFGQVQGALSwfvdnyqslaewrATVdRLAGFEeALEAADALPEAASRIETSEDGALA 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 456 FQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLlerfYDPEAGSVTLDGHDlRTLnpswlrgq 531
Cdd:COG4178 365 LEDLTLRTP--DGRPLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL----WPYGSGRIARPAGA-RVL-------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 vigFISQEPVLFATTIMENIRF--GKLDASDEEVYTAAREANAHEFISSFpdgysTVVGERGTTLSGGQKQRLAIARALI 609
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLL 501
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 610 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRlSTVRAAHSIIV 663
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFHDRVL 554
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
452-689 |
5.35e-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: 99.54 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYpCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEaGSVTLDGHDLRTLNPSWLRgQ 531
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEPVLFATTIMENIR-FGKLdaSDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIK 610
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 611 QPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 689
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
454-673 |
5.43e-23 |
|
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: 97.67 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlrgQVI 533
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT-TIMENIRFGKLdasdeevYTAAREANAHEFISsfpdgystVVGERGT------TLSGGQKQRLAIAR 606
Cdd:cd03268 75 GALIEAPGFYPNlTARENLRLLAR-------LLGIRKKRIDEVLD--------VVGLKDSakkkvkGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 673
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
454-669 |
5.79e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdGHDLRtlnpswlrgqvI 533
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFAT--TIMENIRfgkldasdeEVYTAAREANAHEFISSF---PDGYSTVVGergtTLSGGQKQRLAIARAL 608
Cdd:COG0488 381 GYFDQHQEELDPdkTVLDELR---------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 609 IKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH-R--LSTVraAHSIIVMANGQV 669
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGV 507
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
469-679 |
6.19e-23 |
|
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: 103.23 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 469 FNVLKDFTLKLPSGKIVALVGQSGGGKT----TVASLLERFYDPEAGSVTLDGHDLRTLNPSWL---RGQVIGFISQEPV 541
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrriRGNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 542 -----LFatTI----MENIRFgKLDASDEEVYTAAREA-------NAHEFISSFPdgystvvgergTTLSGGQKQRLAIA 605
Cdd:COG4172 103 tslnpLH--TIgkqiAEVLRL-HRGLSGAAARARALELlervgipDPERRLDAYP-----------HQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 606 RALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:COG4172 169 MALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
.
gi 27753995 679 L 679
Cdd:COG4172 245 F 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
454-650 |
6.71e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.78 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYP-CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlnPSWLRGQV 532
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IgfisQEPVLFA-TTIMENIRFG-KLDAsdeeVYTAAREANAHEFISsfpdgystVVGERGT------TLSGGQKQRLAI 604
Cdd:COG4525 82 F----QKDALLPwLNVLDNVAFGlRLRG----VPKAERRARAEELLA--------LVGLADFarrriwQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27753995 605 ARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 650
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
454-681 |
8.55e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.01 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFN---VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG 530
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQRL 602
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 603 AIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 27753995 681 K 681
Cdd:PRK13633 234 E 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
454-679 |
9.72e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP-------S 526
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 WLRgQVIGFIS----QEPVLFAttimeniRF----GKLDASDEEVYTAA-----REANAHEFISsfpdgystvvgergtT 593
Cdd:COG4604 79 ILR-QENHINSrltvRELVAFG-------RFpyskGRLTAEDREIIDEAiayldLEDLADRYLD---------------E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 594 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRLSTVrAAHS--IIVMANGQV 669
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFA-SCYAdhIVAMKDGRV 214
|
250
....*....|
gi 27753995 670 CEAGTHEELL 679
Cdd:COG4604 215 VAQGTPEEII 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
457-679 |
1.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.63 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNpSWLRGQVIGFI 536
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQEP--VLFATTIMENIRFGKLDAS--DEEVYTAAREA----NAHEFISSFPdgystvvgergTTLSGGQKQRLAIARAL 608
Cdd:PRK13642 87 FQNPdnQFVGATVEDDVAFGMENQGipREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 609 IKQPTVLILDEATSALD----AESERVVQEALDRASAgrTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK13642 156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
457-691 |
1.07e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.41 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVasllerFY------DPEAGSVTLDGHDLRTLnPSWLRG 530
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHL-PMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QV-IGFISQEPVLFAT-TIMENIR----FGKLDAsdeevytAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAI 604
Cdd:COG1137 77 RLgIGYLPQEASIFRKlTVEDNILavleLRKLSK-------KEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 605 ARALIKQPTVLILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRlstVRAAHSII----VMANGQVCEAGTHE 676
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GIGVLITDHN---VRETLGICdrayIISEGKVLAEGTPE 221
|
250
....*....|....*
gi 27753995 677 ELLKkgglySELIRR 691
Cdd:COG1137 222 EILN-----NPLVRK 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
453-676 |
1.43e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYpcrpGFN-VLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGH--DL-RTLNP 525
Cdd:PRK11124 2 SIQLNGINCFY----GAHqALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNhfDFsKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 526 SWLRG--QVIGFISQEPVLFA-TTIMEN-----IRFGKLdaSDEEVYTAAREANAH----EFISSFPdgystvvgergTT 593
Cdd:PRK11124 75 KAIRElrRNVGMVFQQYNLWPhLTVQQNlieapCRVLGL--SKDQALARAEKLLERlrlkPYADRFP-----------LH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 594 LSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCE 671
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARkTASRVVYMENGHIVE 221
|
....*
gi 27753995 672 AGTHE 676
Cdd:PRK11124 222 QGDAS 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
471-668 |
3.53e-22 |
|
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: 95.58 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGH----DLRTLNPS---WLRGQVIGFISQepvlF 543
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRTIGYVSQ----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 544 ATTI---------MENIRfgKLDASDEEVYTAAREANAH-----EFISSFPdgystvvgergTTLSGGQKQRLAIARALI 609
Cdd:COG4778 102 LRVIprvsaldvvAEPLL--ERGVDREEARARARELLARlnlpeRLWDLPP-----------ATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 610 KQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 668
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
466-679 |
3.63e-22 |
|
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: 98.63 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVlkDFTLKLPSGKIVALVGQSGGGKTTVASL---LERfydPEAGSVTLDGHDL----RTLN-PSWLRGqvIGFIS 537
Cdd:COG4148 11 RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLqdsaRGIFlPPHRRR--IGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 538 QEPVLFAT-TIMENIRFGkldasdeevYTAAREANAHefiSSFPD-----GYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:COG4148 84 QEARLFPHlSVRGNLLYG---------RKRAPRAERR---ISFDEvvellGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 679
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERlrDELDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
471-638 |
3.65e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLErfydPEAGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATT 546
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTllkiVASLIS----PTSGTLLFEGEDISTLKPEIYRQQV-SYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 IMENIRFG---KLDASDEEVYTAareanaheFISSF--PDgysTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 621
Cdd:PRK10247 97 VYDNLIFPwqiRNQQPDPAIFLD--------DLERFalPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170
....*....|....*..
gi 27753995 622 SALDAESERVVQEALDR 638
Cdd:PRK10247 166 SALDESNKHNVNEIIHR 182
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
454-677 |
5.23e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.48 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqvi 533
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 gfisQEPV--------LFA-TTIMENIRFG----KLdaSDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQ 600
Cdd:PRK09452 85 ----NRHVntvfqsyaLFPhMTVFENVAFGlrmqKT--PAAEITPRVMEALRMVQLEEFAQ-------RKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESERVVQ---EALDRaSAGRTVLVIAH----RLSTvraAHSIIVMANGQVCEAG 673
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQnelKALQR-KLGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDG 227
|
....
gi 27753995 674 THEE 677
Cdd:PRK09452 228 TPRE 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
457-681 |
5.32e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.25 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYpcrpGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlNPSWLRGQVIGF 535
Cdd:PRK11432 10 KNITKRF----GSNtVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 536 ISQEPVLFA-TTIMENIRFG--KLDASDEEVYTAAREANAHEFISSFPDGYstvVGErgttLSGGQKQRLAIARALIKQP 612
Cdd:PRK11432 83 VFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRY---VDQ----ISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 613 TVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 681
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRelQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
454-674 |
5.93e-22 |
|
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: 95.19 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASL---LERfydPEAGSVTLDGHDLRTLNP---S 526
Cdd:COG4181 9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDEdarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 WLRGQVIGFISQEPVLFAT-TIMENIRFGKLDASDEEVYTAAREANAhefissfpdgysTV-VGERGT----TLSGGQKQ 600
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARALLE------------RVgLGHRLDhypaQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGT 674
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
469-678 |
6.21e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 469 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLD----GHDLRTLNPSWLRGQ-----------VI 533
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYSkkiknfkelrrRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEP--VLFATTIMENIRFG-------KLDASDEEVYTAAREANAHEFISSFPDGystvvgergttLSGGQKQRLAI 604
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFG-----------LSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 605 ARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
475-678 |
6.58e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 97.34 E-value: 6.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 475 FTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHD-----------LRT------------LNPSwlrgQ 531
Cdd:PRK11308 36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkadpeaqklLRQkiqivfqnpygsLNPR----K 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEPVLFATtimenirfgKLDAsdeevytAAREANAHEFISSfpdgystvVGERGT-------TLSGGQKQRLAI 604
Cdd:PRK11308 110 KVGQILEEPLLINT---------SLSA-------AERREKALAMMAK--------VGLRPEhydryphMFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 605 ARALIKQPTVLILDEATSALDAESERVV-------QEALdrasaGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHE 676
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKE 240
|
..
gi 27753995 677 EL 678
Cdd:PRK11308 241 QI 242
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
180-397 |
7.10e-22 |
|
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: 96.40 E-value: 7.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 180 LLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 259
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 260 TQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERY 339
Cdd:cd18546 125 LTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 340 QAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL 397
Cdd:cd18546 205 AELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFL 262
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
471-704 |
8.15e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLrGQVIGFISQEPVL-FATTIME 549
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-SRRVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 550 NIRFGK------LDASDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 623
Cdd:PRK09536 97 VVEMGRtphrsrFDTWTETDRAAVERAMERTGVAQFAD-------RPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 624 LDAESE-RVVQEALDRASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKKGGLyselirRQTLDA-SLTS 700
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTL------RAAFDArTAVG 243
|
....
gi 27753995 701 TPPA 704
Cdd:PRK09536 244 TDPA 247
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
454-679 |
1.07e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.65 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSY---PCRpgfnvlkdFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRG 530
Cdd:PRK10771 2 LKLTDITWLYhhlPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFisQEPVLFA-TTIMENIRFG-----KLDASD-EEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLA 603
Cdd:PRK10771 73 VSMLF--QENNLFShLTVAQNIGLGlnpglKLNAAQrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 604 IARALIKQPTVLILDEATSALD----AESERVVQEALDRASAgrTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQL--TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217
|
.
gi 27753995 679 L 679
Cdd:PRK10771 218 L 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
471-691 |
1.19e-21 |
|
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: 94.15 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGQV-IGFISQEPVLFAT-TIM 548
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARLgIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 549 ENIRfgkldASDEEVY--TAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD- 625
Cdd:cd03218 94 ENIL-----AVLEIRGlsKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 626 ---AESERVVQEALDRasaGRTVLVIAHrlsTVRAAHSII----VMANGQVCEAGTHEELLKkgglySELIRR 691
Cdd:cd03218 167 iavQDIQKIIKILKDR---GIGVLITDH---NVRETLSITdrayIIYEGKVLAEGTPEEIAA-----NELVRK 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
443-673 |
1.45e-21 |
|
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: 93.75 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 443 YCIPNKdIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlrt 522
Cdd:cd03220 10 YPTYKG-GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 523 lNPSWLRGQVIGFisqEPVLfatTIMENIRF-----GKLDASDEEVYtaareanahEFISSFPDgystvVGERGT----T 593
Cdd:cd03220 84 -RVSSLLGLGGGF---NPEL---TGRENIYLngrllGLSRKEIDEKI---------DEIIEFSE-----LGDFIDlpvkT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 594 LSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCE 671
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222
|
..
gi 27753995 672 AG 673
Cdd:cd03220 223 DG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
467-676 |
1.47e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.95 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 467 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT- 545
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENI-------RFGKLDASdeevytAAREAnAHEFISSF-----PDgysTVVGErgttLSGGQKQRLAIARALIKQPT 613
Cdd:COG3845 96 TVAENIvlgleptKGGRLDRK------AARAR-IRELSERYgldvdPD---AKVED----LSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 614 VLILDEATSAL-DAESERVVqEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVceAGTHE 676
Cdd:COG3845 162 ILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKV--VGTVD 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
454-650 |
2.93e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.00 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdLRTLNPSWLRGQVI 533
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 gfiSQEPVLFATTIMENIRFGKLDASdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 613
Cdd:PRK11248 77 ---QNEGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 27753995 614 VLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 650
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
457-678 |
2.97e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrTLNPSWLRGqvIGFI 536
Cdd:PRK11607 23 RNLTKSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRP--INMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQEPVLFA-TTIMENIRFG-KLDA-SDEEVYTAARE----ANAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALI 609
Cdd:PRK11607 97 FQSYALFPhMTVEQNIAFGlKQDKlPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 610 KQPTVLILDEATSALDAE-SERVVQEALD-RASAGRTVLVIAH-RLSTVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlRDRMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
453-678 |
3.94e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.54 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPswlRGQV 532
Cdd:PRK10851 2 SIEIANIKKSFGRT---QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFA-TTIMENIRFG-KLDASDEEVYTAAREANAHEFI-----SSFPDGYSTvvgergtTLSGGQKQRLAIA 605
Cdd:PRK10851 76 VGFVFQHYALFRhMTVFDNIAFGlTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYPA-------QLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 606 RALIKQPTVLILDEATSALDAESE-------RVVQEALDRASagrtVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRkelrrwlRQLHEELKFTS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
453-666 |
5.37e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA---GSVTLDGHDLRTLNPSwLR 529
Cdd:COG4136 1 MLSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAE-QR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 GqvIGFISQEPVLFA-TTIMENIRFG-----KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLA 603
Cdd:COG4136 77 R--IGILFQDDLLFPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 604 IARALIKQPTVLILDEATSALDAE-----SERVVQEAldRASAGRTVLViAHRLSTVRAAHSIIVMAN 666
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAAlraqfREFVFEQI--RQRGIPALLV-THDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
453-682 |
6.59e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.69 E-value: 6.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYpcRPG----FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghDLRTLNPS-- 526
Cdd:PRK13646 2 TIRFDNVSYTY--QKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD--DITITHKTkd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 -WLRG--QVIGFISQ--EPVLFATTIMENIRFG----KLDAsdEEVytaarEANAHEFISSFpdGYS-TVVGERGTTLSG 596
Cdd:PRK13646 78 kYIRPvrKRIGMVFQfpESQLFEDTVEREIIFGpknfKMNL--DEV-----KNYAHRLLMDL--GFSrDVMSQSPFQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 597 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 673
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQT 228
|
....*....
gi 27753995 674 THEELLKKG 682
Cdd:PRK13646 229 SPKELFKDK 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
454-679 |
7.40e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 92.45 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDP-EAGSVTLDGHDLRTLNPSWLRGQv 532
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGEDVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEpvlFATTIMENIR---------FGKLDASDEevYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLA 603
Cdd:COG1119 80 IGLVSPA---LQLRFPRDETvldvvlsgfFDSIGLYRE--PTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 604 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV-IAHRLSTVRAA--HsIIVMANGQVCEAGTHEELL 679
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGitH-VLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
457-669 |
7.99e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.10 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP---SWLRGQV 532
Cdd:PRK10535 8 KDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFA-TTIMENIRFGKLDASDEevyTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:PRK10535 88 FGFIFQRYHLLShLTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRAAHSIIVMANGQV 669
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-679 |
9.15e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.28 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFAT 545
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRV-QMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 -TIMENIRFG----KLDASDEEVYTAAREANAHefiSSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:PRK14247 97 lSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 621 TSALDAESERVVQEALDRASAGRTVLVIAH-RLSTVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
453-681 |
1.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---- 526
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 WLRGQViGFISQ--EPVLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISSfpdgysTVVGERGTTLSGGQKQRL 602
Cdd:PRK13649 82 QIRKKV-GLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGISE------SLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 603 AIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 27753995 681 K 681
Cdd:PRK13649 235 D 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
468-678 |
1.22e-20 |
|
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: 90.89 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVIGFISQEPVL-FATT 546
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVR-RRIGIVFQDLSVdDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 IMENIR-FGKLDAsdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 625
Cdd:cd03265 90 GWENLYiHARLYG----VPGAERRERIDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 626 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:cd03265 164 PQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
470-673 |
1.55e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 90.42 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 470 NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnpSWLRGQVIGFISQEPVLF-ATTIM 548
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYLPEERGLYpKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 549 ENIR-FGKL-DASDEEvytAAREANahEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 626
Cdd:cd03269 89 DQLVyLAQLkGLKKEE---ARRRID--EWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27753995 627 ESERVVQEAL-DRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 673
Cdd:cd03269 162 VNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
472-652 |
1.77e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PE---AGSVTLDGHDL--RTLNPSWLRGQvIGFISQEPVLFA 544
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysPRTDTVDLRKE-IGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENIRFG-KLDA-SDEEVYTAAREANAHEfiSSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:PRK14239 100 MSIYENVVYGlRLKGiKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|
gi 27753995 623 ALDAESERVVQEALDRASAGRTVLVIAHRL 652
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
456-650 |
1.78e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 456 FQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswlRGQVIGF 535
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 536 ISQEPVLFAT-TIMENI-----RFGKLDASDEEVYTA--------AREANAHEFISSFpDGYS------TVVGERG---- 591
Cdd:COG0488 66 LPQEPPLDDDlTVLDTVldgdaELRALEAELEELEAKlaepdedlERLAELQEEFEAL-GGWEaearaeEILSGLGfpee 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 592 ------TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQ--EALDRASAGrTVLVIAH 650
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
472-667 |
2.49e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.60 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlRGQVIGFISQEPVLfatTIMENI 551
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYSLLPWL---TVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 552 RFGkLDASDEEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERV 631
Cdd:TIGR01184 76 ALA-VDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 27753995 632 VQEALDR--ASAGRTVLVIAHRL-STVRAAHSIIVMANG 667
Cdd:TIGR01184 153 LQEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
471-671 |
2.85e-20 |
|
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: 91.02 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG-----QVIGFISQEPVLFAT 545
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIR-----FGKLDASdeevytaAREANAHEFISSFpDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:TIGR02769 106 TVRQIIGeplrhLTSLDES-------EQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 621 TSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCE 671
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
462-664 |
3.80e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 462 SYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqvigfISQEPV 541
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ---------RSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 542 LFATTIMENIRFG---------KLDASDEEVYTAAREANahefissfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQP 612
Cdd:NF040873 69 SLPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALERV----------GLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27753995 613 TVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRAAHSIIVM 664
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
457-679 |
4.04e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.67 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPG------FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlRG 530
Cdd:COG4167 8 RNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEPvlfATTIMENIRFGK-LDA--------SDEEvytaaREANAHEFIssfpdgysTVVGERG-------TTL 594
Cdd:COG4167 87 KHIRMIFQDP---NTSLNPRLNIGQiLEEplrlntdlTAEE-----REERIFATL--------RLVGLLPehanfypHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 595 SGGQKQRLAIARALIKQPTVLILDEATSALDAeSERV--------VQEALdrasaGRTVLVIAHRLSTVR-AAHSIIVMA 665
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVKhISDKVLVMH 224
|
250
....*....|....
gi 27753995 666 NGQVCEAGTHEELL 679
Cdd:COG4167 225 QGEVVEYGKTAEVF 238
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
470-669 |
4.75e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.87 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 470 NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSW---LRGQVIGFISQ-EPVLFAT 545
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLGFIYQfHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIRFGKLDASdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 625
Cdd:PRK11629 103 TALENVAMPLLIGK---KKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27753995 626 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 669
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
457-673 |
7.22e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPGF--------NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEaGSVTLDGHDLRTLNpswl 528
Cdd:PRK15134 279 EQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLN---- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RGQVIGFISQEPVLF-------------ATTIMENIRFGKLDAS----DEEVYTAARE-----ANAHEFISSFpdgystv 586
Cdd:PRK15134 354 RRQLLPVRHRIQVVFqdpnsslnprlnvLQIIEEGLRVHQPTLSaaqrEQQVIAVMEEvgldpETRHRYPAEF------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 587 vgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQE---ALDRASAGR---TVLVIAHRLSTVRA-AH 659
Cdd:PRK15134 427 --------SGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCH 494
|
250
....*....|....
gi 27753995 660 SIIVMANGQVCEAG 673
Cdd:PRK15134 495 QVIVLRQGEVVEQG 508
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
471-680 |
1.08e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.46 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVtldghdlrtlnpsWLRgQVIGFISQEPVLFATTIMEN 550
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAE-RSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 551 IRFgkldaSDEEvyTAAREANA------HEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL 624
Cdd:PTZ00243 741 ILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 625 DAE-SERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
117-650 |
1.13e-19 |
|
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: 93.32 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 117 KLFWHFLHPHLLALGAAIVLALGAALVNVqipLLLGQLVEIVAKYTrdhmgsfvSESRKLSVQLLLLYGVQGLLTFGYLV 196
Cdd:COG4615 2 NLLRLLLRESRWLLLLALLLGLLSGLANA---GLIALINQALNATG--------AALARLLLLFAGLLVLLLLSRLASQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 197 LLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFkSSFKLVISQGLRSCTQVIGSLVSLSMLSPRL 276
Cdd:COG4615 71 LLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 277 TLMLAVVTPALMGVGTLMGSGLRKLSRQcqeqiARAtgvADEAL-GNVRTV----RAFAM-EKREEERYQAELESCCCKA 350
Cdd:COG4615 150 FLLTLVLLGLGVAGYRLLVRRARRHLRR-----ARE---AEDRLfKHFRALlegfKELKLnRRRRRAFFDEDLQPTAERY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 351 EEL-GRGIALFqgLSNIAF-NCMVLGTLfigGSLVAGQQLkggdlmsfLVASQTVQRSMASLSVLF-----GQVVRGLSA 423
Cdd:COG4615 222 RDLrIRADTIF--ALANNWgNLLFFALI---GLILFLLPA--------LGWADPAVLSGFVLVLLFlrgplSQLVGALPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 424 --GARV-FE-YMALSPVIPLTGGYCIPNKDIR-----GSITFQNVTFSYPC---RPGFnVLKDFTLKLPSGKIVALVGQS 491
Cdd:COG4615 289 lsRANVaLRkIEELELALAAAEPAAADAAAPPapadfQTLELRGVTYRYPGedgDEGF-TLGPIDLTIRRGELVFIVGGN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 492 GGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTImenirfGKLDASDEEVytaarean 571
Cdd:COG4615 368 GSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR-QLFSAVFSDFHLFDRLL------GLDGEADPAR-------- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 572 AHEFIS--------SFPDG-YSTvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEAL--DRAS 640
Cdd:COG4615 433 ARELLErleldhkvSVEDGrFST------TDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELlpELKA 506
|
570
....*....|
gi 27753995 641 AGRTVLVIAH 650
Cdd:COG4615 507 RGKTVIAISH 516
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-679 |
3.31e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF---YDPEA---GSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFA 544
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKIkvdGKVLYFGKDIFQIDAIKLRKEV-GMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 -TTIMENIRFGKLDASDEEvytaAREANAHEFISSFPDGYSTVVGER----GTTLSGGQKQRLAIARALIKQPTVLILDE 619
Cdd:PRK14246 104 hLSIYDNIAYPLKSHGIKE----KREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 620 ATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
454-650 |
4.46e-19 |
|
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: 84.04 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTldghdlrtlnpsWLRGQVI 533
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------------WGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQepvlfattimenirfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPT 613
Cdd:cd03221 66 GYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*..
gi 27753995 614 VLILDEATSALDAESERVVQEALdRASAGrTVLVIAH 650
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
454-694 |
5.56e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.98 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR-GQV 532
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEP--VLFATTIMENIRFGKLDAS--DEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARAL 608
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 609 IKQPTVLILDEATSALD----AESERVVQEALDraSAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKKgg 683
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQK--ELGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAE-- 232
|
250
....*....|.
gi 27753995 684 lySELIRRQTL 694
Cdd:PRK13636 233 --KEMLRKVNL 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
454-695 |
6.19e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 533
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR-KFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEP--VLFATTIMENIRFGKLDASDEEVYTAAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLkkggLYSEL 688
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIF----LQPDL 231
|
....*..
gi 27753995 689 IRRQTLD 695
Cdd:PRK13652 232 LARVHLD 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
449-688 |
6.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 449 DIRGSITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPS 526
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI----PA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 527 WLRG--------QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAhefISSFPDGYstvVGERGTTL 594
Cdd:PRK13645 78 NLKKikevkrlrKEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 595 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCE 671
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
250
....*....|....*..
gi 27753995 672 AGTHEELLKKGGLYSEL 688
Cdd:PRK13645 232 IGSPFEIFSNQELLTKI 248
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
471-669 |
6.72e-19 |
|
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: 84.79 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPV---LFAT-T 546
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKregLVLDlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 IMENIRFGKLdasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSALDA 626
Cdd:cd03215 95 VAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27753995 627 ESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:cd03215 138 GAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
466-671 |
7.60e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 7.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--------------- 530
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiqmvfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 ----QVIGFISQEPVLFATTIMEnirfgkldasdeevytAAREANAHEFISSFpDGYSTVVGERGTTLSGGQKQRLAIAR 606
Cdd:PRK10419 102 vnprKTVREIIREPLRHLLSLDK----------------AERLARASEMLRAV-DLDDSVLDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 607 ALIKQPTVLILDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCE 671
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
176-427 |
9.30e-19 |
|
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: 87.50 E-value: 9.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRL--TTDVQEFKSSfkLVIS 253
Cdd:cd18570 44 ISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFndANKIREAISS--TTIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 254 QGLRSCTqVIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEK 333
Cdd:cd18570 122 LFLDLLM-VIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 334 REEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVL 413
Cdd:cd18570 201 QFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINL 280
|
250
....*....|....
gi 27753995 414 FGQVVRGLSAGARV 427
Cdd:cd18570 281 QPKIQEAKVAADRL 294
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
465-680 |
1.33e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 465 CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLErFYDPE----AGSVTLDGHdlrTLNPSWLRgQVIGFISQEP 540
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMR-AISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 541 VLFAT-TIMENIRFGKLDASDEEVYTAAREANAHEFIS--SFPDGYSTVVGERGTT--LSGGQKQRLAIARALIKQPTVL 615
Cdd:TIGR00955 109 LFIPTlTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 616 ILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLST--VRAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
471-669 |
2.06e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVtLDG----HDLRtlnpswlrgQVIGFISQEPVLFA-T 545
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEAR---------EDTRLMFQDARLLPwK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIRFGkldasdeevYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 625
Cdd:PRK11247 97 KVIDNVGLG---------LKGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27753995 626 AESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQV 669
Cdd:PRK11247 166 ALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
454-660 |
2.34e-18 |
|
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: 82.97 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVasllerfydpeagsvtldghdLRTLN---PsWLRG 530
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL---------------------FRALAglwP-WGSG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QV-------IGFISQEPVLFATTIMENIrfgkldasdeeVYTAAREanahefissfpdgystvvgergttLSGGQKQRLA 603
Cdd:cd03223 57 RIgmpegedLLFLPQRPYLPLGTLREQL-----------IYPWDDV------------------------LSGGEQQRLA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 604 IARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHRlSTVRAAHS 660
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR-PSLWKFHD 155
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-427 |
3.10e-18 |
|
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: 86.08 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLVEIVAKYTR-------------DHMGSFVSesrkLSVQLLLLYGVQGLLTFGYLV 196
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEAsflplvpaslgpaDPRGQLWL----LGGLTVAAFLLESLFQYLSGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 197 LLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRL 276
Cdd:cd18565 77 LWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 277 TLMLAVVTPaLMGVGTLMGSG-LRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGR 355
Cdd:cd18565 157 ALVALLPVP-LIIAGTYWFQRrIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 356 GIALFQGLSNIAFNCMVLGTLFIGGSLV------AGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18565 236 LRAAFFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
468-679 |
4.44e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHD--LRTLNPSWLRGqvIGFISQEPVLFAT 545
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRG--IGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIRFGKLDASDeEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 625
Cdd:PRK10895 93 LSVYDNLMAVLQIRD-DLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 626 AES----ERVVQEALDRasaGRTVLVIAHRL-STVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK10895 170 PISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
453-697 |
4.95e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.93 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnpswLRGQV 532
Cdd:PRK15056 6 GIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQE-------PVLFATTIMENiRFGKL------DASDEEVYTAARE-ANAHEFissfpdgYSTVVGErgttLSGGQ 598
Cdd:PRK15056 80 VAYVPQSeevdwsfPVLVEDVVMMG-RYGHMgwlrraKKRDRQIVTAALArVDMVEF-------RHRQIGE----LSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAESE-RVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEE 677
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
|
250 260
....*....|....*....|...
gi 27753995 678 LLKKGGL---YSELIRRQTLDAS 697
Cdd:PRK15056 228 TFTAENLelaFSGVLRHVALNGS 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
466-650 |
6.52e-18 |
|
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: 82.54 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGqvIGFISQEPVLFAT 545
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG--LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 -TIMENIRFGKLDASDEEVYTAAREANAHEFiSSFPDGYstvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSAL 624
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 27753995 625 DAESERVVQEAL-DRASAGRTVLVIAH 650
Cdd:cd03231 157 DKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
468-669 |
6.85e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLL--ERfyDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT 545
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 ----TIMENI-----------RFGKLDasdeevyTAAREANAHEFISSF---PDGYSTVVGergtTLSGGQKQRLAIARA 607
Cdd:COG3845 348 vpdmSVAENLilgryrrppfsRGGFLD-------RKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 608 LIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
476-679 |
7.10e-18 |
|
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: 87.55 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 476 TLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL----DGHDLRTLNPSwLRGQV---IGFISQEPVLFA-TTI 547
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRAkryIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 548 MENIRFG-KLDASDE-----EVYT----AAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALIKQPTVLIL 617
Cdd:TIGR03269 383 LDNLTEAiGLELPDElarmkAVITlkmvGFDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 618 DEATSALDAESERVVQEAL--DRASAGRTVLVIAHRLSTV-----RAAhsiiVMANGQVCEAGTHEELL 679
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVldvcdRAA----LMRDGKIVKIGDPEEIV 516
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
457-673 |
8.18e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 8.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPG-FNVLK-------DFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 528
Cdd:PRK10261 317 RNLVTRFPLRSGlLNRVTrevhaveKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RG--QVIGFISQEPvlFAT---------TIMENIRFGKLDASDEevyTAAREANAHEFISSFPDGYSTVVGErgttLSGG 597
Cdd:PRK10261 397 QAlrRDIQFIFQDP--YASldprqtvgdSIMEPLRVHGLLPGKA---AAARVAWLLERVGLLPEHAWRYPHE----FSGG 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 598 QKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALD-RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 673
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
471-682 |
8.21e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.19 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA--GSVTLDGHDLRTLNPS--WLRGQVIGFisQEPVLFA-T 545
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEerARLGIFLAF--QYPPEIPgV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIRFgkldasdeevytaareanahefissfpdgystvVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATSALD 625
Cdd:cd03217 93 KNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 626 AESERVVQEALDR-ASAGRTVLVIAHR---LSTVRA--AHsiiVMANGQVCEAGTHE---ELLKKG 682
Cdd:cd03217 137 IDALRLVAEVINKlREEGKSVLIITHYqrlLDYIKPdrVH---VLYDGRIVKSGDKElalEIEKKG 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
471-679 |
1.07e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlRGQVIGFISQEPVLFAT----- 545
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDK--DGQLKVADKNQLRLLRTrltmv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 ----------TIMENIR--------FGKLDASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIARA 607
Cdd:PRK10619 98 fqhfnlwshmTVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQGKYP-----------VHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 608 LIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVRAAHS-IIVMANGQVCEAGTHEELL 679
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDpelvGEVLRIMQQL---AEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
477-678 |
1.78e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.73 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 477 LKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWL---RGQVIGFisQEPVLFAT-TIMENIr 552
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiarMGVVRTF--QHVRLFREmTVIENL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 553 fgkLDASDEEVYT----------AAR--EANAHEFISSFPD--GYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 618
Cdd:PRK11300 102 ---LVAQHQQLKTglfsgllktpAFRraESEALDRAATWLErvGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 619 EATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-680 |
3.50e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.81 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDLRT--LNPSWLRGQViGFISQEPVLF 543
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSpdVDPIEVRREV-GMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 544 A-TTIMENIRFG-KL-------DASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIARALIKQPTV 614
Cdd:PRK14267 98 PhLTIYDNVAIGvKLnglvkskKELDERVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 615 LILDEATSALDAESERVVQEALDRASAGRTVLVIAHR-LSTVRAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
453-655 |
3.95e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA-----GSVTLDGHDL--RTLNP 525
Cdd:PRK14258 7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 526 SWLRGQViGFISQEPVLFATTIMENIRFG--------KLDAsDEEVYTAAREANahefissFPDGYSTVVGERGTTLSGG 597
Cdd:PRK14258 84 NRLRRQV-SMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI-DDIVESALKDAD-------LWDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 598 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 655
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
468-678 |
4.26e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLK--DFTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT 545
Cdd:PRK15439 23 GVEVLKgiDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 -TIMENIRFG--KLDASDEEVYTAAREANAHEFISSfpdgystvvgeRGTTLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:PRK15439 101 lSVKENILFGlpKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 623 ALD-AESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK15439 170 SLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
477-678 |
4.48e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.60 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 477 LKLPSGKIVALVGQSGGGKTTV----ASLLERFYDPEA------GSVTLDGHDLRTLNPSwlRGQViGFISQEPVLF-AT 545
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGShiellgRTVQREGRLARDIRKS--RANT-GYIFQQFNLVnRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIRFGKLDASD-----EEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:PRK09984 102 SVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 621 TSALDAESERVVQEALD--RASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK09984 180 IASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
453-692 |
4.50e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.28 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRPG-------------------FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSV 513
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 514 TLDGhdlrtlNPSWLRGQVIGFisqEPVLfatTIMENIRFGK--LDASDEEVytAAREANAHEF--ISSFPDgysTVVGe 589
Cdd:COG1134 84 EVNG------RVSALLELGAGF---HPEL---TGRENIYLNGrlLGLSRKEI--DEKFDEIVEFaeLGDFID---QPVK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 590 rgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANG 667
Cdd:COG1134 146 ---TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKG 222
|
250 260
....*....|....*....|....*
gi 27753995 668 QVCEAGTHEELLKkggLYSELIRRQ 692
Cdd:COG1134 223 RLVMDGDPEEVIA---AYEALLAGR 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
458-679 |
5.39e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 458 NVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDP-----EAGSVTLDGHDLRTLNPSWLRGQV 532
Cdd:PRK14271 26 NLTLGFA---GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPVLFATTIMENI----RFGKLDASDEevYTAAREANAHEFisSFPDGYSTVVGERGTTLSGGQKQRLAIARAL 608
Cdd:PRK14271 103 VGMLFQRPNPFPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 609 IKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
473-678 |
5.77e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 473 KDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--QVIGFISQEPV-------LF 543
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrSDIQMIFQDPLaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 544 ATTIMENIRFGKLDASDEEVYTAAREANA-------------HEFissfpdgystvvgergttlSGGQKQRLAIARALIK 610
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinrypHEF-------------------SGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 611 QPTVLILDEATSALDAESE-RVVQ--EALDRaSAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQaQVVNllQQLQR-EMGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
460-679 |
1.81e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 460 TFSYpcRPGF------NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlRGQVI 533
Cdd:PRK15112 13 TFRY--RTGWfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPvlfATTIMENIRFGK-LDAS---DEEVYTAAREANAHEFISS---FPDGystvVGERGTTLSGGQKQRLAIAR 606
Cdd:PRK15112 90 RMIFQDP---STSLNPRQRISQiLDFPlrlNTDLEPEQREKQIIETLRQvglLPDH----ASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 607 ALIKQPTVLILDEATSALD-AESERVVQEALD-RASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK15112 163 ALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVL 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
471-669 |
2.22e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGQVIGFISQEPVL---FATTI 547
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAKYIGRVFQDPMMgtaPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 548 MEN------------IRFGKldasdeevyTAAREANAHEFISSFPDGY----STVVGergtTLSGGQKQRLAIARALIKQ 611
Cdd:COG1101 100 EENlalayrrgkrrgLRRGL---------TKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 612 PTVLILDEATSALD---AE-----SERVVQEaldrasAGRTVLVIAHRLstvRAAHS----IIVMANGQV 669
Cdd:COG1101 167 PKLLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNM---EQALDygnrLIMMHEGRI 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
447-680 |
2.65e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 447 NKDIRGSITFQ--NVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLN 524
Cdd:PRK10575 3 EYTNHSDTTFAlrNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 525 PSWLRGQVIGFISQEPVLFATTIMENI------------RFGKLDAS--DEEVYTAAREANAHEFISSfpdgystvvger 590
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAADREkvEEAISLVGLKPLAHRLVDS------------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 591 gttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIA--HRLS-TVRAAHSIIVMANG 667
Cdd:PRK10575 148 ---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGG 224
|
250
....*....|...
gi 27753995 668 QVCEAGTHEELLK 680
Cdd:PRK10575 225 EMIAQGTPAELMR 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
464-691 |
2.88e-16 |
|
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: 83.52 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 464 PC-RPGFNVLkdfTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVIGFISQEPVL 542
Cdd:TIGR01257 940 PSgRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVR-QSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 543 FA-TTIMENIRF-GKLDASDEEVYTAAREANAHEfissfpDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:TIGR01257 1015 FHhLTVAEHILFyAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 621 TSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTheELLKKG----GLYSELIRR 691
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT--PLFLKNcfgtGFYLTLVRK 1162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
454-667 |
3.52e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVI 533
Cdd:PRK09700 6 ISMAGIGKSFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQE-PVLFATTIMENIRFGKL--------DASDeevYTAAREANAhefISSFPDGYSTVVGERGTTLSGGQKQRLAI 604
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGRHltkkvcgvNIID---WREMRVRAA---MMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 605 ARALIKQPTVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANG 667
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
469-691 |
6.86e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 469 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGQVIGFISQEPVLFA-TTI 547
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY-ASKEVARRIGLLAQNATTPGdITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 548 MENIR---------FGKLDASDEEVYTAAREANahefissfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 618
Cdd:PRK10253 99 QELVArgryphqplFTRWRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 619 EATSALDAESERVVQEALDRAS--AGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKkgglySELIRR 691
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-----AELIER 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
454-669 |
1.07e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.84 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRG 530
Cdd:PRK10908 2 IRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QvIGFISQEP-VLFATTIMENIRFGKL--DASDEE----VYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLA 603
Cdd:PRK10908 80 Q-IGMIFQDHhLLMDRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 604 IARALIKQPTVLILDEATSALD-AESERVVQ--EALDRasAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 669
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDdALSEGILRlfEEFNR--VGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
202-344 |
1.60e-15 |
|
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: 78.09 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 202 GERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLA 281
Cdd:cd18558 87 AGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVIL 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 282 VVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELE 344
Cdd:cd18558 167 AISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLE 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
454-681 |
1.72e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSY-PCRP-GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL------DGHDLRTLNP 525
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 526 swLRGQV-IGFISQEPVLFATTIMENIRFG--KLDASDEEVYTAAreANAHEFIssfpdGYSTVVGERGT-TLSGGQKQR 601
Cdd:PRK13643 82 --VRKKVgVVFQFPESQLFEETVLKDVAFGpqNFGIPKEKAEKIA--AEKLEMV-----GLADEFWEKSPfELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 602 LAIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
..
gi 27753995 680 KK 681
Cdd:PRK13643 233 QE 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
466-655 |
1.98e-15 |
|
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: 75.38 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLERFYDPEaGSVTLDGHDLRTlNPSWLRGQVIgFISQEPV 541
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKE-FAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 542 LFAT-TIMENIRFgkldasdeevytaAREANAHEFIssfpdgystvvgeRGttLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:cd03233 94 HFPTlTVRETLDF-------------ALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190
....*....|....*....|....*....|....*
gi 27753995 621 TSALDAEServvqeALDRASAGRTvlvIAHRLSTV 655
Cdd:cd03233 146 TRGLDSST------ALEILKCIRT---MADVLKTT 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
467-652 |
2.92e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 467 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT- 545
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENI--------RFGKLDASdeEVYTAAREANAHEFISSFPDgysTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 617
Cdd:PRK10762 95 TIAENIflgrefvnRFGRIDWK--KMYAEADKLLARLNLRFSSD---KLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 27753995 618 DEATSAL-DAESE---RVVQEALDRasaGRTVLVIAHRL 652
Cdd:PRK10762 166 DEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRL 201
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
454-676 |
3.54e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDgHDLRtlnpswlrgqvI 533
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-GKLR-----------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENIRFGKL--DASDEEVYTAAREANAHEFISsFPdgystvvgerGTTLSGGQKQRLAIARALIKQ 611
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQAGHLID-AP----------MQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 612 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHE 676
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
457-673 |
3.78e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPGFnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDG-----HDLRTLNPSWLRGQ 531
Cdd:PRK11701 10 RGLTKLYGPRKGC---RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 V---IGFISQEPvlfattiMENIRFG---------KLDASDEEVYTAAREANAH-----EFISSFPDgystvvgERGTTL 594
Cdd:PRK11701 87 LrteWGFVHQHP-------RDGLRMQvsaggnigeRLMAVGARHYGDIRATAGDwlervEIDAARID-------DLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 595 SGGQKQRLAIARALIKQPTVLILDEATSALDAEservVQ-EALD--R---ASAGRTVLVIAHRLSTVR-AAHSIIVMANG 667
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDllRglvRELGLAVVIVTHDLAVARlLAHRLLVMKQG 228
|
....*.
gi 27753995 668 QVCEAG 673
Cdd:PRK11701 229 RVVESG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
471-673 |
4.36e-15 |
|
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: 75.00 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLERFYDPEaGSVTLDGHDLRtlnpswlRGQV---IGFISQEPVLF 543
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGTTS-GQILFNGQPRK-------PDQFqkcVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 544 AT-TIMENIRFGKLDASDEEVYTAAREANAhEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 623 ALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRAAHSIIVMANGQVCEAG 673
Cdd:cd03234 173 GLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
454-680 |
4.88e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.66 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSY-PCRP-GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL---DGHDL-RTLNPSW 527
Cdd:PRK13651 3 IKVKNIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 528 --------------------LRGQViGFISQ--EPVLFATTIMENIRFGKLD--ASDEEVYTAAREanahefissfpdgY 583
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRV-GVVFQfaEYQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAK-------------Y 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 584 STVVG------ERGT-TLSGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQEALD----RASAGRTVLVIAHRL 652
Cdd:PRK13651 149 IELVGldesylQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEifdnLNKQGKTIILVTHDL 225
|
250 260
....*....|....*....|....*....
gi 27753995 653 STV-RAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PRK13651 226 DNVlEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
466-649 |
6.00e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.93 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlrGQVIGFISQEPVLFAT 545
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 -TIMENIRFGK--LDASDEEVYTAAREANAHEFiSSFPDGYstvvgergttLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:TIGR01189 88 lSALENLHFWAaiHGGAQRTIEDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*..
gi 27753995 623 ALDAESERVVQEALdRASAGRTVLVIA 649
Cdd:TIGR01189 157 ALDKAGVALLAGLL-RAHLARGGIVLL 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
469-651 |
6.11e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 469 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFY--DPEAGSVTLDGHDlrtlnpswlrgqvigfISQEpvlfaTT 546
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------FGRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 IMENIrfGKLDASDE--EVYTAAREANAHEFISSFPdgystvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATSAL 624
Cdd:COG2401 102 LIDAI--GRKGDFKDavELLNAVGLSDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*....
gi 27753995 625 DAESERVVQEALDRAS--AGRTVLVIAHR 651
Cdd:COG2401 168 DRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
471-680 |
6.36e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS--WLRGqvIGFIS----QEPVLFA 544
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaIRAG--IAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENI---------RFGKLDASDEEvytaareANAHEFISSF---PDGYSTVVGergtTLSGGQKQRLAIARALIKQP 612
Cdd:COG1129 345 LSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 613 TVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVIahrlST-----VRAAHSIIVMANGQVC-----EAGTHEEL 678
Cdd:COG1129 414 KVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAI 486
|
..
gi 27753995 679 LK 680
Cdd:COG1129 487 MA 488
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
467-668 |
1.02e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 467 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEA---GSVTLDGHDLR--TLNPSWLRGQVIgfISQEPV 541
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQasNIRDTERAGIAI--IHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 542 LFAT-TIMENI-------RFGKLDasDEEVYTAAREANAHEFISSFPDgysTVVGErgttLSGGQKQRLAIARALIKQPT 613
Cdd:PRK13549 93 LVKElSVLENIflgneitPGGIMD--YDAMYLRAQKLLAQLKLDINPA---TPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 614 VLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 668
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIrDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
453-678 |
1.08e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYpcrpGFNVL-KDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGq 531
Cdd:PRK11000 3 SVTLRNVTKAY----GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 vIGFISQEPVLFA-TTIMENIRFG-KLdASDEEVYTAAREANAHEFISsfpdgYSTVVGERGTTLSGGQKQRLAIARALI 609
Cdd:PRK11000 77 -VGMVFQSYALYPhLSVAENMSFGlKL-AGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 610 KQPTVLILDEATSALDAeSERV---VQEALDRASAGRTVLVIAHrlSTVRA---AHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
466-680 |
1.30e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.59 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL-------------RGQV 532
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIelseqsaaqmrhvRGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 533 IGFISQEPV-----LFAT--TIMENIRFGKlDASDEEVYTAA-------REANAHEFISSFPDgystvvgergtTLSGGQ 598
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQ-GASREEAMVEAkrmldqvRIPEAQTILSRYPH-----------QLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAESE-------RVVQEALDRAsagrtVLVIAHRLSTV-RAAHSIIVMANGQVC 670
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVaEIADRVLVMYQGEAV 248
|
250
....*....|
gi 27753995 671 EAGTHEELLK 680
Cdd:PRK10261 249 ETGSVEQIFH 258
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
454-679 |
2.09e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLerFYDPEA--GSVTLDGHDLRTLNPSWLRGQ 531
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQEPVLFA-TTIMENIRFGKLDASDEEVYTaaREANAHEFissFPDGYSTVVgERGTTLSGGQKQRLAIARALIK 610
Cdd:PRK11614 81 AVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 611 QPTVLILDEATSALdaeSERVVQEALD-----RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK11614 155 QPRLLLLDEPSLGL---APIIIQQIFDtieqlREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-679 |
2.49e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPSWLR---- 529
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARharq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 --GQVIGFISQEPVLfatTIMENIR-FGK---LDASDeevyTAAREANAHEFiSSFPDGYSTVVGErgttLSGGQKQRLA 603
Cdd:PRK13537 81 rvGVVPQFDNLDPDF---TVRENLLvFGRyfgLSAAA----ARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 604 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-679 |
2.85e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVA-SLLERFYDPEA----GSVTLDGHDL-----RTLNPswLRGQVIGFISQEP 540
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPVvypsGDIRFHGESLlhaseQTLRG--VRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 541 VlfattimenIRFGKLDASDEEVYTA-------AREANAHEFISSFPDgystvVGERGTT---------LSGGQKQRLAI 604
Cdd:PRK15134 102 M---------VSLNPLHTLEKQLYEVlslhrgmRREAARGEILNCLDR-----VGIRQAAkrltdyphqLSGGERQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 605 ARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
456-678 |
3.25e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 456 FQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGF 535
Cdd:PRK11288 7 FDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 536 ISQE----PVLfatTIMENIRFGKLDAS-----DEEVYTAAREANAHEFISSFPDgysTVVGErgttLSGGQKQRLAIAR 606
Cdd:PRK11288 84 IYQElhlvPEM---TVAENLYLGQLPHKggivnRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 607 ALIKQPTVLILDEATSALDA-ESE---RVVQEALDRasaGRTVLVIAHRLSTV-RAAHSIIVMANGQvcEAGTHEEL 678
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGR--YVATFDDM 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
454-681 |
3.53e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.61 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF--YDPEAGSVTLDghdlRTLNPSWLRGQ 531
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH----VALCEKCGYVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 VIGFISQE-PVLFATTIMENIRFGKLDasdEEVYTAAREANAHEF----------------ISSFPD-GYS--------- 584
Cdd:TIGR03269 74 RPSKVGEPcPVCGGTLEPEEVDFWNLS---DKLRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEgkeavgrav 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 585 -----TVVGERGT----TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsagrtvlVIAHRLSTV 655
Cdd:TIGR03269 151 dliemVQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA-------VKASGISMV 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 27753995 656 RAAH----------SIIVMANGQVCEAGTHEELLKK 681
Cdd:TIGR03269 224 LTSHwpeviedlsdKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
455-650 |
5.24e-14 |
|
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: 75.36 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 455 TFQNVTFSYPcrPGFNVLKDFTLK-LPSGKIvALVGQSGGGKTTVASL---LERFYDPEAgsvtldghdlrtlnpsWLR- 529
Cdd:TIGR03719 6 TMNRVSKVVP--PKKEILKDISLSfFPGAKI-GVLGLNGAGKSTLLRImagVDKDFNGEA----------------RPQp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 530 GQVIGFISQEPVLFAT-TIMENIRFG---KLDASDE--EVYTAARE---------------------ANAHEFISSF--- 579
Cdd:TIGR03719 67 GIKVGYLPQEPQLDPTkTVRENVEEGvaeIKDALDRfnEISAKYAEpdadfdklaaeqaelqeiidaADAWDLDSQLeia 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 580 ------PDGYSTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIA 649
Cdd:TIGR03719 147 mdalrcPPWDADV-----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVT 215
|
.
gi 27753995 650 H 650
Cdd:TIGR03719 216 H 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
453-661 |
5.64e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.71 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPSWLRG-- 530
Cdd:PRK13536 41 AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLar 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEPVL-FATTIMENI----RFGKLDASD-EEVYTAAREANAHEfissfpdgysTVVGERGTTLSGGQKQRLAI 604
Cdd:PRK13536 114 ARIGVVPQFDNLdLEFTVRENLlvfgRYFGMSTREiEAVIPSLLEFARLE----------SKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 605 ARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAH----------RLSTVRAAHSI 661
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaerlcdRLCVLEAGRKI 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
470-647 |
6.42e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 470 NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP---SWLRGQVIGFISQEPVLFAT- 545
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKHVGFVFQSFMLIPTl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIRFGKL--DASDEEVYTAAREANAHefissfpdgysTVVGER----GTTLSGGQKQRLAIARALIKQPTVLILDE 619
Cdd:PRK10584 104 NALENVELPALlrGESSRQSRNGAKALLEQ-----------LGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|.
gi 27753995 620 ATSALDAES-ERVVQE--ALDRASAGRTVLV 647
Cdd:PRK10584 173 PTGNLDRQTgDKIADLlfSLNREHGTTLILV 203
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
130-397 |
6.73e-14 |
|
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: 72.90 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 130 LGAAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHMGSFVsesrklsVQLLLLYGVQGLLTFGYLVLLSHIGERMAMD 208
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIdHFITPGTLDGLTGFI-------LLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 209 MRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALM 288
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 289 GVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQ---AELESCCCKAEELGrgiALF----Q 361
Cdd:cd18540 157 VVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKeltEEMRRASVRAARLS---ALFlpivL 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 27753995 362 GLSNIAfncmVLGTLFIGGSLVAGQQLKGGDLMSFL 397
Cdd:cd18540 234 FLGSIA----TALVLWYGGILVLAGAITIGTLVAFI 265
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
474-677 |
7.34e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 474 DFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLNPS----WL----RGqvIGFISQEPVLFA- 544
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAekgiCLppekRR--IGYVFQDARLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENIRFGKLDASDEE----VYTAAREAnaheFISSFPdgystvvgergTTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:PRK11144 91 YKVRGNLRYGMAKSMVAQfdkiVALLGIEP----LLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 621 TSALDAESERVVQEALDRASagRTV----LVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEE 677
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLA--REInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
452-667 |
9.07e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 70.35 E-value: 9.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQNVTFSYPCRPGF-NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLL-ERfydPEAGSVT----LDGhdlRTLNP 525
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVITgeilING---RPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 526 SWLRgqVIGFISQEPVLFAT-TIMENIRFgkldasdeevytaarEANAhefissfpdgystvvgeRGttLSGGQKQRLAI 604
Cdd:cd03232 76 NFQR--STGYVEQQDVHSPNlTVREALRF---------------SALL-----------------RG--LSVEQRKRLTI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 605 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAH--SIIVMANG 667
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASIFEKfdRLLLLKRG 185
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
133-393 |
1.08e-13 |
|
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: 72.15 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVeivakytrDHMGSFVSESRKLSVQLLLLYGVQGLLT--FGYL--VLLSHIGERMAMD 208
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAV--------DALSAPASALLAVPLLLLLAYGLARILSslFNELrdALFARVSQRAVRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 209 MRKALFSSLLRQDIAFFDAKKTGQLVSrlttdvqefkssfklVISQGLRSCTQVIGSLV------------SLSMLSPRL 276
Cdd:cd18582 73 LALRVFRHLHSLSLRFHLSRKTGALSR---------------AIERGTRGIEFLLRFLLfnilptilelllVCGILWYLY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 277 TLMLAVVTPALMGV---GTLMGSGLR-KLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEE 352
Cdd:cd18582 138 GWSYALITLVTVALyvaFTIKVTEWRtKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALA----KYEK 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27753995 353 LG----RGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDL 393
Cdd:cd18582 214 AAvksqTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDF 258
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
473-678 |
1.79e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 473 KDFTLKLPSGKIVALVGQSGGGKT-TVASLLERFydPE-----AGSVTLDGhdlRTLNPSWLRGQVIGFISQEP------ 540
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PAgvrqtAGRVLLDG---KPVAPCALRGRKIATIMQNPrsafnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 541 -VLFATTIMENIR-FGKLdaSDEEVYTAAREA----NAHEFISSFPdgystvvgergTTLSGGQKQRLAIARALIKQPTV 614
Cdd:PRK10418 95 lHTMHTHARETCLaLGKP--ADDATLTAALEAvgleNAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 615 LILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 678
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
468-668 |
2.14e-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: 73.32 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEA---GSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFA 544
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 T-TIMENIRFGK------LDASDEEVYTAAREANAHEFISSFPDgySTVVGERGttlsGGQKQRLAIARALIKQPTVLIL 617
Cdd:TIGR02633 92 ElSVAENIFLGNeitlpgGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27753995 618 DEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 668
Cdd:TIGR02633 166 DEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
180-671 |
2.84e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 180 LLLLYGVqgllTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSF----KLVisQG 255
Cdd:PRK10522 58 LLLLMAV----TLGSQLALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFvrlpELV--QG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LrscTQVIGSLVSLSMLSPRltlMLAVvTPALMGVgTLMGSGLrkLSRQCQEQIARATGVADEALGNVRTVrafaMEKRE 335
Cdd:PRK10522 132 I---ILTLGSAAYLAWLSPK---MLLV-TAIWMAV-TIWGGFV--LVARVYKHMATLRETEDKLYNDYQTV----LEGRK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 336 E-----ER----YQAELEScccKAEELGRGIAL---FQGLSNIAFNCMVLGTlfIGgslvagqqlkggdlMSFLVA---- 399
Cdd:PRK10522 198 EltlnrERaeyvFENEYEP---DAQEYRHHIIRadtFHLSAVNWSNIMMLGA--IG--------------LVFYMAnslg 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 400 -SQTVQRSMASLSVLF-----GQVVRGLSA--GARV-FEYMALSPVIPLTGGYCIPN--KDIRgSITFQNVTFSYPcRPG 468
Cdd:PRK10522 259 wADTNVAATYSLTLLFlrtplLSAVGALPTllSAQVaFNKLNKLALAPYKAEFPRPQafPDWQ-TLELRNVTFAYQ-DNG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 469 FNVlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGqvigfisqepvLFATTIM 548
Cdd:PRK10522 337 FSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK-----------LFSAVFT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 549 ENIRFGKL-----DASDEEVYTA--AREANAHEFissfpdgysTVVGERGTT--LSGGQKQRLAIARALIKQPTVLILDE 619
Cdd:PRK10522 405 DFHLFDQLlgpegKPANPALVEKwlERLKMAHKL---------ELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDE 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 620 ATSALDAESERVV-QEALDRASA-GRTVLVIAHRLSTVRAAHSIIVMANGQVCE 671
Cdd:PRK10522 476 WAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
471-694 |
3.38e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL----RTLNPswLRGQViGFISQEP--VLFA 544
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLA--LRQQV-ATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENIRFG--KLDASDEEVytaAREAnahefissfpDGYSTVVGERG------TTLSGGQKQRLAIARALIKQPTVLI 616
Cdd:PRK13638 93 TDIDSDIAFSlrNLGVPEAEI---TRRV----------DEALTLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 617 LDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGglysELIRRQTL 694
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT----EAMEQAGL 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
467-671 |
5.61e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 467 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEA---GSVTLDGH--DLRTLNPSWLRGQVIgfISQE-- 539
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEvcRFKDIRDSEALGIVI--IHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 540 --PVLfatTIMENI-------RFGKLDAsdEEVYTAAREANAHEFISSFPDgysTVVGERGTtlsgGQKQRLAIARALIK 610
Cdd:NF040905 89 liPYL---SIAENIflgneraKRGVIDW--NETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 611 QPTVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCE 671
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
482-680 |
7.59e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 482 GKIVALVGQSGGGKTtVASL----LERFydP---EAGSVTLDGHDLRTLNPSWLR---GQVIGFISQEPVL-------FA 544
Cdd:PRK11022 33 GEVVGIVGESGSGKS-VSSLaimgLIDY--PgrvMAEKLEFNGQDLQRISEKERRnlvGAEVAMIFQDPMTslnpcytVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENIRFGKLDASdeevytAAREANAHEFIS--SFPDGYSTVvGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:PRK11022 110 FQIMEAIKVHQGGNK------KTRRQRAIDLLNqvGIPDPASRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 623 ALDAESE-RVVQEALDRASAGRTVLV-IAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLK 680
Cdd:PRK11022 183 ALDVTIQaQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
470-674 |
8.13e-13 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 69.18 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 470 NVLKDFTLKLPSGKIVALVGQSGGGKTT------VASLLERFYdpeAGSVTLDGHD----LRTLnpswlrGQVIgFISQE 539
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSlindtlYPALARRLH---LKKEQPGNHDriegLEHI------DKVI-VIDQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 540 PV--------LFATTIMENIR--F-------------------GK-----LDASDEEvytaareanAHEFISSFPD---- 581
Cdd:cd03271 79 PIgrtprsnpATYTGVFDEIRelFcevckgkrynretlevrykGKsiadvLDMTVEE---------ALEFFENIPKiark 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 582 ---------GYSTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVI 648
Cdd:cd03271 150 lqtlcdvglGYIKL-GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVI 228
|
250 260 270
....*....|....*....|....*....|..
gi 27753995 649 AHRLSTVRAAHSIIVM------ANGQVCEAGT 674
Cdd:cd03271 229 EHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
471-650 |
1.62e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLErfydPEAGSVTLDGHDLRTLNPswlrGQVIGFISQ----EPVL 542
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLP----PAAGTIKLDGGDIDDPDV----AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 543 fatTIMENIRFGKldasdeEVYtAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:PRK13539 89 ---TVAENLEFWA------AFL-GGEELDIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*....
gi 27753995 623 ALDAESERVVQEAL-DRASAGRTVLVIAH 650
Cdd:PRK13539 157 ALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
471-669 |
3.03e-12 |
|
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: 66.97 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR--GQVIGFISQE----PVLFA 544
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRriGVVFGQKTQLwwdlPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 TTIMENI------RFGK--------LDASdEEVYTAAREanahefissfpdgystvvgergttLSGGQKQRLAIARALIK 610
Cdd:cd03267 116 FYLLAAIydlppaRFKKrldelselLDLE-ELLDTPVRQ------------------------LSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 611 QPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
176-404 |
9.41e-12 |
|
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: 66.37 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRlttdVQEFKSSFKLVISQG 255
Cdd:cd18588 44 LAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELESIRQFLTGSA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LRSCTQVIGSLVSLSML---SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAME 332
Cdd:cd18588 120 LTLVLDLVFSVVFLAVMfyySPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 333 KREEERYQAELesccckAEELGRGIALfQGLSNIAFN-------CMVLGTLFIGGSLVAGQQLKGGDLMSF-LVASQTVQ 404
Cdd:cd18588 200 PQFQRRWEELL------ARYVKASFKT-ANLSNLASQivqliqkLTTLAILWFGAYLVMDGELTIGQLIAFnMLAGQVSQ 272
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
127-411 |
1.22e-11 |
|
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: 66.08 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 127 LLALGAAIVLALGAaLVNvqiPLLLGQLVEIVAkyTRDHMGSFVSesrkLSVQLLLLYGVQGLLTFGYLVLLSHIGERMA 206
Cdd:cd18782 5 IEVLALSFVVQLLG-LAN---PLLFQVIIDKVL--VQQDLATLYV----IGVVMLVAALLEAVLTALRTYLFTDTANRID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 207 MDMRKALFSSLLRQDIAFFDAKKTGQLVSRL--TTDVQEFkssfklVISQGLRSCTQVIGSLVSLSML---SPRLTLMLA 281
Cdd:cd18782 75 LELGGTIIDHLLRLPLGFFDKRPVGELSTRIseLDTIRGF------LTGTALTTLLDVLFSVIYIAVLfsySPLLTLVVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 282 VVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQ 361
Cdd:cd18782 149 ATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27753995 362 GLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLS 411
Cdd:cd18782 229 SLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLS 278
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
454-654 |
1.89e-11 |
|
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: 67.27 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdGHDLRtlnpswlrgqvI 533
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQ--EPVLFATTIMENIRFGkldasDEEVYTAAREANAHEFISSF----PDgYSTVVGErgttLSGGQKQRLAIARA 607
Cdd:TIGR03719 388 AYVDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPSRAYVGRFnfkgSD-QQKKVGQ----LSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27753995 608 LIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH------RLST 654
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALL-NFAG-CAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
176-396 |
2.26e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents 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: 350010 [Multi-domain] Cd Length: 294 Bit Score: 65.30 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLttdvQEFKSSFKLVISQG 255
Cdd:cd18566 44 LVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL----NSLEQIREFLTGQA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LRSCTQ---VIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAME 332
Cdd:cd18566 120 LLALLDlpfVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAME 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 333 KREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSF 396
Cdd:cd18566 200 PQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
449-678 |
3.50e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 449 DIRGsitfqnVTFSYPCRPGFNvlkDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 528
Cdd:PRK11831 9 DMRG------VSFTRGNRCIFD---NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RG--QVIGFISQEPVLFA-TTIMENIRFgkldasdeevytAAREanaHefiSSFPDG--YSTV------VGERG------ 591
Cdd:PRK11831 80 YTvrKRMSMLFQSGALFTdMNVFDNVAY------------PLRE---H---TQLPAPllHSTVmmkleaVGLRGaaklmp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 592 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVR--AAHSIIVmANG 667
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLsiADHAYIV-ADK 220
|
250
....*....|.
gi 27753995 668 QVCEAGTHEEL 678
Cdd:PRK11831 221 KIVAHGSAQAL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
455-650 |
3.91e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 455 TFQNVTFSYPcrPGFNVLKDFTLK-LPSGKIvALVGQSGGGKTTVASL---LERFYDPEAgsvtldghdlrTLNPswlrG 530
Cdd:PRK11819 8 TMNRVSKVVP--PKKQILKDISLSfFPGAKI-GVLGLNGAGKSTLLRImagVDKEFEGEA-----------RPAP----G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEPVLFAT-TIMENIRFG---KLDASDE--EVY------------TAAREA---------NAHEFISSF---- 579
Cdd:PRK11819 70 IKVGYLPQEPQLDPEkTVRENVEEGvaeVKAALDRfnEIYaayaepdadfdaLAAEQGelqeiidaaDAWDLDSQLeiam 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 580 -----PDGYSTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 650
Cdd:PRK11819 150 dalrcPPWDAKV-----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD-----YPG-TVVAVTH 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
448-713 |
3.94e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 448 KDIRgsitfqnVTFSYPcrPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPE---AGSVTLDGHDLRTL 523
Cdd:PRK09473 16 KDLR-------VTFSTP--DGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 524 NPSWL---RGQVIGFISQEPVL-----------FATTIMENIRFGKLDASDEEV--YTAAREANAHEFISSFPDGYStvv 587
Cdd:PRK09473 87 PEKELnklRAEQISMIFQDPMTslnpymrvgeqLMEVLMLHKGMSKAEAFEESVrmLDAVKMPEARKRMKMYPHEFS--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 588 gergttlsGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVM 664
Cdd:PRK09473 164 --------GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGiCDKVLVM 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 665 ANGQVCEAGTHEELLKKG------GLYSELIRRQTLDASLTSTP--PAEKPEDPKSC 713
Cdd:PRK09473 236 YAGRTMEYGNARDVFYQPshpysiGLLNAVPRLDAEGESLLTIPgnPPNLLRLPKGC 292
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
150-418 |
6.22e-11 |
|
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: 64.07 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 150 LLGQLVEIVAKYTRDH--MGSFVSESRKLSVQLLLLYGVQGLLTF--GYLVLlsHIGERMAMDMRKALFSSLLRQDIAFF 225
Cdd:cd18555 16 LLTLLIPILTQYVIDNviVPGNLNLLNVLGIGILILFLLYGLFSFlrGYIII--KLQTKLDKSLMSDFFEHLLKLPYSFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 226 DAKKTGQLVSRL--TTDVQEFKSSfkLVISqGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTpALMGVGTLMGSG-LRKLS 302
Cdd:cd18555 94 ENRSSGDLLFRAnsNVYIRQILSN--QVIS-LIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLLLLTRKkIKKLN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 303 RQCQEQIARATGVADEALGNVRTVRAFAME----KREEERYQAELESccckAEELGRGIALFQGLSNIAFNCMVLGTLFI 378
Cdd:cd18555 170 QEEIVAQTKVQSYLTETLYGIETIKSLGSEkniyKKWENLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLILWI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 27753995 379 GGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVV 418
Cdd:cd18555 246 GAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
180-413 |
8.75e-11 |
|
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: 63.35 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 180 LLLLYGVQGLLTFGYLV---------LLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRL--TTDVQEFKSsf 248
Cdd:cd18568 39 SLLNLILIGLLIVGIFQillsavrqyLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFqeNQKIRRFLT-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 249 KLVISQGLRSCTQVIgSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRA 328
Cdd:cd18568 117 RSALTTILDLLMVFI-YLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 329 FAME----KREEERYQAELESccckaeELgRGIALFQGLSNIAFNCMVLGT---LFIGGSLVAGQQLKGGDLMSFLVASQ 401
Cdd:cd18568 196 LAAErpirWRWENKFAKALNT------RF-RGQKLSIVLQLISSLINHLGTiavLWYGAYLVISGQLTIGQLVAFNMLFG 268
|
250
....*....|..
gi 27753995 402 TVQRSMASLSVL 413
Cdd:cd18568 269 SVINPLLALVGL 280
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
469-655 |
9.95e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 469 FNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGQVIgFISQEPVLFA 544
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVV-YNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 T-TIMENIRFG--------KLDASDEEVYtAAREANAHEFISSFPDGYSTVVGE---RGttLSGGQKQRLAIARALIKQP 612
Cdd:TIGR00956 152 HlTVGETLDFAarcktpqnRPDGVSREEY-AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27753995 613 TVLILDEATSALDAEServvqeALDRASAGRTVLVIAHRLSTV 655
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
475-684 |
1.13e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 475 FTLKLPSGKIVALVGQSGGGKTT----VASLLerfydPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFATTImen 550
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 551 irFGKLDAS-DEEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQR-------LAIARALIKQPTVLILDEATS 622
Cdd:PRK03695 87 --FQYLTLHqPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 623 ALDaeserVVQE-ALDR-----ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKKGGL 684
Cdd:PRK03695 163 SLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
452-650 |
1.27e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITF--QNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVT---------LDGHdl 520
Cdd:PRK11147 316 GKIVFemENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtklevayFDQH-- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 521 R-TLNPSwlrgqvigfisqepvlfaTTIMENIRFGKldasdEEVYTAAREANAHEFISSF---PDGYSTVVgergTTLSG 596
Cdd:PRK11147 391 RaELDPE------------------KTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 597 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAH 650
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
556-678 |
1.46e-10 |
|
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: 64.65 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 556 LDASDEEvytaareanAHEFISSFPD-------------GYSTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDE 619
Cdd:TIGR00630 789 LDMTVEE---------AYEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDE 858
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 620 ATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVM------ANGQVCEAGTHEEL 678
Cdd:TIGR00630 859 PTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
134-427 |
2.07e-10 |
|
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: 62.44 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 134 IVLALGAALVNVQIPLLLgqlvEIVAKYTRDH--MGSFVSESRKLSvqllLLYGVQGLLTFGYLVL----------LSH- 200
Cdd:cd18554 1 IIITIVIGLVRFGIPLLL----PLILKYIVDDviQGSSLTLDEKVY----KLFTIIGIMFFIFLILrppveyyrqyFAQw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 201 IGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLML 280
Cdd:cd18554 73 IANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 281 AVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALF 360
Cdd:cd18554 153 LVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 361 QGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 427
Cdd:cd18554 233 FSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-679 |
2.82e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 475 FTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEP----VLFATTIMEN 550
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRkrdgLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 551 I----------RFGKLDASDEevytaaREAnAHEFISSF----PdGYSTVVGErgttLSGGQKQRLAIARALIKQPTVLI 616
Cdd:PRK10762 351 MsltalryfsrAGGSLKHADE------QQA-VSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 617 LDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRA-AHSIIVMANGQVC-----EAGTHEELL 679
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRISgeftrEQATQEKLM 488
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
482-668 |
3.06e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 482 GKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgqvIGFISQEPVLFA-TTIMENIRFGKLDASD 560
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR---TGFVTQDDILYPhLTVRETLVFCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 561 EEVYTAAREANAHEFISSF--PDGYSTVVGE---RGttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESE-RVVQE 634
Cdd:PLN03211 171 KSLTKQEKILVAESVISELglTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLT 248
|
170 180 190
....*....|....*....|....*....|....*.
gi 27753995 635 ALDRASAGRTVLVIAHRLST--VRAAHSIIVMANGQ 668
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
466-680 |
3.54e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTV-ASLLERFYDPEA-------GSVTLDGHDLRTLNPSWL-RGQVIGFI 536
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLlKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 537 SQEPVlFATTIMENI---------RFGKLDASDEEVYTAAREANahefissfpdGYSTVVGERGTTLSGGQKQRLAIARA 607
Cdd:PRK13547 91 AAQPA-FAFSAREIVllgrypharRAGALTHRDGEIAWQALALA----------GATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 608 L---------IKQPTVLILDEATSALD-AESERVVQEALDRASAGRT-VLVIAHRLS-TVRAAHSIIVMANGQVCEAGTH 675
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
....*
gi 27753995 676 EELLK 680
Cdd:PRK13547 240 ADVLT 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
472-650 |
6.22e-10 |
|
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: 62.49 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKI-----VALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswLRgqvigfISQEPvlfatt 546
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----------LK------ISYKP------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 imeniRFGKLDaSDEEVYTAAREANAHEFISSFpdgYSTVVGER----------GTTLSGGQKQRLAIARALIKQPTVLI 616
Cdd:COG1245 408 -----QYISPD-YDGTVEEFLRSANTDDFGSSY---YKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 27753995 617 LDEATSALDAEsERV-VQEALDR--ASAGRTVLVIAH 650
Cdd:COG1245 479 LDEPSAHLDVE-QRLaVAKAIRRfaENRGKTAMVVDH 514
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
481-662 |
6.72e-10 |
|
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: 58.15 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 481 SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVtldghdlRTLNPSWLRGQVIGFISQEPVlfattimenirfgkldasd 560
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------IYIDGEDILEEVLDQLLLIIV------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 561 eevytaareanahefissfpdgystvvGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--- 637
Cdd:smart00382 55 ---------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180
....*....|....*....|....*....
gi 27753995 638 ----RASAGRTVLVIAHRLSTVRAAHSII 662
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
453-678 |
9.65e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.01 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 453 SITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLlERFydpEAGSVTLDGHDLRTLNPSwL 528
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERI---TSGEIWIGGRVVNELEPA-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RGqvIGFISQEPVLFA-TTIMENIRFG----KLDAS--DEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQR 601
Cdd:PRK11650 76 RD--IAMVFQNYALYPhMSVRENMAYGlkirGMPKAeiEERVAEAARILELEPLLDRKP-----------RELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 602 LAIARALIKQPTVLILDEATSALDAE---SERVVQEALDRaSAGRTVLVIAHrlSTVRA---AHSIIVMANGQVCEAGTH 675
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKlrvQMRLEIQRLHR-RLKTTSLYVTH--DQVEAmtlADRVVVMNGGVAEQIGTP 219
|
...
gi 27753995 676 EEL 678
Cdd:PRK11650 220 VEV 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
482-655 |
1.12e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 482 GKIVALVGQSGGGKTTvasLLERFYDPEAGSVTLDGHDL---RTLNPSWLRgqVIGFISQEPVLFAT-TIMENIRFGKLD 557
Cdd:TIGR00956 789 GTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLvngRPLDSSFQR--SIGYVQQQDLHLPTsTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 558 ASDEEVYTAAREANAHEFI-----SSFPDGystVVGERGTTLSGGQKQRLAIARALIKQPTVLI-LDEATSALDAESERV 631
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEVIkllemESYADA---VVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 940
|
170 180
....*....|....*....|....*
gi 27753995 632 VQEALDR-ASAGRTVLVIAHRLSTV 655
Cdd:TIGR00956 941 ICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
472-650 |
1.75e-09 |
|
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: 58.96 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSG-----KIVALVGQSGGGKTTVASLLerfydpeAGSVTLDGHDLRTLNPSwlrgqvIGFISQEPVLFATT 546
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT------VSYKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 IMENIRFGKLDASDEEVYTAAREANahefissfPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 626
Cdd:cd03237 77 TVRDLLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*.
gi 27753995 627 ESERVVQEALDR--ASAGRTVLVIAH 650
Cdd:cd03237 149 EQRLMASKVIRRfaENNEKTAFVVEH 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
472-711 |
3.06e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRtlNPSWlRGQV---IGFISQ------EPVL 542
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARH-RRAVcprIAYMPQglgknlYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 543 fatTIMENIRF-GKL---DAsdeevytAAREANAHEF-----ISSFPD---GystvvgergtTLSGGQKQRLAIARALIK 610
Cdd:NF033858 94 ---SVFENLDFfGRLfgqDA-------AERRRRIDELlratgLAPFADrpaG----------KLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 611 QPTVLILDEATSALDAESERVVQEALDRASAGR---TVLViahrlSTV------RAAHsIIVMANGQVCEAGTHEELLKK 681
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLV-----ATAymeeaeRFDW-LVAMDAGRVLATGTPAELLAR 227
|
250 260 270
....*....|....*....|....*....|
gi 27753995 682 GGlyselirRQTLDASLTSTPPAEKPEDPK 711
Cdd:NF033858 228 TG-------ADTLEAAFIALLPEEKRRGHQ 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
454-650 |
3.23e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYpcrpGFNVL-KDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdghdlrtlnpswlrGQ- 531
Cdd:PRK11819 325 IEAENLSKSF----GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--------------GEt 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 532 -VIGFISQ-----EPvlfATTIMENIrfgkldaSD--EEVYTAAREANAHEFISSF----PDgYSTVVGergtTLSGGQK 599
Cdd:PRK11819 387 vKLAYVDQsrdalDP---NKTVWEEI-------SGglDIIKVGNREIPSRAYVGRFnfkgGD-QQKKVG----VLSGGER 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27753995 600 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH 650
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL-EFPG-CAVVISH 500
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
476-679 |
3.36e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 476 TLKLPSGKIVALVGQSGGGKTTVASLL----ERFYDPEAGSVTLDGHDLRTLNPSWLR---GQVIGFISQEP-------V 541
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRklvGHNVSMIFQEPqscldpsE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 542 LFATTIMENI-----------RFGKLDASDEEVYTAAREANAHEFISSFPdgYStvvgergttLSGGQKQRLAIARALIK 610
Cdd:PRK15093 107 RVGRQLMQNIpgwtykgrwwqRFGWRKRRAIELLHRVGIKDHKDAMRSFP--YE---------LTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 611 QPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 679
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
458-657 |
5.67e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 458 NVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlrGQVIGFIS 537
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY--QKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 538 QE----PVLfatTIMENIRFgkldasdeEVYTAAREANAHEFISSFPDGYstVVGERGTTLSGGQKQRLAIARALIKQPT 613
Cdd:PRK13540 81 HRsginPYL---TLRENCLY--------DIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27753995 614 VLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA 657
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQehRAKGGAVLLTSHQDLPLNKA 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
475-652 |
6.38e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 475 FTL-KLPS---GKIVALVGQSGGGKTTVASLLerfydpeAGSVT--LDGHDLrtlNPSWlrgqvigfisqEPVL--FATT 546
Cdd:PRK13409 88 FKLyGLPIpkeGKVTGILGPNGIGKTTAVKIL-------SGELIpnLGDYEE---EPSW-----------DEVLkrFRGT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 IMENIrFGKLdaSDEEVyTAAREANAHEFISSFPDGysTV------VGERG-------------------TTLSGGQKQR 601
Cdd:PRK13409 147 ELQNY-FKKL--YNGEI-KVVHKPQYVDLIPKVFKG--KVrellkkVDERGkldevverlglenildrdiSELSGGELQR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27753995 602 LAIARALIKQPTVLILDEATSALDAEsERV-VQEALDRASAGRTVLVIAHRL 652
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
474-659 |
6.46e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 474 DFTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR-----GQVIGFisqEPVLfatTIM 548
Cdd:PRK13538 21 SFTLN--AGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylGHQPGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 549 ENIRF-GKL-DASDEEVYTAAREAnahefissfpdgystvVGERGT------TLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:PRK13538 93 ENLRFyQRLhGPGDDEALWEALAQ----------------VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27753995 621 TSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAH 659
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVASDK 196
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
129-410 |
1.04e-08 |
|
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: 57.09 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 129 ALGAAIVLALGAALVNVQIPLLLgQLV--EIVAKYTRDHMGSfvsesrkLSVQLLLLYGVQGLLTF--GYLVLlsHIGER 204
Cdd:cd18567 3 ALLQILLLSLALELFALASPLYL-QLVidEVIVSGDRDLLTV-------LAIGFGLLLLLQALLSAlrSWLVL--YLSTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 205 MAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRL--TTDVQEFkssfklvISQGL-RSCTQVIGSLVSLSML---SPRLTL 278
Cdd:cd18567 73 LNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFgsLDEIQQT-------LTTGFvEALLDGLMAILTLVMMflySPKLAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 279 MLAVVTPALMGVGTLMgsgLRKLSRQCQEQI---ARATGVADEALGNVRTVRAFAMEKREEERYQAelesccCKAEELGR 355
Cdd:cd18567 146 IVLAAVALYALLRLAL---YPPLRRATEEQIvasAKEQSHFLETIRGIQTIKLFGREAEREARWLN------LLVDAINA 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27753995 356 GI------ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASL 410
Cdd:cd18567 217 DIrlqrlqILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSL 277
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
472-668 |
1.16e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.02 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVasLLERFYdpEAGSVTLDghDLRTLNPswlRGQVIgFISQEPVLFATTImeni 551
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI--SFLPKFS---RNKLI-FIDQLQFLIDVGL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 552 rfgkldasdeevytaareanahefissfpdGYSTVvGERGTTLSGGQKQRLAIARALIKQP--TVLILDEATSALDAESE 629
Cdd:cd03238 77 ------------------------------GYLTL-GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27753995 630 RVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVMANGQ 668
Cdd:cd03238 126 NQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
471-688 |
1.21e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF--YDPEAGSVTLDGHDLRTLNPSwLRGQVIGFIS-QEPVlfatTI 547
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAfQYPI----EI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 548 --MENIRFGKLDASDEEVYTAAREANAHEFISSFPDGySTVVGERGTTL--------SGGQKQRLAIARALIKQPTVLIL 617
Cdd:CHL00131 97 pgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEK-LKLVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27753995 618 DEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRAAHSIIVMANGQVCEAGTHE---ELLKKGglYSEL 688
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElakELEKKG--YDWL 250
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
451-684 |
1.49e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 451 RGSITFQNVTFSYPCRPGFnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTldghdlrtlnpsWLRG 530
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------------WSEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 531 QVIGFISQEPVL-FAT--TIMENIRFGKLDASDEevyTAAREANAHEFISSfpDGystvVGERGTTLSGGQKQRLAIARA 607
Cdd:PRK15064 382 ANIGYYAQDHAYdFENdlTLFDWMSQWRQEGDDE---QAVRGTLGRLLFSQ--DD----IKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27753995 608 LIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHRLSTVR--AAHSIIVMANGQVCEAGTHEELLKKGGL 684
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHDREFVSslATRIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
475-654 |
1.61e-08 |
|
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: 57.87 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 475 FTL-KLP---SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnPSWlrgqvigfisqEPVL--FATTIM 548
Cdd:COG1245 88 FRLyGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEE--------PSW-----------DEVLkrFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 549 ENiRFGKLdaSDEEVyTAAREANAHEFISSFPDGysTV------VGERG-------------------TTLSGGQKQRLA 603
Cdd:COG1245 149 QD-YFKKL--ANGEI-KVAHKPQYVDLIPKVFKG--TVrellekVDERGkldelaeklglenildrdiSELSGGELQRVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 604 IARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLST 654
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
466-653 |
1.78e-08 |
|
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: 55.84 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 466 RPGFNVLKDFTLKLP-SGKIVALVGQSGGGKTTVASLLerfydpeAGSVT--LDGHDLrtlNPSWlrGQVIGFisqepvl 542
Cdd:cd03236 9 RYGPNSFKLHRLPVPrEGQVLGLVGPNGIGKSTALKIL-------AGKLKpnLGKFDD---PPDW--DEILDE------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 543 FATTIMEN----IRFGKLDASDEEVYT----AAREANAHEFISS-----FPDGYSTVVGERG------TTLSGGQKQRLA 603
Cdd:cd03236 70 FRGSELQNyftkLLEGDVKVIVKPQYVdlipKAVKGKVGELLKKkdergKLDELVDQLELRHvldrniDQLSGGELQRVA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 604 IARALIKQPTVLILDEATSALDAESE----RVVQEaldRASAGRTVLVIAHRLS 653
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLA 200
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
592-680 |
4.13e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 56.96 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 592 TTLSGGQKQRLAIARALIK---QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVM--- 664
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTADWIIDLgpe 904
|
90
....*....|....*....
gi 27753995 665 ---ANGQVCEAGTHEELLK 680
Cdd:COG0178 905 ggdGGGEIVAEGTPEEVAK 923
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
454-653 |
1.03e-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: 55.14 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswlRGQVI 533
Cdd:TIGR00954 452 IKFENIPLVTP--NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------AKGKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVLFATTIMENI-------RFGKLDASDEEVYTAAREANAHEFISSfpDGYSTVVGERGTTLSGGQKQRLAIAR 606
Cdd:TIGR00954 518 FYVPQRPYMTLGTLRDQIiypdsseDMKRRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMAR 595
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEALDRasAGRTVLVIAHRLS 653
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
150-341 |
1.07e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 54.05 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 150 LLGQLVEIVAKY--TRDHMGSFVSESRKLSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDA 227
Cdd:cd18580 13 FLSQFSNIWLDWwsSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 228 KKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPrltlMLAVVTPALMGVGTLMGSGLRKLSRQCQ- 306
Cdd:cd18580 93 TPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLLQRYYLRTSRQLRr 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 27753995 307 -EQIARA---TGVAdEALGNVRTVRAFAMEKREEERYQA 341
Cdd:cd18580 169 lESESRSplySHFS-ETLSGLSTIRAFGWQERFIEENLR 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
457-670 |
1.22e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKT-TVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVI-- 533
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIam 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 --------GFISQEPVLFATTIMENIRF---GKLDASDEE--VYTAAREANAHEFISSFPDGystvvgergtTLSGGQKQ 600
Cdd:TIGR02633 341 vpedrkrhGIVPILGVGKNITLSVLKSFcfkMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 601 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVC 670
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
472-650 |
2.26e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 472 LKDFTLKLPSGKI-----VALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswLRgqvigfISQEPvlfatt 546
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LK------ISYKP------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 547 imENIRfgklDASDEEVYtaareanahEFISSFPDGYST---------------VVGERGTTLSGGQKQRLAIARALIKQ 611
Cdd:PRK13409 407 --QYIK----PDYDGTVE---------DLLRSITDDLGSsyykseiikplqlerLLDKNVKDLSGGELQRVAIAACLSRD 471
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27753995 612 PTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAH 650
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
570-690 |
2.49e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 570 ANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVV-QEALDRASAGRTVLVI 648
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLT 200
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 27753995 649 AHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIR 690
Cdd:NF000106 201 TQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIR 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
468-669 |
2.59e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP---------------------- 525
Cdd:PRK15439 278 GF---RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvylpedrqssglyl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 526 -SWLRGQVIGFISQEPVLFATTIMENIRFgkldasdeEVYTAAREANahefissFPDGYSTVvgergTTLSGGQKQRLAI 604
Cdd:PRK15439 355 dAPLAWNVCALTHNRRGFWIKPARENAVL--------ERYRRALNIK-------FNHAEQAA-----RTLSGGNQQKVLI 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27753995 605 ARALIKQPTVLILDEATSALDAeSER--VVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 669
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDV-SARndIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
593-689 |
2.93e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 593 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 669
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
90 100
....*....|....*....|
gi 27753995 670 CEAGTHEELLKKGGLYSELI 689
Cdd:COG4586 234 IYDGSLEELKERFGPYKTIV 253
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
134-421 |
4.05e-07 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to 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.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 52.15 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 134 IVLALGAALVNVQIPLLLGQLVEivakytrdhmgSFVSESRKLSVQLLLLYGV------QGLLTFGYLVLLSHIGERMAM 207
Cdd:cd18583 2 FLCLLAERVLNVLVPRQLGIIVD-----------SLSGGSGKSPWKEIGLYVLlrflqsGGGLGLLRSWLWIPVEQYSYR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 208 DMRKALFSSLLRQDIAFFDAKKTGQLVSrlttdvqefkssfklVISQG------LRSCT-QVIGSLVSLS--------ML 272
Cdd:cd18583 71 ALSTAAFNHVMNLSMDFHDSKKSGEVLK---------------AIEQGssindlLEQILfQIVPMIIDLViaivylyyLF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 273 SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEScCCKAE- 351
Cdd:cd18583 136 DPYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKN-YQKAEr 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 352 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGL 421
Cdd:cd18583 215 KYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDL 284
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
581-668 |
4.55e-07 |
|
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: 50.65 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 581 DGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRLSTVRAA 658
Cdd:cd03222 59 DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYL 138
|
90
....*....|
gi 27753995 659 HSIIVMANGQ 668
Cdd:cd03222 139 SDRIHVFEGE 148
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
176-394 |
5.50e-07 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 51.84 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTdVQEFKSSFKLVisqG 255
Cdd:cd18586 44 LTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDT-LRNFLTGPSLF---A 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAME--- 332
Cdd:cd18586 120 FFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLgnl 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 333 -KREEERYQAELESccckAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLM 394
Cdd:cd18586 200 rRRWEARHAETLEL----QIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALI 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
582-685 |
6.26e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 582 GYSTVVGergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRA-A 658
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiT 458
|
90 100 110
....*....|....*....|....*....|....
gi 27753995 659 HSIIVMANGQVceAG-------THEELLKKGGLY 685
Cdd:PRK10982 459 DRILVMSNGLV--AGivdtkttTQNEILRLASLH 490
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
482-683 |
9.18e-07 |
|
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: 52.71 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 482 GKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVIGFISQepvlfattimenirFGKLD---A 558
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH-QNMGYCPQ--------------FDAIDdllT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 559 SDEEVYTAAR---------EANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESE 629
Cdd:TIGR01257 2029 GREHLYLYARlrgvpaeeiEKVANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 630 RVVQEAL-DRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKKGG 683
Cdd:TIGR01257 2107 RMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
471-674 |
9.67e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLerfydpeAGSVT---LDGhDLRtlnpswlrgqVIGFISQEPVlFA--- 544
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVL-------AGRKTggyIEG-DIR----------ISGFPKKQET-FAris 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 545 ------------TTIMENIRFGKL-----DASDEEVYTAAREANAHEFISSFPDgysTVVGERGTT-LSGGQKQRLAIAR 606
Cdd:PLN03140 956 gyceqndihspqVTVRESLIYSAFlrlpkEVSKEEKMMFVDEVMELVELDNLKD---AIVGLPGVTgLSTEQRKRLTIAV 1032
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 607 ALIKQPTVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLS--TVRAAHSIIVMA-NGQVCEAGT 674
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSidIFEAFDELLLMKrGGQVIYSGP 1104
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
457-680 |
1.09e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 457 QNVTfsypcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTtvaSLLERFY--DPEA-GSVTLDGHDLRTLNPSWLRGQVI 533
Cdd:PRK09700 269 RNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSPLDAVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQ---EPVLFAT-TIMENIR-------------FGKLDASDEEVYTAAREANAHEFISSfpdgystvVGERGTTLSG 596
Cdd:PRK09700 341 AYITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLALKCHS--------VNQNITELSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 597 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAA-HSIIVMANGQV----- 669
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLtqilt 492
|
250
....*....|..
gi 27753995 670 -CEAGTHEELLK 680
Cdd:PRK09700 493 nRDDMSEEEIMA 504
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
582-685 |
1.34e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 52.00 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 582 GYSTVvGERGTTLSGGQKQRLAIARALIKQPT---VLILDEATSALDAESER----VVQEALDRasaGRTVLVIAHRLST 654
Cdd:PRK00349 820 GYIKL-GQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDV 895
|
90 100 110
....*....|....*....|....*....|....*..
gi 27753995 655 VRAAHSIIVM------ANGQVCEAGTHEELLKKGGLY 685
Cdd:PRK00349 896 IKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
469-681 |
1.79e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 469 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGfisqepvlfattiM 548
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTG-------------I 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 549 ENIRFGKL--DASDEEVYTAARE----ANAHEFISSFPDGYSTvvgergttlsgGQKQRLAIARALIKQPTVLILDEATS 622
Cdd:PRK13546 104 ENIEFKMLcmGFKRKEIKAMTPKiiefSELGEFIYQPVKKYSS-----------GMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27753995 623 ALDaesERVVQEALDR----ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 681
Cdd:PRK13546 173 VGD---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
467-668 |
2.46e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 467 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQE-PVLFAT 545
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 546 TIMENIRFGK-----LDASDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQPTVLILDEA 620
Cdd:PRK10982 89 SVMDNMWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 621 TSALdAESE-----RVVQEALDRasaGRTVLVIAHRLSTV-RAAHSIIVMANGQ 668
Cdd:PRK10982 162 TSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
133-333 |
2.50e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 49.79 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVEIVAKYTrdhmGSFVSESRKLSVQLLLLYGVQGLLTFGYLvllsHIGERMAMDMRKA 212
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYP----DEPLSEGYLLALALFLVSLLQSLLLHQYF----FLSFRLGMRVRSA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 213 LFSSL----LRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFkLVISQGLRSCTQVIGSLVSLSMLsprltlmlaVVTPALM 288
Cdd:cd18579 74 LSSLIyrkaLRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRL---------LGWAALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 289 GVGTLMGS-----GLRKLSRQCQEQIARAT----GVADEALGNVRTVRAFAMEK 333
Cdd:cd18579 144 GLGVLLLLiplqaFLAKLISKLRKKLMKATdervKLTNEILSGIKVIKLYAWEK 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
594-655 |
2.54e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 594 LSGGQkQRLA-IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV------------IAHRLSTV 655
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFV 476
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
454-658 |
3.07e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFNVLKDFtlkLPSGkIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdghdlRTLNPSWLRGQVI 533
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFDLSITF---LPSA-ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNIAKPYC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 534 GFISQEPVL-FATTIMENIRF-GKLDASDEEVYTAAREANAHEFISsfpdgystvvgERGTTLSGGQKQRLAIARALIKQ 611
Cdd:PRK13541 73 TYIGHNLGLkLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27753995 612 PTVLILDEATSALDAESERVVQEALD-RASAGRTVLVIAHRLSTVRAA 658
Cdd:PRK13541 142 SDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
133-398 |
3.26e-06 |
|
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: 49.53 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 133 AIVLALGAALVNVQIPLLLGQLVeivakytrDHMGSFVSESRKLSVQLLLLYGVQGLL--TFGYL--VLLSHIGERMAMD 208
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAV--------NALTLAKVKDLESAVTLILLYALLRFSskLLKELrsLLYRRVQQNAYRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 209 MRKALFSSLLRQDIAFFDAKKTGQLVS---RLTTDVQEFKSSFKLVISQGLRSCTQVigSLVSLSMLSPRLTLMLaVVTP 285
Cdd:cd18560 73 LSLKTFAHLHSLSLDWHLSKKTGEVVRimdRGTESANTLLSYLVFYLVPTLLELIVV--SVVFAFHFGAWLALIV-FLSV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 286 ALMGVGTLMGSGLR-KLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEELGRGIALFQGLS 364
Cdd:cd18560 150 LLYGVFTIKVTEWRtKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVK----EYQKSSVKVQASLSLL 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 27753995 365 NIA----FNCMVLGTLFIGGSLVAGQQLKGGDLMSFLV 398
Cdd:cd18560 226 NVGqqliIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNT 263
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
452-625 |
4.09e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 452 GSITFQ--NVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKT-TVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 528
Cdd:PRK13549 256 GEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RGQVIGFISQE-------PVLfatTIMENI---------RFGKLDASDEEvyTAAREANAHEFI-SSFPDgystvvgERG 591
Cdd:PRK13549 336 IAQGIAMVPEDrkrdgivPVM---GVGKNItlaaldrftGGSRIDDAAEL--KTILESIQRLKVkTASPE-------LAI 403
|
170 180 190
....*....|....*....|....*....|....
gi 27753995 592 TTLSGGQKQRLAIARALIKQPTVLILDEATSALD 625
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
481-677 |
4.15e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 481 SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPswlrGQVI--GFI------SQEPVLFATTIMENI- 551
Cdd:PRK11288 278 AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP----RDAIraGIMlcpedrKAEGIIPVHSVADNIn 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 552 --------RFGKLdasdeevYTAAREA-NAHEFISSF----PDGYSTVVgergtTLSGGQKQRLAIARALIKQPTVLILD 618
Cdd:PRK11288 354 isarrhhlRAGCL-------INNRWEAeNADRFIRSLniktPSREQLIM-----NLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27753995 619 EATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEE 677
Cdd:PRK11288 422 EPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
454-650 |
4.50e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 454 ITFQNVTFSYPCRPGFNVLKDFTLKLPSGkiVALVGQSGGGKTTVASLLERFYDPEAGSV--------------TLDGHD 519
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSR--IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 520 LrtlnpswlrgqvigfiSQEPVLFATtimenirfgkldasdeEVYTAAREANAHEFISSFpdGYS-TVVGERGTTLSGGQ 598
Cdd:PLN03073 587 L----------------SSNPLLYMM----------------RCFPGVPEQKLRAHLGSF--GVTgNLALQPMYTLSGGQ 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27753995 599 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGrtVLVIAH 650
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSH 682
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
582-707 |
5.11e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 582 GYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AH 659
Cdd:PRK10938 124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQ 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 27753995 660 SIIVMANGQVCEAGTHEELLKKgGLYSELIRRQTLDAslTSTPPAEKP 707
Cdd:PRK10938 204 FAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEG--VQLPEPDEP 248
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
176-339 |
9.54e-06 |
|
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: 47.93 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRL--TTDVQEfkssfkLVIS 253
Cdd:cd18779 44 LGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLssNATIRE------LLTS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 254 QGLRSC---TQVIGSLVSLSMLSPRLTLMLAVVtpALMGVGTLMGSG--LRKLSRQCQEQIARATGVADEALGNVRTVRA 328
Cdd:cd18779 118 QTLSALldgTLVLGYLALLFAQSPLLGLVVLGL--AALQVALLLATRrrVRELMARELAAQAEAQSYLVEALSGIETLKA 195
|
170
....*....|.
gi 27753995 329 FAMEKREEERY 339
Cdd:cd18779 196 SGAEDRALDRW 206
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
468-650 |
1.23e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 468 GFNVLKD-FTLKLPSGkIVALVGQSGGGKTTV---------------ASLLERF--YDPEAGSVTLD-GHDLRTLNPSWL 528
Cdd:COG0419 9 NFRSYRDtETIDFDDG-LNLIVGPNGAGKSTIleairyalygkarsrSKLRSDLinVGSEEASVELEfEHGGKRYRIERR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 529 RGQVIGFISQEP--------VLFATTIMENI--RFGKLDASDEEVYTAAREANA--HEFISSFpDGYSTVvgergTTLSG 596
Cdd:COG0419 88 QGEFAEFLEAKPserkealkRLLGLEIYEELkeRLKELEEALESALEELAELQKlkQEILAQL-SGLDPI-----ETLSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 597 GQKQRLAIARALikqptVLILDeaTSALDAESERVVQEALDRASagrtvlVIAH 650
Cdd:COG0419 162 GERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
474-625 |
1.34e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 474 DFT------LKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL-----DGHDLRTlnpswlRGQViGFISQEPVL 542
Cdd:NF033858 278 DFTavdhvsFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIAT------RRRV-GYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 543 FAT-TIMENIrfgKLDASDEEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 621
Cdd:NF033858 351 YGElTVRQNL---ELHARLFHLPAAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 27753995 622 SALD 625
Cdd:NF033858 426 SGVD 429
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
592-713 |
2.59e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 592 TTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMA-- 665
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGpe 887
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 27753995 666 ----NGQVCEAGTHEELLKKGGLYSELIR---RQTLDASLTSTPPaekPEDPKSC 713
Cdd:PRK00635 888 ggnlGGYLLASCSPEELIHLHTPTAKALRpylSSPQELPYLPDPS---PKPPVPA 939
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
464-648 |
3.02e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 464 PCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVA-SLLERFYDP-EAGSVTLDGHDLRTLNPSWLRGQVIGFISQEP- 540
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRk 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 541 ----VLfATTIMENIRFGKLDA-SDEEVYTAAREAN-AHEFISSF----PDGYSTVVgergtTLSGGQKQRLAIARALIK 610
Cdd:NF040905 348 gyglNL-IDDIKRNITLANLGKvSRRGVIDENEEIKvAEEYRKKMniktPSVFQKVG-----NLSGGNQQKVVLSKWLFT 421
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27753995 611 QPTVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVI 648
Cdd:NF040905 422 DPDVLILDEPTRGIDvgAKYEiyTIINEL---AAEGKGVIVI 460
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
181-285 |
6.23e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 45.55 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 181 LLLYG----VQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGL 256
Cdd:cd18603 44 LGVYGalglGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFL 123
|
90 100
....*....|....*....|....*....
gi 27753995 257 RSCTQVIGSLVSLSMLSPrltLMLAVVTP 285
Cdd:cd18603 124 NCLFQVISTLVVISISTP---IFLVVIIP 149
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
472-525 |
8.61e-05 |
|
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: 43.89 E-value: 8.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27753995 472 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP 525
Cdd:pfam06414 1 LDDKTTSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
484-662 |
1.16e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 484 IVALVGQSGGGKTTVAsllerfydpEAGSVTLDGH-----DLRTLNPSWLR-GQVIGFISqepvlfattimenIRFgKLD 557
Cdd:cd03240 24 LTLIVGQNGAGKTTII---------EALKYALTGElppnsKGGAHDPKLIReGEVRAQVK-------------LAF-ENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 558 ASDEevYTAAREANAHEFISSFPDGYST--VVGERGTtLSGGQKQ------RLAIARALIKQPTVLILDEATSALDAES- 628
Cdd:cd03240 81 NGKK--YTITRSLAILENVIFCHQGESNwpLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENi 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 27753995 629 ERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSII 662
Cdd:cd03240 158 EESLAEIIEerKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
180-344 |
1.20e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 44.83 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 180 LLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 259
Cdd:cd18605 48 YGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 260 TQVIGSLVSLSMLSPrltLMLAVVTPaLMGVGTLMGSGLRKLSRqcqeQIARATGVA--------DEALGNVRTVRAFAM 331
Cdd:cd18605 128 FGLLGYLVVICYQLP---WLLLLLLP-LAFIYYRIQRYYRATSR----ELKRLNSVNlsplythfSETLKGLVTIRAFRK 199
|
170
....*....|...
gi 27753995 332 EKREEERYQAELE 344
Cdd:cd18605 200 QERFLKEYLEKLE 212
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
176-410 |
1.37e-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: 44.43 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRL--TTDVQEFKSSfklvis 253
Cdd:cd18783 44 LTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMqqIERIRQFLTG------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 254 qglrsctQVIGSLVSLSML----------SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNV 323
Cdd:cd18783 118 -------QLFGTLLDATSLlvflpvlffySPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 324 RTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTV 403
Cdd:cd18783 191 RTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRV 270
|
250
....*....|
gi 27753995 404 QR---SMASL 410
Cdd:cd18783 271 AGplvQLAGL 280
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
592-675 |
1.50e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 592 TTLSGGQKQRLAIARALIKQPT--VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVMANGq 668
Cdd:cd03270 136 PTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVIDIGPG- 214
|
....*..
gi 27753995 669 vceAGTH 675
Cdd:cd03270 215 ---AGVH 218
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
178-355 |
1.65e-04 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 44.13 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 178 VQLLLLYG---VQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQ 254
Cdd:cd18559 39 VYLSVLGAlaiLQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 255 GLRSCTQVIGSLVSLSMLSPRLTLMLAVVTpALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAmekr 334
Cdd:cd18559 119 WMGPLQNVIGLYLLILLAGPMAAVGIPLGL-LYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE---- 193
|
170 180
....*....|....*....|.
gi 27753995 335 EEERYQAELESccCKAEELGR 355
Cdd:cd18559 194 WEEAFIRQVDA--KRDNELAY 212
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
186-334 |
1.85e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.00 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 186 VQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGS 265
Cdd:cd18606 47 LQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGT 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27753995 266 LVSLSMLSPrltlMLAVVTPALMGVGTLMGSGLRKLSRQCQ--EQIARATGVA--DEALGNVRTVRAFAMEKR 334
Cdd:cd18606 127 FILIIIYLP----WFAIALPPLLVLYYFIANYYRASSRELKrlESILRSFVYAnfSESLSGLSTIRAYGAQDR 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
471-636 |
1.87e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 471 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswlRGQVIGFISQEPVLFattimen 550
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGIKLGYFAQHQLEF------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 551 irfgkLDASDEEVYTAAR------EANAHEFISSFpdGYS-TVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 623
Cdd:PRK10636 388 -----LRADESPLQHLARlapqelEQKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170
....*....|...
gi 27753995 624 LDAESERVVQEAL 636
Cdd:PRK10636 461 LDLDMRQALTEAL 473
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
592-681 |
2.75e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 592 TTLSGGQKQRLAIARALIKQPT-VL-ILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMA--- 665
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTgVLyVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGpga 566
|
90
....*....|....*....
gi 27753995 666 ---NGQVCEAGTHEELLKK 681
Cdd:TIGR00630 567 gehGGEVVASGTPEEILAN 585
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
592-628 |
2.88e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 2.88e-04
10 20 30
....*....|....*....|....*....|....*..
gi 27753995 592 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES 628
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
593-668 |
3.60e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 3.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 593 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASagRTVLVIAHRLSTVRAAHSIIVMANGQ 668
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
479-663 |
4.21e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 479 LPSGKIVALVGQSGGGKTTVasllerfydpeagsvtldghdLRTlnpswlrgqvIGFIsqepvlfatTIMENIRFGKLDA 558
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTI---------------------LDA----------IGLA---------LGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 559 SDEEVYTAAREAnahEFISSFPdgystvvgergtTLSGGQKQRLAIARAL----IKQPTVLILDEATSALDAESERVVQE 634
Cdd:cd03227 58 VKAGCIVAAVSA---ELIFTRL------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180 190
....*....|....*....|....*....|.
gi 27753995 635 AL-DRASAGRTVLVIAHRL-STVRAAHSIIV 663
Cdd:cd03227 123 AIlEHLVKGAQVIVITHLPeLAELADKLIHI 153
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
180-423 |
1.07e-03 |
|
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: 41.50 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 180 LLLLYGVQGLLTFGYLVLLSHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 259
Cdd:cd18561 42 IAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 260 TQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERY 339
Cdd:cd18561 122 LGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 340 QAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVR 419
Cdd:cd18561 202 AARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQ 281
|
....
gi 27753995 420 GLSA 423
Cdd:cd18561 282 GISA 285
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
134-247 |
2.05e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 40.69 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 134 IVLALGAALVNVQiPLLLGQLVeivakytrdhmGSFVSESRKLSVQLLLLYGVQGLLTFGyLVLLSHI----GERMAMDM 209
Cdd:cd18594 4 ILLFLEESLKIVQ-PLLLGRLV-----------AYFVPDSTVTKTEAYLYALGLSLCAFL-RVLLHHPyffgLHRYGMQL 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27753995 210 RKALFSSLLRQDIAF----FDAKKTGQLVSRLTTDVQEFKSS 247
Cdd:cd18594 71 RIALSSLIYKKTLKLsssaLSKITTGHIVNLLSNDVQKFDEV 112
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
587-667 |
3.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 587 VGERGTTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSII 662
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
....*
gi 27753995 663 VMANG 667
Cdd:PRK00635 1773 EMGPG 1777
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
176-334 |
6.41e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 39.37 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 176 LSVQLLLLYGVQGLLTFGYLVLLsHIGERMAMDMRKALFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQG 255
Cdd:cd18604 46 LGIYALISLLSVLLGTLRYLLFF-FGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 256 LRSCTQVIGSLVSLSMLSPRLTLMLAVVTpalmGVGTLMGSGLRKLSRQCQ--EQIARAT--GVADEALGNVRTVRAFAM 331
Cdd:cd18604 125 LESTLSLLVILIAIVVVSPAFLLPAVVLA----ALYVYIGRLYLRASRELKrlESVARSPilSHFGETLAGLVTIRAFGA 200
|
...
gi 27753995 332 EKR 334
Cdd:cd18604 201 EER 203
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
213-340 |
7.96e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 39.08 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27753995 213 LFSSLLRQDIAFFDAKKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVIGSLVSLSMLSPRLTLMLAVVTPALMGVGT 292
Cdd:cd18599 97 LFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSK 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 27753995 293 LMGSGLRKLSRqcQEQIAR--------ATGvadEALGnvrTVRAFAMEKREEERYQ 340
Cdd:cd18599 177 IFRRAIRELKR--LENISRsplfshltATI---QGLS---TIHAFNKEKEFLSKFK 224
|
|
| |
