|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
186-788 |
0e+00 |
|
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: 791.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 186 SAAQQSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLA--WTVTSY 263
Cdd:COG5265 5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVpvGLLLAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 264 VFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVF 343
Cdd:COG5265 85 GLLRLL------SVLF-GELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 344 NVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAE 423
Cdd:COG5265 158 NILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 424 SYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGT 503
Cdd:COG5265 238 AREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 504 YYRMIQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGK 583
Cdd:COG5265 318 VYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 584 STILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAI 663
Cdd:COG5265 398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 664 MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVV 743
Cdd:COG5265 478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1169100883 744 NADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSED 788
Cdd:COG5265 558 DADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEA 602
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
194-783 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 565.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 194 RDFGRKLRLLSGYLWPRgspalQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGgg 273
Cdd:COG1132 3 KSPRKLLRRLLRYLRPY-----RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 274 tgstgFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLAdII 353
Cdd:COG1132 76 -----LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV-TL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 354 IGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREA 433
Cdd:COG1132 150 IGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 434 IIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFI 513
Cdd:COG1132 230 NEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 514 DMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:COG1132 310 SAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQ 673
Cdd:COG1132 390 YDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 674 VGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKD 753
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDD 549
|
570 580 590
....*....|....*....|....*....|
gi 1169100883 754 GCIVERGRHEALLSRGGVYADMWQLQQGQE 783
Cdd:COG1132 550 GRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
222-518 |
0e+00 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. 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, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, 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: 350025 [Multi-domain] Cd Length: 300 Bit Score: 527.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTEK---APWNSLAWTVTSYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd18581 1 CLLLLAAGRVVNVLVPILYKKIVDSLTPDsadSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 378
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 379 LTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLV 458
Cdd:cd18581 161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 459 IGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18581 241 ITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
544-779 |
1.93e-162 |
|
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: 470.17 E-value: 1.93e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIIL 703
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
198-780 |
1.35e-141 |
|
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: 433.88 E-value: 1.35e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 198 RKLRLLSGYLWPRGSPALQLVVL-ICLGLMGLeralnvLVPIFYRNIVNL-LTEKAPwnSLAWTVTsyvflkFLQGGGTG 275
Cdd:COG2274 142 FGLRWFLRLLRRYRRLLLQVLLAsLLINLLAL------ATPLFTQVVIDRvLPNQDL--STLWVLA------IGLLLALL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 276 STGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIadRGTSSVTGLLSYLVFNvipTLADIII 354
Cdd:COG2274 208 FEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAsRF--RDVESIREFLTGSLLT---ALLDLLF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 355 GIIYFSM--FFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYRE 432
Cdd:COG2274 283 VLIFLIVlfFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWEN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 433 AIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNF 512
Cdd:COG2274 363 LLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 513 IDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYA-DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF 591
Cdd:COG2274 443 IALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 592 RFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYR 671
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 672 TQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVI 751
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
570 580
....*....|....*....|....*....
gi 1169100883 752 KDGCIVERGRHEALLSRGGVYADMWQLQQ 780
Cdd:COG2274 683 DKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
222-518 |
1.95e-128 |
|
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: 385.04 E-value: 1.95e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTeKAPWNSLAWTVTSYVFLKFLQGggtgSTGFVSNLRTFLWIRVQQFTSRRVEL 301
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALT-LAKVKDLESAVTLILLYALLRF----SSKLLKELRSLLYRRVQQNAYRELSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 302 LIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTL 381
Cdd:cd18560 76 KTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 382 TIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGL 461
Cdd:cd18560 156 TIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 462 GLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18560 236 GLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
544-776 |
6.20e-121 |
|
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: 363.47 E-value: 6.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMW 776
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
207-782 |
2.30e-114 |
|
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: 358.65 E-value: 2.30e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 207 LWPRGSPALQLVVLICLGlMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQG-GGTGSTGFVSnlrt 285
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVA-MILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGiCSFVSTYLLS---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 286 flWIRVQQFTSRRVELliFSHLHELSLRWHLGRRTGEVLriaDRGTSSVTGLLSYL--VFNVIPTLADIIIGIIYFSMFF 363
Cdd:TIGR02203 80 --WVSNKVVRDIRVRM--FEKLLGLPVSFFDRQPTGTLL---SRITFDSEQVASAAtdAFIVLVRETLTVIGLFIVLLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 364 NAWFGLIVFLCMSLyltLTIVVTEWRTKFRR-AMNTQE-NATRARAVDSLL-NFETVKYYNAESYEVERYREAIIKYQGL 440
Cdd:TIGR02203 153 SWQLTLIVVVMLPV---LSILMRRVSKRLRRiSKEIQNsMGQVTTVAEETLqGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 441 EWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFD 520
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 521 LLKEETEVKDlpGAGPLRFQKGRIEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG 599
Cdd:TIGR02203 310 LLDSPPEKDT--GTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 600 CIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRV-TAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERG 678
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVE 758
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
570 580
....*....|....*....|....
gi 1169100883 759 RGRHEALLSRGGVYADMWQLQQGQ 782
Cdd:TIGR02203 548 RGTHNELLARNGLYAQLHNMQFRE 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
544-779 |
1.77e-112 |
|
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: 341.44 E-value: 1.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAD--GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
297-775 |
2.33e-111 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 351.19 E-value: 2.33e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 297 RRVELLI--FSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLlsYLVF--NVIPTLADIIIgIIYFSMFFNAWFGLIVF 372
Cdd:PRK13657 87 RRLAVLTeyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGL--WLEFmrEHLATLVALVV-LLPLALFMNWRLSLVLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLYLTLTIVVTEwRTK-FRRAMNTQENATRARAVDSLLNFETVKYYN---AESYEVERYREAIIKYQG--LEWKSSA 446
Cdd:PRK13657 164 VLGIVYTLITTLVMR-KTKdGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIADNLLAAQMpvLSWWALA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 447 SLvlLNQTQN----LVIGLGLlagsllcAYFVTEQKLQVGD---YVLFGTYIIQlymplnwfgtyyRMIQT-NFID---- 514
Cdd:PRK13657 243 SV--LNRAAStitmLAILVLG-------AALVQKGQLRVGEvvaFVGFATLLIG------------RLDQVvAFINqvfm 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 515 ----MENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL 590
Cdd:PRK13657 302 aapkLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 591 FRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGY 670
Cdd:PRK13657 382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 671 RTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILV 750
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
|
490 500
....*....|....*....|....*
gi 1169100883 751 IKDGCIVERGRHEALLSRGGVYADM 775
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
542-770 |
2.32e-110 |
|
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: 335.73 E-value: 2.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
222-518 |
5.15e-101 |
|
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: 313.70 E-value: 5.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTE---KAPWNSlawtVTSYVFLKFLQGGGtgstgFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLSGgsgKSPWKE----IGLYVLLRFLQSGG-----GLGLLRSWLWIPVEQYSYRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRIADRGtSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 378
Cdd:cd18583 72 LSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQG-SSINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 379 LTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLV 458
Cdd:cd18583 151 VWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 459 IGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18583 231 LTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
278-779 |
3.80e-100 |
|
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: 321.65 E-value: 3.80e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 278 GFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLriaDRGTSSVTGLLSYLVFNVIPTLADIIIGII 357
Cdd:TIGR02204 72 ALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVV---SRLTTDTTLLQSVIGSSLSMALRNALMCIG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 358 YFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQEN--ATRARAVDSLLNFETVKYYNAESYEVERYREAII 435
Cdd:TIGR02204 149 GLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRiaDAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 436 KYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDM 515
Cdd:TIGR02204 229 KAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 516 ENMFDLLKEETEV------KDLPGagPLRfqkGRIEFENVHFSYADGRET--LQDVSFTVMPGQTLALVGPSGAGKSTIL 587
Cdd:TIGR02204 309 ERLIELLQAEPDIkapahpKTLPV--PLR---GEIEFEQVNFAYPARPDQpaLDGLNLTVRPGETVALVGPSGAGKSTLF 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 588 RLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFP 667
Cdd:TIGR02204 384 QLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 668 EGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQ 747
Cdd:TIGR02204 464 EGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADR 543
|
490 500 510
....*....|....*....|....*....|..
gi 1169100883 748 ILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:TIGR02204 544 IVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
222-518 |
5.96e-98 |
|
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: 305.96 E-value: 5.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLA--WTVTSYVFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRRV 299
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVplLLLLAYGLARIL------SSLF-NELRDALFARVSQRAVRRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 300 ELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYL 379
Cdd:cd18582 74 ALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 380 TLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVI 459
Cdd:cd18582 154 AFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALII 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 460 GLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENM 518
Cdd:cd18582 234 SLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
495-770 |
6.63e-98 |
|
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: 315.16 E-value: 6.63e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 495 YMPLNWFGTYY--RMIQTNFidMENMFDLLkEETEVKDLPGAGPLRFQKG-RIEFENVHFSYADGRETLQDVSFTVMPGQ 571
Cdd:COG4988 288 FLPLRDLGSFYhaRANGIAA--AEKIFALL-DAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRPALDGLSLTIPPGE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 572 TLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVE 651
Cdd:COG4988 365 RVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 652 AAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRT 731
Cdd:COG4988 445 AALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT 524
|
250 260 270
....*....|....*....|....*....|....*....
gi 1169100883 732 TIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:COG4988 525 VILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
518-782 |
1.77e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 304.25 E-value: 1.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 518 MFDLLKEETEvKDLpGAGPLRFQKGRIEFENVHFSYaDGRET--LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYD 595
Cdd:PRK11176 318 LFAILDLEQE-KDE-GKRVIERAKGDIEFRNVTFTY-PGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 596 ISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRV-TAGNDEVEAAAQAAGIHDAIMAFPEGYRTQV 674
Cdd:PRK11176 395 IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 675 GERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
250 260
....*....|....*....|....*...
gi 1169100883 755 CIVERGRHEALLSRGGVYADMWQLQQGQ 782
Cdd:PRK11176 555 EIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
298-778 |
1.69e-92 |
|
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: 300.91 E-value: 1.69e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 298 RVELliFSHLHELSLRWHLGRRTGEVL-RI-ADrgtssVTGLLSYLVFNVIPTLADI--IIGIIYFSMFFNAWFGLIVFL 373
Cdd:COG4987 91 RVRL--YRRLEPLAPAGLARLRSGDLLnRLvAD-----VDALDNLYLRVLLPLLVALlvILAAVAFLAFFSPALALVLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 374 CMSLYLTLTIVVTEWRTKFR-RAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLN 452
Cdd:COG4987 164 GLLLAGLLLPLLAARLGRRAgRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 453 QTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFgtyiiqLYMPLNWF-------GTYYRMIQTnfID-MENMFDLLKE 524
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL------VLAALALFealaplpAAAQHLGRV--RAaARRLNELLDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 525 ETEVKDlPGAGPLRFQKGRIEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI 603
Cdd:COG4987 316 PPAVTE-PAEPAPAPGGPSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 604 DGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSG 683
Cdd:COG4987 395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSG 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHE 554
|
490
....*....|....*
gi 1169100883 764 ALLSRGGVYADMWQL 778
Cdd:COG4987 555 ELLAQNGRYRQLYQR 569
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
107-775 |
8.67e-91 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 300.49 E-value: 8.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 107 LLLASVLESLAGACGLWLLVVERSQARQRLAMGIWIKFRhspgLLLLWTVAFAAENLALVSWNS---------PQW--WW 175
Cdd:TIGR00958 51 VLWLGALGILLNKAGGLLAAVKPLVAALCLATPSLSSLR----ALAFWEALDPAVRVALGLWSWfvwsygaalPAAalWA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 176 ARADLGQQVRSAAQ-QSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMgleralnvLVPIFYRNIVNLLTEKAPWN 254
Cdd:TIGR00958 127 VLSSAGASEKEAEQgQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEM--------FIPFYTGRVIDTLGGDKGPP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 255 SLAWTVTsyvFLKFLQGGGTGSTGFVSNLRTFLWIRVQqftsRRVELLIFSHLHELSLRWHLGRRTGEvlrIADRGTSSV 334
Cdd:TIGR00958 199 ALASAIF---FMCLLSIASSVSAGLRGGSFNYTMARIN----LRIREDLFRSLLRQDLGFFDENKTGE---LTSRLSSDT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 335 TGLLSYLVFNVIPTLADIIIGI-IYFSMFFNAWFGLIVFLcmsLYLTLTIVVTEWRTKFRRAMNTQENATRARAVD---- 409
Cdd:TIGR00958 269 QTMSRSLSLNVNVLLRNLVMLLgLLGFMLWLSPRLTMVTL---INLPLVFLAEKVFGKRYQLLSEELQEAVAKANQvaee 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 410 SLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGT 489
Cdd:TIGR00958 346 ALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 490 YIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKdLPGAGPLRFQKGRIEFENVHFSYAD--GRETLQDVSFTV 567
Cdd:TIGR00958 426 YQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP-LTGTLAPLNLEGLIEFQDVSFSYPNrpDVPVLKGLTFTL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 568 MPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGN 647
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPD 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 648 DEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKvc 727
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR-- 662
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1169100883 728 ANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
544-779 |
1.30e-89 |
|
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: 282.07 E-value: 1.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQ 779
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
544-754 |
1.20e-81 |
|
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: 258.47 E-value: 1.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIrygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
297-793 |
1.77e-81 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 272.15 E-value: 1.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 297 RRVELLI--FSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGL-LSYLVFNVIPTLADIIIGIIYFSMffNAWFGLIVFL 373
Cdd:TIGR01192 87 RRATLLTeaFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLwLEFMRQHLATFVALFLLIPTAFAM--DWRLSIVLMV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 374 CMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYN---AESYEVERYREAII--KYQGLEWKSSASL 448
Cdd:TIGR01192 165 LGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNrieAETSALKQFTNNLLsaQYPVLDWWALASG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 449 vlLNQTQNLViglGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEV 528
Cdd:TIGR01192 245 --LNRMASTI---SMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQR 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 529 KDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI 608
Cdd:TIGR01192 320 EEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 609 SQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQR 688
Cdd:TIGR01192 400 NTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:TIGR01192 480 LAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
490 500
....*....|....*....|....*.
gi 1169100883 769 GGVYADMwqLQQGQEETSED-TKPQT 793
Cdd:TIGR01192 560 DGRFYKL--LRRSGLLTNQPaTKPLR 583
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
541-756 |
4.33e-72 |
|
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: 235.06 E-value: 4.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 541 KGRIEFENVHFSYAD--GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS 618
Cdd:cd03248 9 KGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCI 756
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
521-795 |
3.19e-71 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 244.24 E-value: 3.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 521 LLKEETEVKDlpGAGPLRFQKGRIEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG 599
Cdd:PRK10789 293 MLAEAPVVKD--GSEPVPEGRGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 600 CIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGL 679
Cdd:PRK10789 371 DIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGV 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 680 KLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVER 759
Cdd:PRK10789 451 MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
250 260 270
....*....|....*....|....*....|....*.
gi 1169100883 760 GRHEALLSRGGVYADMWQLQqgQEETSEDTKPQTME 795
Cdd:PRK10789 531 GNHDQLAQQSGWYRDMYRYQ--QLEAALDDAPEIRE 564
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
542-760 |
8.33e-71 |
|
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: 231.71 E-value: 8.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03245 1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPG 700
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
283-768 |
9.52e-70 |
|
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: 240.04 E-value: 9.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 283 LRTFLWIRVQQFTSRRVELLIFSHLHELSLRwHLGRRTGEVLRiaDrgtssVTGLLSYLVFNVIPTLAD-----IIIGII 357
Cdd:COG4618 79 VRSRILVRVGARLDRRLGPRVFDAAFRAALR-GGGGAAAQALR--D-----LDTLRQFLTGPGLFALFDlpwapIFLAVL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 358 YFsmfFNAWFGLIVFLCMSLYLTLTIVvTEWRTKFRRAMNTQENATRARAVDSLLNfetvkyyNAESYE--------VER 429
Cdd:COG4618 151 FL---FHPLLGLLALVGALVLVALALL-NERLTRKPLKEANEAAIRANAFAEAALR-------NAEVIEamgmlpalRRR 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 430 YREAIIKYQGLE--------WKSSASLVLLNQTQNLVIGLGllagsllcAYFVTEQKLQVGdyVLFGTYII--QLYMPL- 498
Cdd:COG4618 220 WQRANARALALQarasdragGFSALSKFLRLLLQSAVLGLG--------AYLVIQGEITPG--AMIAASILmgRALAPIe 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 499 ----NWfgtyyRMIQ---TNFIDMENMFDLLKEETEVKDLPGAgplrfqKGRIEFENVHFSYADGRE-TLQDVSFTVMPG 570
Cdd:COG4618 290 qaigGW-----KQFVsarQAYRRLNELLAAVPAEPERMPLPRP------KGRLSVENLTVVPPGSKRpILRGVSFSLEPG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 571 QTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNI-RYGRVTAgnDE 649
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGDADP--EK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 650 VEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA- 728
Cdd:COG4618 437 VVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAr 516
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1169100883 729 NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG4618 517 GATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
219-751 |
2.83e-69 |
|
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: 237.57 E-value: 2.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFY--RNIVNLLTEKAPWNSLAW---TVTSYVFLKFLQGGGTGSTGFVSNLRtflwIRVQq 293
Cdd:TIGR02857 4 ALALLALLGVLGALLIIAQAWLlaRVVDGLISAGEPLAELLPalgALALVLLLRALLGWLQERAAARAAAA----VKSQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 ftsRRVELLifSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLS-YLVFNViptLADIIIGIIYFSMFFNAWFGLIVF 372
Cdd:TIGR02857 79 ---LRERLL--EAVAALGPRWLQGRPSGELATLALEGVEALDGYFArYLPQLV---LAVIVPLAILAAVFPQDWISGLIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLYLTLTIVVTEWRTKfrRAMNTQENAT---------RARAVDSLLNFETVKYYNAESYEV-ERYREAIIKYQGLEW 442
Cdd:TIGR02857 151 LLTAPLIPIFMILIGWAAQ--AAARKQWAALsrlsghfldRLRGLPTLKLFGRAKAQAAAIRRSsEEYRERTMRVLRIAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 443 KSSASLVLLNQTQNLVIglgllagsllcAYFVTeQKLQVGDYVLFGTYIIQL-----YMPLNWFGTYYRMIQTNFIDMEN 517
Cdd:TIGR02857 229 LSSAVLELFATLSVALV-----------AVYIG-FRLLAGDLDLATGLFVLLlapefYLPLRQLGAQYHARADGVAAAEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 518 MFDLLKEET----EVKDLPGAGPLRfqkgrIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:TIGR02857 297 LFAVLDAAPrplaGKAPVTAAPASS-----LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQ 673
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTP 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 674 VGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVI 751
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
196-775 |
3.09e-69 |
|
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: 242.16 E-value: 3.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 196 FGRKLRLLSGyLWPR--GSP-ALQLVVLICLGLMglerALNVLVPIFYRNIVN--LLTEKAPW-----NSLAWTVTSYVF 265
Cdd:TIGR03796 135 GGRKPSLLRA-LWRRlrGSRgALLYLLLAGLLLV----LPGLVIPAFSQIFVDeiLVQGRQDWlrpllLGMGLTALLQGV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 266 LKFLQGGGTgstgfvsnlrtflwIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEV---LRIADRGTSSVTGLLsylv 342
Cdd:TIGR03796 210 LTWLQLYYL--------------RRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIasrVQLNDQVAEFLSGQL---- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 343 fnvIPTLADIIIGIIYFS-MF-FNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYY 420
Cdd:TIGR03796 272 ---ATTALDAVMLVFYALlMLlYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKAS 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 421 NAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLN- 499
Cdd:TIGR03796 349 GLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNn 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 500 --WFGTYYRMIQTNFID----MENMFDLLKEETEVKDLPGAGPLRFQkGRIEFENVHFSY-ADGRETLQDVSFTVMPGQT 572
Cdd:TIGR03796 429 lvGFGGTLQELEGDLNRlddvLRNPVDPLLEEPEGSAATSEPPRRLS-GYVELRNITFGYsPLEPPLIENFSLTLQPGQR 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 573 LALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEA 652
Cdd:TIGR03796 508 VALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVR 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 653 AAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKV-CanrT 731
Cdd:TIGR03796 588 ACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRgC---T 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1169100883 732 TIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR03796 665 CIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
542-760 |
5.87e-68 |
|
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: 223.91 E-value: 5.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIR-YGRVTagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGEYS--DEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
473-784 |
1.62e-66 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 231.92 E-value: 1.62e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 473 FVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLkeetevkDLPGAG------PLrfQKGRIEF 546
Cdd:PRK10790 273 FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM-------DGPRQQygnddrPL--QSGRIDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQD 626
Cdd:PRK10790 344 DNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFNDTIADNIRYGRvTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDE 706
Cdd:PRK10790 424 PVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 707 ATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEE 784
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
280-775 |
7.47e-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: 226.93 E-value: 7.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 280 VSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIADrgTSSVTGLLSYLVFNVIPTLAdIIIGIIY 358
Cdd:TIGR01193 212 LSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVsRFTD--ASSIIDALASTILSLFLDMW-ILVIVGL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 359 FSMFFNAWFGLIVFLCMSLYltlTIVVTEWRTKFRRaMNT---QENATRARAV-DSLLNFETVKYYNAES-------YEV 427
Cdd:TIGR01193 289 FLVRQNMLLFLLSLLSIPVY---AVIIILFKRTFNK-LNHdamQANAVLNSSIiEDLNGIETIKSLTSEAeryskidSEF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 428 ERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLlagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRM 507
Cdd:TIGR01193 365 GDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTG-------AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 508 IQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTIL 587
Cdd:TIGR01193 438 LQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 588 RLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYG-RVTAGNDEVEAAAQAAGIHDAIMAF 666
Cdd:TIGR01193 518 KLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENM 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 667 PEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcANRTTIVVAHRLSTVVNAD 746
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSD 676
|
490 500
....*....|....*....|....*....
gi 1169100883 747 QILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| MTABC_N |
pfam16185 |
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ... |
6-209 |
8.99e-61 |
|
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five transmembrane helices of eukaryotic mitochondrial ABC-transporters.
Pssm-ID: 465049 Cd Length: 244 Bit Score: 205.59 E-value: 8.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 6 NYCEAEGPVGPAWMQDGLSPCFFFTLVPSTRMALGTLALVLALPCRRRErpagADSLSWGAGPRISPYVLQLLLATLQAA 85
Cdd:pfam16185 1 SYCEPNVSLTPVWVDHGLSPCFYDTLVPSVLLGFLLLFGTIQLIMYRKY----GTPMEPKFIPRSRLYVLQLFLALLLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 86 LPLAGLAGRVGTARGAPLPSYLLLASVLESLAGACGLWLLVVERSQARQRLAMgiwikFRHSPGLLLLWTVAFAAENLAL 165
Cdd:pfam16185 77 LALARFILRAALIGGGRLYGYMVLYACLSLLAWPFSLALLRLERRYALPSLPT-----RGHGLVLLLFWTLAFVAENLAF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 166 VSWNSPQWWWARADLGQQV-------------------------------------------------RSAAQQSTWRDF 196
Cdd:pfam16185 152 VSWNSPDWWWGLETLSDQVefglfvvryvctlllfvlglkapglprkpymllinederdvessqpllgDSEENGSTWRNF 231
|
250
....*....|...
gi 1169100883 197 GRKLRLLSGYLWP 209
Cdd:pfam16185 232 GKKLRLLWPYLWP 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
520-777 |
4.14e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 202.36 E-value: 4.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 520 DLLKEETEVKdLPGAGPLRFQKGRIEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS 598
Cdd:PRK11160 316 EITEQKPEVT-FPTTSTAAADQVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 599 GCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIhDAIMAFPEGYRTQVGERG 678
Cdd:PRK11160 395 GEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILK-APgIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHdAP-LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
250 260
....*....|....*....|
gi 1169100883 758 ERGRHEALLSRGGVYADMWQ 777
Cdd:PRK11160 553 EQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
540-761 |
2.08e-53 |
|
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: 183.77 E-value: 2.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYA-DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS 618
Cdd:cd03369 3 EHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQDTVLFNDTIADNI-RYGRVTagNDEVEAAaqaagihdaimafpegyrTQVGERGLKLSGGEKQRVAIARTILK 697
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGR 761
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
544-756 |
1.16e-52 |
|
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: 180.49 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:cd03246 1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIrygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVNADQILVIKDGCI 756
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
495-784 |
1.58e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 192.75 E-value: 1.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 495 YMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEV-----KDLPGAGPLRfqkgrIEFENVHFSYADGRETLQDVSFTVMP 569
Cdd:PRK11174 301 YQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHpqqgeKELASNDPVT-----IEAEDLEILSPDGKTLAGPLNFTLPA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 570 GQTLALVGPSGAGKSTILRLLFRF--YdisSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGN 647
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 648 DEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC 727
Cdd:PRK11174 453 EQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS 532
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 728 ANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMwqLQQGQEE 784
Cdd:PRK11174 533 RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL--LAHRQEE 587
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
516-739 |
1.20e-50 |
|
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: 186.03 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 516 ENMFDLLKEETEVKD--LPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEgsAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQ 673
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 674 VGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRL 739
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
544-768 |
8.86e-49 |
|
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: 171.75 E-value: 8.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagihDAIMAfpegyrtQVGERGLK------LSGGEKQRVAIARTI 695
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGPENLGLPREEIRERV----EEALE-------LVGLEHLAdrppheLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVV-NADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFSD 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
544-756 |
1.63e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADNI----RYGRVTAGNDEVEAAAQAAGIHDAIMAfpegyrTQVGErglkLSGGEKQRVAIARTILKAP 699
Cdd:COG4619 80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILD------KPVER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH------RLstvvnADQILVIKDGCI 756
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
544-758 |
1.02e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 168.69 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLRSHI 620
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYG-RVT-AGNDEVEAAAQAA----GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPlRVTgKSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVNADQ-ILVIKDGCIVE 758
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
545-754 |
1.33e-46 |
|
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: 165.33 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagihdaimafpEGYRTQVGERGLK------LSGGEKQRVAIARTI 695
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLGLPEEEIEERV-----------EEALELVGLEGLRdrspftLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDG 754
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
544-761 |
5.84e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.06 E-value: 5.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---- 616
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRV 689
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARellervGLGDRLDHRPS-----------QLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGR 761
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
544-768 |
2.23e-45 |
|
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: 170.47 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET----LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---L 616
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQD---------TVLfnDTIADNIR-YGRVTAG--NDEVEAAAQAAGIHDAIM-AFPegyrtqvGErglkLSG 683
Cdd:COG1123 341 RRRVQMVFQDpysslnprmTVG--DIIAEPLRlHGLLSRAerRERVAELLERVGLPPDLAdRYP-------HE----LSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*...
gi 1169100883 761 RHEALLSR 768
Cdd:COG1123 488 PTEEVFAN 495
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
544-760 |
4.15e-45 |
|
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: 159.79 E-value: 4.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRSHIGV 622
Cdd:cd03247 1 LSINNVSFSYPEQEQQvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIrygrvtagndeveaaaqaagihdaimafpegyrtqvgerGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
543-767 |
4.93e-45 |
|
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: 162.14 E-value: 4.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVL-FNDTIADNIRYGR---------VTAGNDE-VEAAAQAAGIHDaiMAfpegyrtqvgERGL-KLSGGEKQRVA 690
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREaVEEALERTGLEH--LA----------DRPVdELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
544-760 |
5.89e-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: 161.19 E-value: 5.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDI-----SSGCIRIDGQDI--SQVTQASL 616
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFNDTIADNIRYG-------RVTAGNDEVEAAAQAAGIHDaimafpegyrtQVGER--GLKLSGGEKQ 687
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD-----------EVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAH------RLstvvnADQILVIKDGCIVERG 760
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
544-768 |
3.10e-44 |
|
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: 159.97 E-value: 3.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY---ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQD---------TVlfNDTIADNIRYGRVTAGNDEVEAAAQAAGIhdaimafPEGYRTQvgeRGLKLSGGEKQRVAI 691
Cdd:COG1124 82 QMVFQDpyaslhprhTV--DRILAEPLRIHGLPDREERIAELLEQVGL-------PPSFLDR---YPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLStVVN--ADQILVIKDGCIVERGRHEALLS 767
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLA 228
|
.
gi 1169100883 768 R 768
Cdd:COG1124 229 G 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
560-709 |
3.30e-44 |
|
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: 156.27 E-value: 3.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFND-TIADNI 638
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 639 RYGRVTAGNDEVEAAAQAAGIHDAiMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATS 709
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
544-770 |
1.10e-43 |
|
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: 158.10 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAsLRSHIGVV 623
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAiMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGII 702
Cdd:COG4555 80 PDERGLYdRLTVRENIRYFAELYGLFDEELKKRIEELIEL-LGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
541-772 |
3.36e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 169.82 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 541 KGRIEFENVHFSYADGRET--LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDI---------------------- 596
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 597 --------------------------------SSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVT 644
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 645 AGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLA 724
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 725 --KVCANRTTIVVAHRLSTVVNADQILVI----KDGCIVE-RGRHEALLS-RGGVY 772
Cdd:PTZ00265 1403 diKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSvQDGVY 1458
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
544-760 |
5.95e-43 |
|
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: 154.98 E-value: 5.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRtqvgeRGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNR-----YPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
544-754 |
6.19e-43 |
|
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: 154.96 E-value: 6.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---- 616
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRV 689
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEellervGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
544-760 |
7.80e-43 |
|
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: 155.36 E-value: 7.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---R 617
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQD--TVLfND--TIADNIRYGRVTAGNDEVEAAAQAAGIHDAIM-----AFPEGYRTQvgerglkLSGGEKQR 688
Cdd:cd03257 82 KEIQMVFQDpmSSL-NPrmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYPHE-------LSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
544-768 |
1.81e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.45 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAsLRSHIGVV 623
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAImafpegyRTQVGerglKLSGGEKQRVAIARTIL 696
Cdd:COG1131 79 PQEPALYPDlTVRENLRFFARLYGLPRKEARERIDellelfGLTDAA-------DRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
544-766 |
2.42e-42 |
|
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: 154.37 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHI 620
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNI-----RYGRVTAgnDEVEAAA----QAAGIHDAIMAFPegyrtqvGErglkLSGGEKQRVA 690
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLSE--AEIRELVleklELVGLPGAADKMP-------SE----LSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 691 IARTILKAPGIILLDEATSALD--TSNE-----RAIQASLakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRH 762
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpiTSAVideliRELRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....
gi 1169100883 763 EALL 766
Cdd:COG1127 227 EELL 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
543-753 |
7.70e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 165.59 E-value: 7.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYaDGR---ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQASLRS 618
Cdd:PTZ00265 382 KIQFKNVRFHY-DTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQDTVLFNDTIADNIRYG-------------------------------RVTAGND------------------- 648
Cdd:PTZ00265 461 KIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscRAKCAGDlndmsnttdsneliemrkn 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 649 -------EVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQA 721
Cdd:PTZ00265 541 yqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270
....*....|....*....|....*....|....
gi 1169100883 722 SL--AKVCANRTTIVVAHRLSTVVNADQILVIKD 753
Cdd:PTZ00265 621 TInnLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
545-754 |
8.65e-42 |
|
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: 149.70 E-value: 8.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVP 624
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QdtvlfndtiadnirygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGIILL 704
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 705 DEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVVNA-DQILVIKDG 754
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
544-768 |
6.18e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.14 E-value: 6.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQASLRSHIG 621
Cdd:COG1126 2 IEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFND-TIADNIRYGRVTAGN---DEVEAAAQAA----GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:COG1126 81 MVFQQFNLFPHlTVLENVTLAPIKVKKmskAEAEERAMELlervGLADKADAYPA-----------QLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALD--TSNE--RAIQaSLAKvcANRTTIVVAHRLS---TVvnADQILVIKDGCIVERGRHEALL 766
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDpeLVGEvlDVMR-DLAK--EGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFF 224
|
..
gi 1169100883 767 SR 768
Cdd:COG1126 225 EN 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
544-768 |
1.90e-40 |
|
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: 148.50 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---R 617
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVA 690
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLellelvGLEDKADAYPA-----------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNR----TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 1169100883 766 LSR 768
Cdd:cd03258 229 FAN 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
544-757 |
2.89e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 148.67 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHI 620
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQD-------TVLfndtiaDNI---RYGRVTA--------GNDEVEAAAQAAgihdaimafpegyrTQVG------E 676
Cdd:COG3638 83 GMIFQQfnlvprlSVL------TNVlagRLGRTSTwrsllglfPPEDRERALEAL--------------ERVGladkayQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 677 RGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKD 753
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRD 222
|
....
gi 1169100883 754 GCIV 757
Cdd:COG3638 223 GRVV 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
489-775 |
5.15e-40 |
|
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: 159.73 E-value: 5.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 489 TYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVK-DLPGAGPLRF--QKGRIEFENVHFSYADGRE-TLQDVS 564
Cdd:TIGR00957 1227 SYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGwpPRGRVEFRNYCLRYREDLDlVLRHIN 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 565 FTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIR-YGRV 643
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 644 TagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASL 723
Cdd:TIGR00957 1387 S--DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 724 AKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADM 775
Cdd:TIGR00957 1465 RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
544-751 |
1.42e-39 |
|
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: 145.69 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHI 620
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFN-DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEellelvGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIV-VAHRLSTVVN-ADQILVI 751
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTHDIDEAVFlADRVVVL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
544-768 |
1.99e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.14 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGR-ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS---SGCIRIDGQDISQVTQASLRSH 619
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQD--TVLFNDTIADNI----RYGRVTAGN--DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAI 691
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIaealENLGLSRAEarARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
544-760 |
4.40e-39 |
|
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: 144.95 E-value: 4.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHI 620
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNI-----RYGRVTAG--NDEVEAAAQAAGIHDAIMAFPegyrtqvGErglkLSGGEKQRVAIA 692
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafplrEHTRLSEEeiREIVLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 693 RTILKAPGIILLDEATSALD--TSNE-----RAIQASLakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDpiASGViddliRSLKKEL-----GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
544-765 |
9.38e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.08 E-value: 9.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHIGVV 623
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ-------------DTVLFNdtiadniRYGRV-------TAGNDEVEAAAQAAGIhdaimafpEGYR-TQVGErglkLS 682
Cdd:COG1121 81 PQraevdwdfpitvrDVVLMG-------RYGRRglfrrpsRADREAVDEALERVGL--------EDLAdRPIGE----LS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 683 GGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVV-NADQILVIKDGCIVERG 760
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVReYFDRVLLLNRGLVAHGP 221
|
....*
gi 1169100883 761 RHEAL 765
Cdd:COG1121 222 PEEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
545-760 |
1.01e-38 |
|
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: 141.80 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVP 624
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QdtvlfndtiadnirygrvtagndeveaAAQAAGIHDaiMAfpegyrtqvgERGLK-LSGGEKQRVAIARTILKAPGIIL 703
Cdd:cd03214 80 Q---------------------------ALELLGLAH--LA----------DRPFNeLSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
544-761 |
1.27e-38 |
|
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: 142.93 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLRSHI 620
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRVTAG------NDEVEAAAQAAGIHDAIMAFPEGyrtqvgerglkLSGGEKQRVAIAR 693
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEVTGvppreiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVikdgCIVERGR 761
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRV----IALERGK 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
544-768 |
1.41e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 147.17 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRsHIGVV 623
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKR-NVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYG-RVtagnDEVEAAAQAAGIHDAImafpegyrTQVGERGL------KLSGGEKQRVAIARTI 695
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGlRM----RGVPKAEIRARVAELL--------ELVGLEGLadryphQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 696 LKAPGIILLDEATSALD------TSNE-RAIQASLakvcaNRTTIVVAHRLS---TVvnADQILVIKDGCIVERGRHEAL 765
Cdd:COG3842 151 APEPRVLLLDEPLSALDaklreeMREElRRLQREL-----GITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
...
gi 1169100883 766 LSR 768
Cdd:COG3842 224 YER 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
544-754 |
1.68e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 141.17 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS--LRSHIG 621
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLF-NDTIADNIRYGrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPG 700
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
544-754 |
2.37e-38 |
|
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: 141.45 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE----TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGciridgqdisqvtQASLRSH 619
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------------SVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDTVLFNDTIADNI---------RYGRVtagndeVEAAAqaagIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVA 690
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgkpfdeeRYEKV------IKACA----LEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 691 IARTILKAPGIILLDEATSALD--TSN---ERAIQASLAKvcaNRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDahVGRhifENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
543-750 |
4.68e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 142.54 E-value: 4.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvtqasLRSH 619
Cdd:COG1116 7 ALELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDTVLFN-DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPegyrtqvGErglkLSGGEKQRVAIA 692
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARellelvGLAGFEDAYP-------HQ----LSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH------RLstvvnADQILV 750
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVV 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
517-770 |
2.49e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 151.28 E-value: 2.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 517 NMFDLLKEETEV--KDLPGAG-PLRfqkGRIEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFR 592
Cdd:PLN03232 1208 NYIDLPSEATAIieNNRPVSGwPSR---GSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 593 FYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIryGRVTAGND-EVEAAAQAAGIHDAIMAFPEGYR 671
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI--DPFSEHNDaDLWEALERAHIKDVIDRNPFGLD 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 672 TQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVI 751
Cdd:PLN03232 1363 AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVL 1442
|
250
....*....|....*....
gi 1169100883 752 KDGCIVERGRHEALLSRGG 770
Cdd:PLN03232 1443 SSGQVLEYDSPQELLSRDT 1461
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
544-761 |
2.96e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 142.91 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILR---LLFRFydiSSGCIRIDGQDISQVTQASL- 616
Cdd:COG1135 2 IELENLSKTFPTKGGPvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLERP---TSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 --RSHIGVVPQDtvlFN----DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGG 684
Cdd:COG1135 79 aaRRKIGMIFQH---FNllssRTVAENVALPLEIAGVPKAEIRKRVAellelvGLSDKADAYPS-----------QLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNRT---TIVVA-HRLStVVN--ADQILVIKDGCIVE 758
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRElglTIVLItHEMD-VVRriCDRVAVLENGRIVE 221
|
...
gi 1169100883 759 RGR 761
Cdd:COG1135 222 QGP 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
544-765 |
3.23e-37 |
|
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: 139.63 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHI 620
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRVTAGN-----------DEVEAAAQA---AGIHDaiMAFpegyrtqvgERGLKLSGGE 685
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRRStwrslfglfpkEEKQRALAAlerVGLLD--KAY---------QRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 686 KQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVV-NADQILVIKDGCIVERGRH 762
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPP 229
|
...
gi 1169100883 763 EAL 765
Cdd:cd03256 230 AEL 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
532-775 |
5.80e-37 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 150.31 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 532 PGAGPLRFQKGRIEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 610
Cdd:PTZ00243 1297 TSAAPHPVQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 611 VTQASLRSHIGVVPQDTVLFNDTIADNIRyGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVA 690
Cdd:PTZ00243 1377 YGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMC 1455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 691 IARTILK-APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGR-HEALLSR 768
Cdd:PTZ00243 1456 MARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSpRELVMNR 1535
|
....*..
gi 1169100883 769 GGVYADM 775
Cdd:PTZ00243 1536 QSIFHSM 1542
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
542-773 |
1.53e-36 |
|
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: 138.50 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIRYGRvTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPG 700
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR-GGVYA 773
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFA 250
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
544-756 |
4.42e-36 |
|
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: 134.06 E-value: 4.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRSHIGVV 623
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNirygrvtagndeveaaaqaagihdaimafpegyrtqvgergLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03230 79 PEEPSLYENlTVREN-----------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCI 756
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
544-767 |
6.80e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.44 E-value: 6.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK13548 3 LEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVL-FNDTIADNIRYGRV--TAGNDEVEAAAQAAgihdaiMAfpegyrtQVGERGLK------LSGGEKQRVAIART 694
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAA------LA-------QVDLAHLAgrdypqLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 695 IL------KAPGIILLDEATSALDTSNERAIqASLAKVCANR---TTIVVAHRLstvvN-----ADQILVIKDGCIVERG 760
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHV-LRLARQLAHErglAVIVVLHDL----NlaaryADRIVLLHQGRLVADG 223
|
....*..
gi 1169100883 761 RHEALLS 767
Cdd:PRK13548 224 TPAEVLT 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
545-752 |
7.99e-36 |
|
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: 134.58 E-value: 7.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHIGVVP 624
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QDTVL---FNDTIADNIRYGRVTAGN----------DEVEAAAQAAGIhdaimafpEGYRT-QVGErglkLSGGEKQRVA 690
Cdd:cd03235 75 QRRSIdrdFPISVRDVVLMGLYGHKGlfrrlskadkAKVDEALERVGL--------SELADrQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVVN-ADQILVIK 752
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
544-756 |
1.10e-35 |
|
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: 134.19 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA--SLRSHIG 621
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLF-NDTIADNIRYGRVTAGN---DEVEAAAQAA----GIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIAR 693
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVKGmskAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 694 TILKAPGIILLDEATSALD--TSNE-RAIQASLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCI 756
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDpeLVGEvLDVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
544-768 |
3.00e-35 |
|
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: 133.97 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIryGRVTAGNDEVEAAAQAAGihDAIMAF----PEGYRTQVGErglKLSGGEKQRVAIARTILKA 698
Cdd:cd03295 81 IQQIGLFpHMTVEENI--ALVPKLLKWPKEKIRERA--DELLALvgldPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKV--CANRTTIVVAHRL-STVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
534-760 |
3.20e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 134.39 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 534 AGPLRFQKGRIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDI 608
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 609 --SQVTQASLRSHIGVVPQDTVLFNDTIADNIRYG-RVtAGN------DE-VEAAAQAAGIHDaimafpegyrtQVGER- 677
Cdd:COG1117 81 ydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlRL-HGIkskselDEiVEESLRKAALWD-----------EVKDRl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 678 ---GLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAH------RLStvvnaDQI 748
Cdd:COG1117 149 kksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYT 223
|
250
....*....|..
gi 1169100883 749 LVIKDGCIVERG 760
Cdd:COG1117 224 AFFYLGELVEFG 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
544-761 |
1.14e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.19 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYG----RVTAG--NDEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIART 694
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkKVPPKkmKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQA---SLAKVcANRTTIVVAHRLSTVVNADQILVIKDGCIVERGR 761
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKimvDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
516-777 |
2.01e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 142.18 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 516 ENMFDLLKEETEVKDLPGAGPLRFQ----------KGRIEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKS 584
Cdd:PLN03130 1200 ENSLNAVERVGTYIDLPSEAPLVIEnnrpppgwpsSGSIKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKS 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 585 TILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIryGRVTAGND-EVEAAAQAAGIHDAI 663
Cdd:PLN03130 1280 SMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL--DPFNEHNDaDLWESLERAHLKDVI 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 664 MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLA---KVCanrTTIVVAHRLS 740
Cdd:PLN03130 1358 RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIReefKSC---TMLIIAHRLN 1434
|
250 260 270
....*....|....*....|....*....|....*...
gi 1169100883 741 TVVNADQILVIKDGCIVERGRHEALLSR-GGVYADMWQ 777
Cdd:PLN03130 1435 TIIDCDRILVLDAGRVVEFDTPENLLSNeGSAFSKMVQ 1472
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
544-768 |
5.18e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.40 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAG------NDEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTI 695
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGPVNMGldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
547-757 |
9.84e-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: 128.53 E-value: 9.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtQASLRSHIGVVPQD 626
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 T--VLFNDTIADNIRYG--RVTAGNDEVEAAAQAAGIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03226 80 VdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 703 LLDEATSALDTSNERAIqASLAKVCANRTT--IVVAHR---LSTVvnADQILVIKDGCIV 757
Cdd:cd03226 149 IFDEPTSGLDYKNMERV-GELIRELAAQGKavIVITHDyefLAKV--CDRVLLLANGAIV 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
542-757 |
1.82e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.12 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRsHIG 621
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL-PPKDR-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLF-NDTIADNIRYG----RVTAG--NDEVEAAAQAAGIhdaimafpegyrTQVGERglK---LSGGEKQRVAI 691
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrKVPKAeiDRRVREAAELLGL------------EDLLDR--KpkqLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 692 ARTILKAPGIILLDEATSALD------TSNE-RAIQASLakvcaNRTTIVVAH------RLstvvnADQILVIKDGCIV 757
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRIQ 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
560-766 |
4.73e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 128.53 E-value: 4.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL----RSHIGVVPQDTVLF-NDTI 634
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAealelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 709 SALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALL 766
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
544-768 |
5.31e-33 |
|
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: 129.79 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQ---DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYD---ISSGCIRIDGQDISQVTQASLR 617
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 S----HIGVVPQD---------TVLfnDTIADNIRYGRVtAGNDEVEAAAQAA----GIHDAimafpegyrtqvgERGLK 680
Cdd:COG0444 82 KirgrEIQMIFQDpmtslnpvmTVG--DQIAEPLRIHGG-LSKAEARERAIELlervGLPDP-------------ERRLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 -----LSGGEKQRVAIARTILKAPGIILLDEATSALDTSneraIQAS----LAKVCANR-TTIV-VAHRLSTVVN-ADQI 748
Cdd:COG0444 146 rypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVT----IQAQilnlLKDLQRELgLAILfITHDLGVVAEiADRV 221
|
250 260
....*....|....*....|
gi 1169100883 749 LVIKDGCIVERGRHEALLSR 768
Cdd:COG0444 222 AVMYAGRIVEEGPVEELFEN 241
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
544-767 |
6.04e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.92 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG4559 2 LEAENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVL-FNDTIADNIRYGRVTAGNDeveaAAQAAGIHDAIMAfpegyrtQVGERGLK------LSGGEKQRVAIAR--- 693
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALGRAPHGSS----AAQDRQIVREALA-------LVGLAHLAgrsyqtLSGGEQQRVQLARvla 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 ----TILKAPGIILLDEATSALDTSNERAIqASLAKVCANRTTIVVA--HRLstvvN-----ADQILVIKDGCIVERGRH 762
Cdd:COG4559 150 qlwePVDGGPRWLFLDEPTSALDLAHQHAV-LRLARQLARRGGGVVAvlHDL----NlaaqyADRILLLHQGRLVAQGTP 224
|
....*
gi 1169100883 763 EALLS 767
Cdd:COG4559 225 EEVLT 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
544-769 |
8.30e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.21 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK13635 6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYGRVTAG--NDE----VEAAAQAAGIHDaiMAFPEGYRtqvgerglkLSGGEKQRVAIART 694
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGLENIGvpREEmverVDQALRQVGMED--FLNREPHR---------LSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
544-768 |
2.24e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.64 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYadGRETLQdVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRShIGVV 623
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYG-----RVTAGN-DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTIL 696
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
544-761 |
2.37e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.77 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGR---ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS-- 618
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 -HIGVVPQDtvlFN----DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPEgyrtqvgerglKLSGGEKQ 687
Cdd:PRK11153 82 rQIGMIFQH---FNllssRTVFDNVALPLELAGTPKAEIKARVTellelvGLSDKADRYPA-----------QLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNRT---TIV-VAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRElglTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
560-768 |
5.39e-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: 124.37 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVVPQDTVLF-NDTIADNI 638
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 639 RYGRVTAGNDEVEaaaqaagIHDAIMAFPE--GYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNE 716
Cdd:cd03299 93 AYGLKKRKVDKKE-------IERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 717 RAIQASLAKV--CANRTTIVVAHRLSTV-VNADQILVIKDGCIVERGRHEALLSR 768
Cdd:cd03299 166 EKLREELKKIrkEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
544-769 |
2.21e-31 |
|
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: 123.69 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQasLRSH 619
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWE--IRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQ--DTVLFNDTIADNIRYGRVTAG--NDE----VEAAAQAAGIhdaimafpEGYRTQVGERglkLSGGEKQRVAI 691
Cdd:TIGR04520 79 VGMVFQnpDNQFVGATVEDDVAFGLENLGvpREEmrkrVDEALKLVGM--------EDFRDREPHL---LSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRG 769
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
544-768 |
2.77e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.64 E-value: 2.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqVTQASLRSHIGVV 623
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYG-RVtAGNDEVEAAA---------QAAGIHDAimafpegYRTQvgerglkLSGGEKQRVAIA 692
Cdd:COG1118 81 FQHYALFpHMTVAENIAFGlRV-RPPSKAEIRArveellelvQLEGLADR-------YPSQ-------LSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH------RLstvvnADQILVIKDGCIVERGRHEA 764
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDE 220
|
....
gi 1169100883 765 LLSR 768
Cdd:COG1118 221 VYDR 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
543-760 |
3.75e-31 |
|
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: 120.73 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENV-----HFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL--FRFYDISSGCIRIDGQDISQvtqAS 615
Cdd:cd03213 3 TLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQDTVLF-NDTIADNIRYgrvtagndeveaaaqAAGIhdaimafpegyrtqvgeRGLklSGGEKQRVAIART 694
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMF---------------AAKL-----------------RGL--SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAHRLSTVV--NADQILVIKDGCIVERG 760
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
231-498 |
4.34e-31 |
|
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: 123.14 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLkflqgGGTGSTGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHEL 310
Cdd:pfam00664 13 AISPAFPLVLGRILDVLLPDGDPETQALNVYSLALL-----LLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 311 SLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIyFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRT 390
Cdd:pfam00664 88 PMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGII-VMFYYGWKLTLVLLAVLPLYILVSAVFAKILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 391 KFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLC 470
Cdd:pfam00664 167 KLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFG 246
|
250 260
....*....|....*....|....*...
gi 1169100883 471 AYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:pfam00664 247 AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
544-760 |
9.75e-31 |
|
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: 119.99 E-value: 9.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTlALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAsLRSHIGVV 623
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQD-------TVL-FNDTIA--DNIRYGRVTAgndEVEAAAQAAGIHDAimafpegYRTQVGerglKLSGGEKQRVAIAR 693
Cdd:cd03264 78 PQEfgvypnfTVReFLDYIAwlKGIPSKEVKA---RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTV-VNADQILVIKDGCIVERG 760
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
544-770 |
1.77e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 121.38 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE--TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAG------NDEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIAR 693
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENKGipheemKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
544-767 |
1.85e-30 |
|
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: 119.46 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqaSLRSH---- 619
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-----GLPPHerar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 --IGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAqaagihDAIMA-FP---EGYRTQVGErglkLSGGEKQRVAIA 692
Cdd:cd03224 75 agIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARL------ERVYElFPrlkERRKQLAGT----LSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV----AHRLSTVvnADQILVIKDGCIVERGRHEALLS 767
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
560-768 |
2.21e-30 |
|
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: 126.34 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQA---SLRSHIGVVPQD------ 626
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDpfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 ---TVLfnDTIADNIRYGRVTAGNDEVEAAAQAA----GIHDAIMA-FP-EgyrtqvgerglkLSGGEKQRVAIART-IL 696
Cdd:COG4172 377 prmTVG--QIIAEGLRVHGPGLSAAERRARVAEAleevGLDPAARHrYPhE------------FSGGQRQRIAIARAlIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 697 KaPGIILLDEATSALDtsneRAIQAS----LAKVCANR--TTIVVAHRLStVVNA--DQILVIKDGCIVERGRHEALLSR 768
Cdd:COG4172 443 E-PKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
560-767 |
8.37e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 8.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHIGVVPQD---------T 627
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDpyaslnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VlfNDTIADNIRYGRVTAGnDEVEAAAQaagihdAIMAfpegyrtQVgerGLK----------LSGGEKQRVAIARTILK 697
Cdd:COG4608 114 V--GDIIAEPLRIHGLASK-AERRERVA------ELLE-------LV---GLRpehadrypheFSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 698 APGIILLDEATSALDTSneraIQA-------------SLakvcanrTTIVVAHRLStVVN--ADQILVIKDGCIVERG-- 760
Cdd:COG4608 175 NPKLIVCDEPVSALDVS----IQAqvlnlledlqdelGL-------TYLFISHDLS-VVRhiSDRVAVMYLGKIVEIApr 242
|
250
....*....|....*..
gi 1169100883 761 -------RH---EALLS 767
Cdd:COG4608 243 delyarpLHpytQALLS 259
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
544-761 |
1.66e-29 |
|
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: 117.34 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVTAGNDEveaAAQAAGIHDAI-MAFPEGYRtqvGERGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGLRLKKLPK---AEIKERVAEALdLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLS-TVVNADQILVIKDGCIVERGR 761
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
543-753 |
2.01e-29 |
|
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: 116.04 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRSHIGV 622
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFND-TIADNIRY----GRVTAGNDEVEAAAQAAGIhdaimafpEGYR-TQVGerglKLSGGEKQRVAIARTIL 696
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGL--------AGLAdLPVR----QLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKD 753
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
544-760 |
4.40e-29 |
|
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: 115.54 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQ---DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRSHI 620
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRY-GRV-----TAGNDEVEAAAQAAGIHDAImafpegyrtqvGERGLKLSGGEKQRVAIAR 693
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfAGLyglkgDELTARLEELADRLGMEELL-----------DRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
542-759 |
4.68e-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: 125.02 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYA-DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQASLRSHI 620
Cdd:TIGR01271 1216 GQMDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIR-YGRVTagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDpYEQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIkDGCIVER 759
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVI-EGSSVKQ 1431
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
544-760 |
8.26e-29 |
|
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: 114.66 E-value: 8.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRShIGVV 623
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRD-IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDE------VEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTIL 696
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGLKLRKVPKdeiderVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAH-RLSTVVNADQILVIKDGCIVERG 760
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
544-764 |
8.76e-29 |
|
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: 115.22 E-value: 8.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLR 617
Cdd:COG4181 9 IELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 S-HIGVVPQD-------TVLFNdtiadnirygrVT-----AGNDEVEAAAQAA----GIHDAIMAFPEGyrtqvgerglk 680
Cdd:COG4181 89 ArHVGFVFQSfqllptlTALEN-----------VMlplelAGRRDARARARALlervGLGHRLDHYPAQ----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR-TTIV-VAHRLSTVVNADQILVIKDGCIVE 758
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVlVTHDPALAARCDRVLRLRAGRLVE 226
|
....*.
gi 1169100883 759 RGRHEA 764
Cdd:COG4181 227 DTAATA 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
553-739 |
9.39e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.64 E-value: 9.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 553 YADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQASLRSHIGVVPQ 625
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFNDTIADNIRYGRVTAG-------NDEVEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGikdkqvlDEAVEKSLKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRL 739
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
542-793 |
1.01e-28 |
|
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: 116.49 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYAD-GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISsGCIRIDGQDISQVTQASLRSHI 620
Cdd:cd03289 1 GQMTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFNDTIADNIR-YGRVTagNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVY------A 773
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFkqaispS 237
|
250 260
....*....|....*....|
gi 1169100883 774 DMWQLQQGQEETSEDTKPQT 793
Cdd:cd03289 238 DRLKLFPRRNSSKSKRKPRP 257
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
544-766 |
1.10e-28 |
|
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: 115.57 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGC-IRIDGQDISQVTQASLRSHIGV 622
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 V---------PQDTVL------FNDTIAdniRYGRVTagnDEVEAAAqaagihDAIMAFpegyrtqVGERGLK------L 681
Cdd:COG1119 83 VspalqlrfpRDETVLdvvlsgFFDSIG---LYREPT---DEQRERA------RELLEL-------LGLAHLAdrpfgtL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 682 SGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR-TTIV-VAHRLSTVVNA-DQILVIKDGCIVE 758
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
....*...
gi 1169100883 759 RGRHEALL 766
Cdd:COG1119 224 AGPKEEVL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
560-758 |
2.16e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.74 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGVVPQDTVLFND-TIADN 637
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 638 IRYGR--VTAG---NDEVEAAAQAA----GIH-DAimafpegyRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:COG1129 100 IFLGRepRRGGlidWRAMRRRARELlarlGLDiDP--------DTPVGD----LSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 708 TSALdTSNERAI-QASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:COG1129 168 TASL-TEREVERlFRIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
544-769 |
4.26e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.46 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY-ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYG---RVTAGNDEVEAAAQAagIHDAIMAFPEGYRTQvgerglKLSGGEKQRVAIARTILK 697
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGlenHAVPYDEMHRRVSEA--LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
544-757 |
6.51e-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: 110.21 E-value: 6.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGV 622
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQdtvlfndtiadnirygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGII 702
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 703 LLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIV 757
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
544-774 |
9.55e-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: 120.82 E-value: 9.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqaslrshIGV 622
Cdd:TIGR00957 637 ITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADNIRYGRVTAGNdEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILFGKALNEK-YYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 703 LLDEATSALDTSNERAIQASL---AKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYAD 774
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE 857
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
545-767 |
1.17e-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: 112.00 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqaSLRSH----- 619
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-----GLPPHriarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 -IGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQaagihDAIMA-FP--EGYRTQvgeRGLKLSGGEKQRVAIART 694
Cdd:COG0410 79 gIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADL-----ERVYElFPrlKERRRQ---RAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV----AHRLSTVvnADQILVIKDGCIVERGRHEALLS 767
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
544-756 |
1.59e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.04 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRsHIGVV 623
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYG----RVtaGNDEVEAAaqaagIHDAI-MAFPEGYRTQvgeRGLKLSGGEKQRVAIARTILK 697
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqKT--PAAEITPR-----VMEALrMVQLEEFAQR---KPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 698 APGIILLDEATSALD------TSNE-RAIQASLakvcaNRTTIVVAH----RLSTvvnADQILVIKDGCI 756
Cdd:PRK09452 162 KPKVLLLDESLSALDyklrkqMQNElKALQRKL-----GITFVFVTHdqeeALTM---SDRIVVMRDGRI 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
544-765 |
1.80e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQA----SLR 617
Cdd:COG4161 3 IQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVV-------PQDTVLFNDTIADNirygRVtAGNDEVEAAAQAAGI------HDAIMAFPegyrtqvgergLKLSGG 684
Cdd:COG4161 82 QKVGMVfqqynlwPHLTVMENLIEAPC----KV-LGLSKEQAREKAMKLlarlrlTDKADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTsnerAIQASLAKVCANR-----TTIVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDP----EITAQVVEIIRELsqtgiTQVIVTHEVEFARKvASQVVYMEKGRIIE 221
|
....*..
gi 1169100883 759 RGRHEAL 765
Cdd:COG4161 222 QGDASHF 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
544-717 |
2.07e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.96 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK10247 8 LQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADN------IRygrvtagNDEVEAAAQAAGIhdAIMAFPEgyrTQVGERGLKLSGGEKQRVAIARTILK 697
Cdd:PRK10247 87 AQTPTLFGDTVYDNlifpwqIR-------NQQPDPAIFLDDL--ERFALPD---TILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180
....*....|....*....|
gi 1169100883 698 APGIILLDEATSALDTSNER 717
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKH 174
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
564-767 |
2.52e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.83 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 564 SFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVVPQDTVLFND-TIADNIRYG- 641
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 642 ----RVTAGN-DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNE 716
Cdd:PRK10771 97 npglKLNAAQrEKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 717 RAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
548-760 |
2.68e-27 |
|
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: 110.46 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGRETLqDVSFTVmPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdISQVTQASL-----RSHIGV 622
Cdd:cd03297 3 CVDIEKRLPDFTL-KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLF-NDTIADNIRYGRVTAGNDE----VEAAAQAAGIhdaimafpegyrTQVGERG-LKLSGGEKQRVAIARTIL 696
Cdd:cd03297 80 VFQQYALFpHLNVRENLAFGLKRKRNREdrisVDELLDLLGL------------DHLLNRYpAQLSGGEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03297 148 AQPELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
544-760 |
4.17e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL--RSHIG 621
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAG--NDEVEA----AAQAAGIhdaimafpEGYRTQVGERglkLSGGEKQRVAIAR 693
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGPLNLGlsKEEVEKrvkeALKAVGM--------EGFENKPPHH---LSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTV-VNADQILVIKDGCIVERG 760
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
560-754 |
6.74e-27 |
|
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: 109.45 E-value: 6.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI--DGQDISqVTQAS------LRSH-IGVVPQdtvlF 630
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVD-LAQASpreilaLRRRtIGYVSQ----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 NDTIAdnirygRVTA-----------GNDEVEAAAQAAgihdAIMAfpegyRTQVGERGLKL-----SGGEKQRVAIART 694
Cdd:COG4778 102 LRVIP------RVSAldvvaepllerGVDREEARARAR----ELLA-----RLNLPERLWDLppatfSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDG 754
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
544-712 |
8.69e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.19 E-value: 8.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---LRSHI 620
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRVTAGNDE------VEAAAQAAGIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIAR 693
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLIIAGASGddirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170
....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALD 712
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD 169
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
544-739 |
1.07e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 110.26 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCiRIDGQDI--------SQVTQAS 615
Cdd:PRK14243 11 LRTENLNVYYGSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQDTVLFNDTIADNIRYG-RVTA--GN-DE-VEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRVA 690
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGaRINGykGDmDElVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRL 739
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
544-768 |
1.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.66 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRE-TLQDVSFTVMPGQTLALVGPSGAGKSTILRL---LFRFYDISSGCIRIDGQDISQVTQASLRSH 619
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQ--DTVLFNDTIADNIRYG---RVTAGNDEVEAAAQA---AGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAI 691
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVladVGMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
544-760 |
1.16e-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: 108.35 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdgrETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03298 1 VRLDKIRFSYG---EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRV-----TAGNDE-VEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTIL 696
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLSpglklTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
544-754 |
3.33e-26 |
|
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: 107.42 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCI----RIDGQDISQVTQASLRSH 619
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDTVLFNDTIADNIRYGRvTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 700 GIILLDEATSALDTS-NERAIQASLAKVCAN--RTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03290 160 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
562-783 |
3.94e-26 |
|
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: 110.58 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 562 DVSFTVMPGQTLALVGPSGAGKSTILRL---LFRFydiSSGCIRIDG---QDISQVTqaSLRSH---IGVVPQDTVLFND 632
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGevlQDSARGI--FLPPHrrrIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 633 -TIADNIRYG--RVTAGNDEV--EAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:COG4148 92 lSVRGNLLYGrkRAPRAERRIsfDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 708 TSALDTSNERAIQASLAKVCAN-RTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRggvyADMWQLQQGQE 783
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDElDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR----PDLLPLAGGEE 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
556-767 |
1.53e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 106.37 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIR-----ID-----GQDISQVTQasLRSHIGVVPQ 625
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDtarslSQQKGLIRQ--LRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLF-NDTIADNIRYGRVTAGNDEVEAAAQAA-------GIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILK 697
Cdd:PRK11264 93 NFNLFpHRTVLENIIEGPVIVKGEPKEEATARArellakvGLAGKETSYPR-----------RLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQA---SLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNtirQLAQ--EKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
544-754 |
1.84e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 105.28 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRSHIGV 622
Cdd:cd03263 1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFND-TIADNIR-YGRV-----TAGNDEVEAAAQAAGIHDaimafpegYR-TQVGErglkLSGGEKQRVAIART 694
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLkglpkSEIKEEVELLLRVLGLTD--------KAnKRART----LSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
544-760 |
2.11e-25 |
|
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: 104.67 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqvtQASLRSHIGVV 623
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQaagIHDAIMAFP-EGYRTQVGErglKLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYLAQLKGLKKEEARRR---IDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
542-754 |
2.46e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.44 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISqvtqaslrshi 620
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 gVVPQDTVLFNDTIADNIRYGRVTA--GNDEVEAAAQAAGIHDAIMAFPEGYR-TQVgerglkLSGGEKQRVAIARTILK 697
Cdd:COG4178 430 -FLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLH 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
544-764 |
5.18e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQA----SLR 617
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVV-------PQDTVLFNDTIADNirygRVtAGNDEVEAAAQAAGI------HDAIMAFPegyrtqvgergLKLSGG 684
Cdd:PRK11124 82 RNVGMVfqqynlwPHLTVQQNLIEAPC----RV-LGLSKDQALARAEKLlerlrlKPYADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALD---TSNERAIQASLAKVcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAET--GITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
....
gi 1169100883 761 RHEA 764
Cdd:PRK11124 224 DASC 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
560-761 |
6.52e-25 |
|
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: 104.06 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRSHIGVVP--QDTVLFND-TIAD 636
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGRtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 NIRygrvtagndeveAAAQAAGIHDAIMAFPEGYRTQVGER--------GL---------KLSGGEKQRVAIARTILKAP 699
Cdd:cd03219 95 NVM------------VAAQARTGSGLLLARARREEREARERaeellervGLadladrpagELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
544-767 |
7.28e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.01 E-value: 7.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK09536 4 IDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVL-FNDTIADNIRYGRV----------TAGNDEVEAAAQAAGIhdaimafpegyrTQVGERGL-KLSGGEKQRVAI 691
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGV------------AQFADRPVtSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNE-RAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
555-714 |
7.95e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.95 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL-------FRFydisSGCIRIDGQDISQVtQASLRsHIGVVPQDT 627
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFSA----SGEVLLNGRRLTAL-PAEQR-RIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VLF-NDTIADNIRYG---RVTAGN--DEVEAAAQAAGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGI 701
Cdd:COG4136 86 LLFpHLSVGENLAFAlppTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRA 154
|
170
....*....|...
gi 1169100883 702 ILLDEATSALDTS 714
Cdd:COG4136 155 LLLDEPFSKLDAA 167
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
560-768 |
1.16e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.82 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQASLRSHIGVVPQDTvlfndtiad 636
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 nirYG----RVTAG---------NDEVEAAAQAAGIHdAIMAfpegyrtQVgerGLK----------LSGGEKQRVAIAR 693
Cdd:PRK11308 102 ---YGslnpRKKVGqileeplliNTSLSAAERREKAL-AMMA-------KV---GLRpehydryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALDTSneraIQASLAKVCAN-----RTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGRHEALL 766
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVS----VQAQVLNLMMDlqqelGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 243
|
..
gi 1169100883 767 SR 768
Cdd:PRK11308 244 NN 245
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
560-754 |
1.21e-24 |
|
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: 104.55 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqaslrshIGVVPQDTVLFNDTIADNIR 639
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 YGrVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAI 719
Cdd:cd03291 120 FG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 1169100883 720 -QASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03291 199 fESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
544-768 |
1.23e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.25 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQASLRSHIG 621
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIA-DNIRYG-RVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTILKAP 699
Cdd:PRK09493 81 MVFQQFYLFPHLTAlENVMFGpLRVRGASKEEAEKQARELLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 700 GIILLDEATSALDTS--NE--RAIQaSLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK09493 156 KLMLFDEPTSALDPElrHEvlKVMQ-DLAE--EGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
219-516 |
1.34e-24 |
|
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: 104.55 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRA-------LLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLY 378
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVL-TLIGALVILFYLNWKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 379 LTLTIVVTEW-RTKFRRAMNTQENATrARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNL 457
Cdd:cd07346 153 VLILRYFRRRiRKASREVRESLAELS-AFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 458 VIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDME 516
Cdd:cd07346 232 LTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
544-761 |
2.38e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.85 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDtvlfND-----TIADNI---RY----GRVTAgNDEveaaaqaAGIHDAIMAFP-EGYRtqvgERGLK-LSGGEKQRV 689
Cdd:COG4604 81 RQE----NHinsrlTVRELVafgRFpyskGRLTA-EDR-------EIIDEAIAYLDlEDLA----DRYLDeLSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGT 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
544-761 |
4.25e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----AS 615
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQA------AGIHDAIMafpegyrtqvGERGLKLSGGEKQ 687
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAreklalVGISESLF----------EKNPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
544-760 |
4.87e-24 |
|
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: 101.65 E-value: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSHIGVV 623
Cdd:cd03296 3 IEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYG-RVTAGNDEVEAAAQAAGIHD-----AIMAFPEGYRTQvgerglkLSGGEKQRVAIARTIL 696
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHEllklvQLDWLADRYPAQ-------LSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVG 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
544-767 |
5.71e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.48 E-value: 5.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET--LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQaagIHDAIMAFPE-GYRTQVGERglkLSGGEKQRVAIARTILKA 698
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQGIPREEMIKR---VDEALLAVNMlDFKTREPAR---LSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKV--CANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
544-760 |
7.23e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.01 E-value: 7.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRsHIGVV 623
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-HARDR-KVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYG-RVTAGNDEVEAAAqaagIHDAIMAFPEGYR-TQVGER-GLKLSGGEKQRVAIARTILKAP 699
Cdd:PRK10851 80 FQHYALFRHmTVFDNIAFGlTVLPRRERPNAAA----IKAKVTQLLEMVQlAHLADRyPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAG 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
544-760 |
7.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.43 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS--QVTQASLR 617
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQ--DTVLFNDTIADNIRYGRVTAG------NDEVEAAAQAAGIHdaimafPEGYRTQvgeRGLKLSGGEKQRV 689
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGlseeeiENRVKRAMNIVGLD------YEDYKDK---SPFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIqasLAKVCA-----NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEI---LNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
544-760 |
8.94e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.24 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK11231 3 LRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGRVT--------AGNDE--VEAAAQAAGIhdaimafpegyrTQVGERGL-KLSGGEKQRVAI 691
Cdd:PRK11231 82 PQHHLTPEGiTVRELVAYGRSPwlslwgrlSAEDNarVNQAMEQTRI------------NHLADRRLtDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNeraiQASLAKVC-----ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
524-758 |
1.13e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 524 EETEVKDLPGAGPLRFQKGR------IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS 597
Cdd:COG0488 290 EREEPPRRDKTVEIRFPPPErlgkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 598 SGCIRIdGQDIsqvtqaslrsHIGVVPQDTVLF--NDTIADNIRYGRvtAGNDEVEAAAQAAGihdaiMAFPegyrtqvG 675
Cdd:COG0488 369 SGTVKL-GETV----------KIGYFDQHQEELdpDKTVLDELRDGA--PGGTEQEVRGYLGR-----FLFS-------G 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 676 ERGLK----LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAK----VcanrttIVVAH-R--LSTVvn 744
Cdd:COG0488 424 DDAFKpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV-- 495
|
250
....*....|....
gi 1169100883 745 ADQILVIKDGCIVE 758
Cdd:COG0488 496 ATRILEFEDGGVRE 509
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
544-757 |
1.42e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 106.35 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---- 616
Cdd:PRK10535 5 LELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTI 695
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
544-768 |
2.04e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVV 623
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ--DTVLFNDTIADNIRYGRVTAGNDE------VEAAAQAAGIHDaimafpegYRTQVGERglkLSGGEKQRVAIARTI 695
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEE--------LRDRVPHH---LSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 696 LKAPGIILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
544-785 |
2.77e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.86 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA----S 615
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHdAIMAFPEGYRTQvgeRGLKLSGGEKQRVAIAR 693
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMI-ELVGLPEELLAR---SPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVC--ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGg 770
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP- 237
|
250
....*....|....*
gi 1169100883 771 vyADMWQLQQGQEET 785
Cdd:PRK13634 238 --DELEAIGLDLPET 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
556-760 |
5.51e-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: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqVTQASLRSHIGVVPQDTVLF-NDTI 634
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAG--NDEVEAAAQAAGIHDAimafpegYRTQVGerglKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:cd03268 90 RENLRLLARLLGirKKRIDEVLDVVGLKDS-------AKKKVK----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1169100883 713 TSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
553-754 |
1.02e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.58 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 553 YADGR---ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT---QASLRSH-IGVVPQ 625
Cdd:PRK11629 15 YQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFND-TIADNIRYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILL 704
Cdd:PRK11629 95 FHHLLPDfTALENVAMPLLIGKKKPAEINSRALEMLAAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 705 DEATSALDTSNERAIQASLAKVCANRTT--IVVAHRLSTVVNADQILVIKDG 754
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
544-778 |
1.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.70 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----AS 615
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagiHDAIMAFpeGYRTQVGERG-LKLSGGEKQRVAIA 692
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA---HRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAK--VCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237
|
....*....
gi 1169100883 770 GVYADmWQL 778
Cdd:PRK13646 238 KKLAD-WHI 245
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
544-766 |
2.10e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.52 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRSHIGVV 623
Cdd:PRK13536 42 IDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQ-DTVLFNDTIADNI----RYGRVTAgnDEVEAAAQaagihdAIMAFPEgYRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMST--REIEAVIP------SLLEFAR-LESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV-------AHRLstvvnADQILVIKDGCIVERGRHEALL 766
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
545-765 |
2.20e-22 |
|
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: 96.44 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVV 623
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITkLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIRYGrvtagndeveAAAQAAG---IHDAIMA-FPEgYRTQVGERGLKLSGGEKQRVAIARTILKA 698
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTG----------LAALPRRsrkIPDEIYElFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
544-763 |
2.95e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.52 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqASLRSHIGVV 623
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGrvtAGNDEVEAAAQAAGIHDaiMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGII 702
Cdd:PRK11607 97 FQSYALFpHMTVEQNIAFG---LKQDKLPKAEIASRVNE--MLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 703 LLDEATSALDTSNERAIQAS----LAKVCAnrTTIVVAH-RLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEvvdiLERVGV--TCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
544-767 |
3.77e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.59 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADG----RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA----S 615
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQA------AGIHDAIMAfpegyrtqvgERGLKLSGGEKQ 687
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKAlkwlkkVGLSEDLIS----------KSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALD-TSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
..
gi 1169100883 766 LS 767
Cdd:PRK13641 233 FS 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
560-767 |
4.20e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.34 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS----HIGVVPQDTVLF-NDTI 634
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAGNDEVEAAAQA------AGIHDAIMAFPEgyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKAldalrqVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 709 SALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
544-768 |
4.29e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 100.91 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQ---DVSFTVMPGQTLALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVTQASL 616
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEavkGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 R----SHIGVVPQD--TVLfND--TIADNIRYG-RVTAGNDEVEAAAQAA------GIHDA---IMAFPEgyrtqvgerg 678
Cdd:COG4172 87 RrirgNRIAMIFQEpmTSL-NPlhTIGKQIAEVlRLHRGLSGAAARARALellervGIPDPerrLDAYPH---------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 lKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTT--IVVAHRLSTVVN-ADQILVIKDGC 755
Cdd:COG4172 156 -QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMalLLITHDLGVVRRfADRVAVMRQGE 234
|
250
....*....|...
gi 1169100883 756 IVERGRHEALLSR 768
Cdd:COG4172 235 IVEQGPTAELFAA 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
560-754 |
7.56e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 101.91 E-value: 7.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqaslrshIGVVPQDTVLFNDTIADNIR 639
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 YGrVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAI 719
Cdd:TIGR01271 509 FG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*.
gi 1169100883 720 -QASLAKVCANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:TIGR01271 588 fESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
544-742 |
9.02e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 9.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS-----GCIRIDGQDI--SQVTQASL 616
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLFNDTIADNIRYGRVTAG-------NDEVEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRV 689
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASL--AKVCANRTTIVVAHRLSTV 742
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQV 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
551-767 |
1.15e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ------DISQVTQASLRSHIGVVP 624
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QDTVLF-NDTIADNIRYGRVTAGNDE-------VEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQRVAIARTIL 696
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHGIKEkreikkiVEECLRKVGLWKEV-------YDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 697 KAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
548-761 |
1.21e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.41 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGRETlQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRShIGVVPQDT 627
Cdd:PRK11000 8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RG-VGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VLF-NDTIADNIRYGRVTAGNDEVEAAA---QAAGIhdaimafpegyrTQVG---ERGLK-LSGGEKQRVAIARTILKAP 699
Cdd:PRK11000 85 ALYpHLSVAENMSFGLKLAGAKKEEINQrvnQVAEV------------LQLAhllDRKPKaLSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAH-RLSTVVNADQILVIKDGCIVERGR 761
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
544-753 |
1.36e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 92.22 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGqdisqvtqaslRSHIGVV 623
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFNDTIADNIRY--GRVtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGI 701
Cdd:cd03223 70 PQRPYLPLGTLREQLIYpwDDV-------------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCAnrTTIVVAHRLSTVVNADQILVIKD 753
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
544-770 |
1.38e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.95 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqaslRSHIGVV 623
Cdd:COG4152 2 LELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRY-GRVTaGNDEVEAAAQAagihDAIMAfpegyRTQVGERGLK----LSGGEKQRVAIARTILK 697
Cdd:COG4152 77 PEERGLYpKMKVGEQLVYlARLK-GLSKAEAKRRA----DEWLE-----RLGLGDRANKkveeLSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGG 770
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
562-769 |
1.43e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.10 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 562 DVSFTVmPGQTL-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDG---QDISQVTQASL-RSHIGVVPQDTVLFND-TIA 635
Cdd:TIGR02142 15 DADFTL-PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPPeKRRIGYVFQEARLFPHlSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRYGRVTAGNDEVEAAaqaagiHDAIMAFpEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSN 715
Cdd:TIGR02142 94 GNLRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 716 ERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRG 769
Cdd:TIGR02142 167 KYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
544-760 |
2.35e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQASLRSHIG 621
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAagihDAIMAfpegyRTQVGERGLK----LSGGEKQRVAIARTI 695
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRV----DNALK-----RTGIEHLKDKpthcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 696 LKAPGIILLDEATSALD---TSNERAIQASLAKVcANRTTIVVAHRLSTV-VNADQILVIKDGCIVERG 760
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKE-LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQG 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
560-751 |
3.11e-21 |
|
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: 93.95 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQASLRSHIGVVP--QDTVLFND-TIAD 636
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL-PPHRIARLGIARtfQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 NIRYGRVTAGN---------------DEVEAAAQAagihDAIMAFP--EGYR-TQVGErglkLSGGEKQRVAIARTILKA 698
Cdd:COG0411 99 NVLVAAHARLGrgllaallrlprarrEEREARERA----EELLERVglADRAdEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVI 751
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVL 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
545-760 |
3.23e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.59 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL--FRFYDISSGCIRIDGQDISQ--VTQaslRSHI 620
Cdd:COG0396 2 EIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILElsPDE---RARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GV---------VPQDTVL-FNDTIADNIRYGRVTAG--NDEVEAAAQAAGIHDAIMafpegyrtqvgERGL--KLSGGEK 686
Cdd:COG0396 78 GIflafqypveIPGVSVSnFLRTALNARRGEELSARefLKLLKEKMKELGLDEDFL-----------DRYVneGFSGGEK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALDTSnerAIQAsLAKVC-----ANRTTIVVAH--RLSTVVNADQILVIKDGCIVER 759
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDID---ALRI-VAEGVnklrsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKS 222
|
.
gi 1169100883 760 G 760
Cdd:COG0396 223 G 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
543-726 |
3.81e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.77 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVTQASLRSh 619
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 iGVVPQDTVLFN-DTIADNIRYGRVTAGNDEVEAAAQAA------GIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIA 692
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEellalvGLADFARRRI-----------WQLSGGMRQRVGIA 146
|
170 180 190
....*....|....*....|....*....|....
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKV 726
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
494-787 |
5.60e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.89 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 494 LYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVkdLPGAGPLRFQKGRIEFENVHFSYADGRE--TLQDVSFTVMPGQ 571
Cdd:PLN03232 567 LRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERI--LAQNPPLQPGAPAISIKNGYFSWDSKTSkpTLSDINLEIPVGS 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 572 TLALVGPSGAGKSTILR-LLFRFYDISSGCIRIdgqdisqvtqaslRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEV 650
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGSDFESERYW 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 651 EAAAQAAGIHDAIMaFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAK-VCAN 729
Cdd:PLN03232 712 RAIDVTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdELKG 790
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 730 RTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSE 787
Cdd:PLN03232 791 KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQE 848
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
544-768 |
6.94e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.10 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRSHIGVV 623
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNIR-YGRVTAgndevEAAAQAAGIHDAIMAFP---EGYRTQVGErglkLSGGEKQRVAIARTILKA 698
Cdd:PRK13537 86 PQFDNLDPDfTVRENLLvFGRYFG-----LSAAAARALVPPLLEFAkleNKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV-------AHRLstvvnADQILVIKDGCIVERGRHEALLSR 768
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
521-788 |
8.57e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 98.66 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 521 LLKEETEVKDLPgagPLRFQKGRIEFENVHFSY-ADG-RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS 598
Cdd:PLN03130 595 LLAEERVLLPNP---PLEPGLPAISIKNGYFSWdSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 599 GciridgqdisqvTQASLRSHIGVVPQDTVLFNDTIADNIRYGrVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERG 678
Cdd:PLN03130 672 D------------ASVVIRGTVAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERG 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAI-QASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:PLN03130 739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIK 818
|
250 260 270
....*....|....*....|....*....|.
gi 1169100883 758 ERGRHEALLSRGGVYADMWQLQQGQEETSED 788
Cdd:PLN03130 819 EEGTYEELSNNGPLFQKLMENAGKMEEYVEE 849
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
556-725 |
2.41e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGvvPQDTVLFNDTIA 635
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRYGRVTAGNDE--VEAAAQAAGIHDaIMAFPEGYrtqvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDT 713
Cdd:PRK13539 92 ENLEFWAAFLGGEEldIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|....*.
gi 1169100883 714 SNERA----IQASLAK 725
Cdd:PRK13539 161 AAVALfaelIRAHLAQ 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
546-712 |
3.81e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 546 FENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqasLRshIGVVPQ 625
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFND-TIADNI-----------------------------RYGRVTAGNDEV---EAAAQAAGIHDAiMAFPEGYRT 672
Cdd:COG0488 69 EPPLDDDlTVLDTVldgdaelraleaeleeleaklaepdedleRLAELQEEFEALggwEAEARAEEILSG-LGFPEEDLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1169100883 673 Q-VGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:COG0488 148 RpVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
544-760 |
4.31e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.30 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRET-----LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA-SLR 617
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQDTVlfNDTIAdnirygrvTAGNDEVEAAAQAAGIHdaimafPEGYRTQVGErGLK--------------LSG 683
Cdd:PRK13633 85 NKAGMVFQNPD--NQIVA--------TIVEEDVAFGPENLGIP------PEEIRERVDE-SLKkvgmyeyrrhaphlLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVNADQILVIKDGCIVERG 760
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
551-758 |
6.47e-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: 90.25 E-value: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---LRSHIGVVPQD 626
Cdd:TIGR02769 17 LFGAKQRAPvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TV-LFN------DTIADNIR-YGRVtagnDEVEAAAQAAGIHDAImafpeGYRTQVGER-GLKLSGGEKQRVAIARTILK 697
Cdd:TIGR02769 97 SPsAVNprmtvrQIIGEPLRhLTSL----DESEQKARIAELLDMV-----GLRSEDADKlPRQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTT--IVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
560-767 |
7.09e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 7.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQASL---RSHIGVVPQD------ 626
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 ---TVLfnDTIADNIR--YGRVTAGNDE--VEAAAQAAGIHdaimafPEGYRTQVGErglkLSGGEKQRVAIARTILKAP 699
Cdd:PRK15134 377 prlNVL--QIIEEGLRvhQPTLSAAQREqqVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLStVVNA--DQILVIKDGCIVERGRHEALLS 767
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
544-712 |
8.92e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.83 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASlRShIGVV 623
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLF-NDTIADNIRYGRVTAGNDEVEAA---AQAAGIHDaIMAFPEgyrtqvgERGLKLSGGEKQRVAIARTILKAP 699
Cdd:PRK11650 82 FQNYALYpHMSVRENMAYGLKIRGMPKAEIEervAEAARILE-LEPLLD-------RKPRELSGGQRQRVAMGRAIVREP 153
|
170
....*....|...
gi 1169100883 700 GIILLDEATSALD 712
Cdd:PRK11650 154 AVFLFDEPLSNLD 166
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
544-763 |
1.17e-19 |
|
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: 87.97 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTqASLRSHIG 621
Cdd:cd03217 1 LEIKDLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VvpqdTVLFND-------TIADNIRYgrvtagndeveaaaqaagihdaimafpegyrtqVGErglKLSGGEKQRVAIART 694
Cdd:cd03217 79 I----FLAFQYppeipgvKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAK-VCANRTTIVVAH--RLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
557-775 |
1.27e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.85 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDgqdisqvtqaslRShIGVVPQDTVLFNDTIAD 636
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 NIRYgrvtagNDEveaaAQAAGIHDAI---------MAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:PTZ00243 740 NILF------FDE----EDAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 708 TSALDTS-NERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLsRGGVYADM 775
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATL 877
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
560-737 |
1.50e-19 |
|
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: 88.10 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQdisQVTQASLRSHIGVVPQ-DTVLFNDTIA 635
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQdDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRY------GRVTAGNDEVEAAAQAAGIHDAImafpegyrTQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:cd03234 100 ETLTYtailrlPRKSSDAIRKKRVEDVLLRDLAL--------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 1169100883 709 SALDTSNERAIQASLAKVCA-NRTTIVVAH 737
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARrNRIVILTIH 201
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
540-765 |
1.50e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.93 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADGReTLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDisqVTQASLRSH 619
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 -IGVVPQDTVLF-NDTIADNIRYGRVTAG--NDEV-EAAAQAAGIHDaIMAFPEGYRTQVgerglklSGGEKQRVAIART 694
Cdd:PRK11432 79 dICMVFQSYALFpHMSLGENVGYGLKMLGvpKEERkQRVKEALELVD-LAGFEDRYVDQI-------SGGQQQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERA-------IQASLakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSmrekireLQQQF-----NITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
557-738 |
1.85e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 87.71 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFY--DISSGCIRIDGQDISQvtqaslrshigvvpqdtvlfNDTI 634
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIryGRVTAGNDEVEAAAqAAGIHDAIMafpegYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTS 714
Cdd:COG2401 103 IDAI--GRKGDFKDAVELLN-AVGLSDAVL-----WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 1169100883 715 NERAIQASLAKVC--ANRTTIVVAHR 738
Cdd:COG2401 171 TAKRVARNLQKLArrAGITLVVATHH 196
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
542-706 |
2.32e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.16 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTIlrllfrFYDI------SSGCIRIDGQDIsqvTQAS 615
Cdd:COG1137 2 MTLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIvglvkpDSGRIFLDGEDI---THLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 L--RSH--IGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAAQAA------GIhdaimafpEGYRTQvgeRGLKLSGG 684
Cdd:COG1137 72 MhkRARlgIGYLPQEASIFRKlTVEDNILAVLELRKLSKKEREERLEelleefGI--------THLRKS---KAYSLSGG 140
|
170 180
....*....|....*....|..
gi 1169100883 685 EKQRVAIARTILKAPGIILLDE 706
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDE 162
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
543-763 |
2.61e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.05 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGrETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDISQVTQASLR 617
Cdd:PRK14247 3 KIEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 618 SHIGVVPQ-DTVLFNDTIADNIRYG----RVTAGNDEVEA----AAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQR 688
Cdd:PRK14247 82 RRVQMVFQiPNPIPNLSIFENVALGlklnRLVKSKKELQErvrwALEKAQLWDEV-------KDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAH------RLStvvnaDQILVIKDGCIVERG-- 760
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGpt 229
|
250
....*....|
gi 1169100883 761 -------RHE 763
Cdd:PRK14247 230 revftnpRHE 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
560-760 |
2.73e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILR-----LLFRFYDISSGCIRIdGQDISQVTQAS------------LRSHIGV 622
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYI-GDKKNNHELITnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAaQAAGIHDAIMAFPEGYRtqvgERG-LKLSGGEKQRVAIARTILKAP 699
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGPVALGVKKSEAK-KLAKFYLNKMGLDDSYL----ERSpFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 700 GIILLDEATSALDTSNERA-IQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
560-757 |
3.64e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.63 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVTQAS----LRSHIGVVPQDTVLFND-TI 634
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAG---------NDEVEAAAQAAGIH---DAImafpegyrtqVGErglkLSGGEKQRVAIARTILKAPGII 702
Cdd:COG3845 98 AENIVLGLEPTKggrldrkaaRARIRELSERYGLDvdpDAK----------VED----LSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 703 LLDEATSALdTSNE-RAIQASLAKVCANRTTIV-VAHRLSTVV-NADQILVIKDGCIV 757
Cdd:COG3845 164 ILDEPTAVL-TPQEaDELFEILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
556-760 |
5.20e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.29 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---------RSHIGVVPQD 626
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TvlfndtiADNIR--------------------YGRV--TAGN--DEVEAAAqaAGIHDAIMAFpegyrtqvgerglklS 682
Cdd:PRK11701 98 P-------RDGLRmqvsaggnigerlmavgarhYGDIraTAGDwlERVEIDA--ARIDDLPTTF---------------S 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 683 GGEKQRVAIARTILKAPGIILLDEATSALDTSneraIQASLAKVCANRTT------IVVAHRLSTV-VNADQILVIKDGC 755
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVArLLAHRLLVMKQGR 229
|
....*
gi 1169100883 756 IVERG 760
Cdd:PRK11701 230 VVESG 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
555-767 |
5.81e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRetLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQASLRSHIGVVPQDTV------ 628
Cdd:COG4138 9 AGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 629 ------LFNDTIADnirygrVTAGNDEVEAAAQAAGIHDAIMafpegyrtqvgeRGL-KLSGGEKQRVAIARTILKA-PG 700
Cdd:COG4138 86 vfqylaLHQPAGAS------SEAVEQLLAQLAEALGLEDKLS------------RPLtQLSGGEWQRVRLAAVLLQVwPT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 701 I------ILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAHRLS-TVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:COG4138 148 InpegqlLLLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
560-758 |
7.70e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.37 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ASLRS-HIGVVPQDTVLFNDTIA 635
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAkHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 -DNIRYGRVTAGNDEVEAAAQAAGIHDAImafpegyrtQVGER----GLKLSGGEKQRVAIARTILKAPGIILLDEATSA 710
Cdd:PRK10584 106 lENVELPALLRGESSRQSRNGAKALLEQL---------GLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 711 LDTSNERAIQASLAKVcaNR----TTIVVAHRLSTVVNADQILVIKDGCIVE 758
Cdd:PRK10584 177 LDRQTGDKIADLLFSL--NRehgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
548-767 |
8.98e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDISQVTQA-SLRSHIG 621
Cdd:PRK14271 26 NLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFNDTIADNIRYG---RVTAGNDEVEAAAQA----AGIHDAImafpegyRTQVGERGLKLSGGEKQRVAIART 694
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGvraHKLVPRKEFRGVAQArlteVGLWDAV-------KDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
540-763 |
1.63e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.48 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLrsh 619
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 620 IGVVPQDT-------VLFNDTIADNiRYG-----RVTAGNDE--VEAAAQAAGIHDaimafpegYR-TQVGErglkLSGG 684
Cdd:PRK15056 80 VAYVPQSEevdwsfpVLVEDVVMMG-RYGhmgwlRRAKKRDRqiVTAALARVDMVE--------FRhRQIGE----LSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVNADQILVIKDGCIVERGRHE 763
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
544-760 |
1.64e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 85.78 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDISQVtQASLRSHIG 621
Cdd:TIGR01978 1 LKIKDLHVSVED-KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLEL-EPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 V---------VPQDTVLFNDTIADNIRygRVTAGNDEVEAAAQAAGIHD--AIMAFPEGYRtqvgERGLK--LSGGEKQR 688
Cdd:TIGR01978 79 LflafqypeeIPGVSNLEFLRSALNAR--RSARGEEPLDLLDFEKLLKEklALLDMDEEFL----NRSVNegFSGGEKKR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAH--RLSTVVNADQILVIKDGCIVERG 760
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREpDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
544-765 |
1.99e-18 |
|
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: 84.73 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRSHIGVV 623
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQdtvlfnDTIADNIRYGRvtagnDEVEaaaqaagIHDAIMAFPEGYRTQVGERGLKL--------------SGGEKQRV 689
Cdd:cd03265 79 FQ------DLSVDDELTGW-----ENLY-------IHARLYGVPGAERRERIDELLDFvglleaadrlvktySGGMRRRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 690 AIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCA-NRTTIVV-------AHRLstvvnADQILVIKDGCIVERGR 761
Cdd:cd03265 141 EIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGT 215
|
....
gi 1169100883 762 HEAL 765
Cdd:cd03265 216 PEEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
560-754 |
2.23e-18 |
|
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: 84.82 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLrshigVVPQDTVLFN-DTIADNI 638
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 639 rYGRVTAGNDEVEAAAQAAGIHDAIMAFpeGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERA 718
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1169100883 719 IQASLAKVC--ANRTTIVVAHRL-STVVNADQILVIKDG 754
Cdd:TIGR01184 153 LQEELMQIWeeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
545-754 |
3.40e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 545 EFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVV 623
Cdd:PRK11288 6 SFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFND-TIADNI-------RYGRVTAGNDEVEAAAQAAGIHDAIMafPEgyrTQVGErglkLSGGEKQRVAIARTI 695
Cdd:PRK11288 85 YQELHLVPEmTVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDID--PD---TPLKY----LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 696 LKAPGIILLDEATSALdTSNE-----RAIQASLAKvcaNRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK11288 156 ARNARVIAFDEPTSSL-SAREieqlfRVIRELRAE---GRVILYVSHRMEEIFAlCDAITVFKDG 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
544-767 |
3.66e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ-ASLRSHIGV 622
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQ--DTVLFNDTIADNIRYGR------VTAGNDEVEAAAQAAGIhdaimafpEGYRTQVGErglKLSGGEKQRVAIART 694
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPenlclpPIEIRKRVDRALAEIGL--------EKYRHRSPK---TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
555-751 |
4.12e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfydisSGCIRidgQDISQVTQASLRShIGVVPQDTVL---FN 631
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-------AGVLR---PTSGTVRRAGGAR-VAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 632 DTIADNIRYG---------RVTAGN-DEVEAAAQAAGIHDAImafpegyRTQVGErglkLSGGEKQRVAIARTILKAPGI 701
Cdd:NF040873 72 LTVRDLVAMGrwarrglwrRLTRDDrAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCA-NRTTIVVAHRLSTVVNADQILVI 751
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
544-726 |
4.46e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqaslrSHIGVV 623
Cdd:PRK11248 2 LQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLFN-DTIADNIRYGRVTAG--NDEVEAAAQAAGIHDAIMAFPEGYRTQvgerglkLSGGEKQRVAIARTILKAPG 700
Cdd:PRK11248 76 FQNEGLLPwRNVQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQ-------LSGGQRQRVGIARALAANPQ 148
|
170 180
....*....|....*....|....*.
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKV 726
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
549-765 |
5.20e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.91 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 549 VHFSYADGR-------ETLQ---DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL-- 616
Cdd:PRK15079 16 VHFDIKDGKqwfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWra 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 -RSHIGVVPQD---------TVlfNDTIADNIRYGRVTAGNDEVEAAAQAagihdaiMAFPEGYRTQVGER-GLKLSGGE 685
Cdd:PRK15079 96 vRSDIQMIFQDplaslnprmTI--GEIIAEPLRTYHPKLSRQEVKDRVKA-------MMLKVGLLPNLINRyPHEFSGGQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 686 KQRVAIARTILKAPGIILLDEATSALDTSneraIQASLAKVCAN------RTTIVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQQlqremgLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
....*..
gi 1169100883 759 RGRHEAL 765
Cdd:PRK15079 243 LGTYDEV 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
560-758 |
5.23e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHIGVVPQDTV-LFN--DT 633
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSIsAVNprKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYG-RVTAGNDEVEAAAQAAGIHDAIMAFPEgyrtQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PRK10419 108 VREIIREPlRHLLSLDKAERLARASEMLRAVDLDDS----VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1169100883 713 TSNERAIQASLAKVCANRTT--IVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
556-764 |
6.19e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQAsLRSHIGVVPQD----TVL 629
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDA-IRAGIAYVPEDrkgeGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 FNDTIADNI---RYGRVTAG-----NDEVEAAAQ--------AAGIHDAIMAfpegyrtqvgerglkLSGGEKQRVAIAR 693
Cdd:COG1129 343 LDLSIRENItlaSLDRLSRGglldrRRERALAEEyikrlrikTPSPEQPVGN---------------LSGGNQQKVVLAK 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAhrlST----VV-NADQILVIKDGCIV-ERGRHEA 764
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpeLLgLSDRILVMREGRIVgELDREEA 481
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
542-760 |
9.51e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYADGR----ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG-------CIRIDGQDISQ 610
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 611 VTQasLRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDaIMAFPEGYrtqVGERGLKLSGGEKQR 688
Cdd:PRK13645 85 VKR--LRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLK-LVQLPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 689 VAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCAN--RTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIG 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
547-756 |
9.54e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqaslRSHIGVVPQD 626
Cdd:PRK11247 16 NAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFN-DTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGyrtqvgerglkLSGGEKQRVAIARTILKAPGIILLD 705
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 706 EATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCI 756
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
544-719 |
1.17e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqasLRshIGVV 623
Cdd:PRK09544 5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQDTVLfNDTIADNI-RYGRVTAG---NDEVEAAA--QAAGIHDAIMAfpegyrtqvgerglKLSGGEKQRVAIARTILK 697
Cdd:PRK09544 73 PQKLYL-DTTLPLTVnRFLRLRPGtkkEDILPALKrvQAGHLIDAPMQ--------------KLSGGETQRVLLARALLN 137
|
170 180
....*....|....*....|..
gi 1169100883 698 APGIILLDEATSALDTSNERAI 719
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVAL 159
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
544-754 |
1.32e-17 |
|
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: 80.19 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQDISqvtqaslrshIGVV 623
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 624 PQdtvlfndtiadnirygrvtagndeveaaaqaagihdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGIIL 703
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVcaNRTTIVVAH-R--LSTVvnADQILVIKDG 754
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
544-712 |
1.34e-17 |
|
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: 82.59 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqASLRSHIGV- 622
Cdd:cd03218 1 LRAENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-MHKRARLGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 -VPQDTVLFND-TIADNIRygrvtagndeveAAAQaagihdaIMAFPEGYRTQVGE--------------RGLKLSGGEK 686
Cdd:cd03218 79 yLPQEASIFRKlTVEENIL------------AVLE-------IRGLSKKEREEKLEelleefhithlrksKASSLSGGER 139
|
170 180
....*....|....*....|....*.
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALD 712
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
544-760 |
2.17e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.58 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGrETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQASL 616
Cdd:PRK14267 5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RSHIGVVPQDTVLF-NDTIADNI----RYGRVTAGNDE----VEAAAQAAGIHDAImafpegyRTQVGERGLKLSGGEKQ 687
Cdd:PRK14267 84 RREVGMVFQYPNPFpHLTIYDNVaigvKLNGLVKSKKElderVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 688 RVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
543-760 |
3.02e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYadGRETL-QDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIG 621
Cdd:PRK10253 7 RLRGEQLTLGY--GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLFND-TIADNIRYGRV----------TAGNDEVEAAAQAAGIHDAimafpegyrtqVGERGLKLSGGEKQRVA 690
Cdd:PRK10253 85 LLAQNATTPGDiTVQELVARGRYphqplftrwrKEDEEAVTKAMQATGITHL-----------ADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNR----TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL--NRekgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
560-754 |
5.91e-17 |
|
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: 79.40 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-VTQASLRSHIGVVPQD---TVLFND-TI 634
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIAYVPEDrkrEGLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIrygrvtagndeveaaaqAAGIHdaimafpegyrtqvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTS 714
Cdd:cd03215 96 AENI-----------------ALSSL--------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1169100883 715 NERAIQASLAKVCANRTTIVVahrLST-----VVNADQILVIKDG 754
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEG 180
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
544-768 |
6.19e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.85 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL--FRFYDISSG-----------CIRIDGQ---- 606
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekCGYVERPskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 607 ------------------DISQVTQASLRSHIGVVPQDT-VLF-NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDaimaf 666
Cdd:TIGR03269 80 epcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 667 pegyRTQVGER----GLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAK-VCANRTTIVVAHRLST 741
Cdd:TIGR03269 155 ----MVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*....
gi 1169100883 742 VVN--ADQILVIKDGCIVERGRHEALLSR 768
Cdd:TIGR03269 231 VIEdlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
557-767 |
7.54e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKS----TILRLLFR---FYdiSSGCIRIDGQDISQVTQASLR----SHIGVVPQ 625
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY--PSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 D-TVLFN--DTIADNI-------RYGRVTAGNDEVEAAAQAAGIHDA---IMAFPEgyrtqvgerglKLSGGEKQRVAIA 692
Cdd:PRK15134 100 EpMVSLNplHTLEKQLyevlslhRGMRREAARGEILNCLDRVGIRQAakrLTDYPH-----------QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLA--KVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
547-712 |
9.56e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGVVPQ 625
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFND-TIADNIRygRVTAGNDEVEAAAQAAGIHDAIMAFP-EGYRTQVGErglKLSGGEKQRVAIARTILKAPGIIL 703
Cdd:PRK10895 86 EASIFRRlSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHiEHLRDSMGQ---SLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 1169100883 704 LDEATSALD 712
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
544-760 |
1.06e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAD----GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS---- 615
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERG-LKLSGGEKQRVAIA 692
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSpFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
544-760 |
1.50e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA-SLRSHIGV 622
Cdd:PRK09700 6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFND-TIADNIRYGRVTA----GNDEVEAAAQAagIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILK 697
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGRHLTkkvcGVNIIDWREMR--VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
558-760 |
4.63e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.14 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQASLRSHIGVV-PQDTVLFND-TIA 635
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfGQKTQLWWDlPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYrTQVgeRglKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSN 715
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLD-TPV--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1169100883 716 ERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03267 189 QENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
540-767 |
4.97e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA----- 614
Cdd:PRK10619 2 SENKLNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 615 --------SLRSHIGVVPQDtvlFNdtiadniRYGRVTAGNDEVEAAAQAAGIHDAIM-AFPEGYRTQVG--ERG----- 678
Cdd:PRK10619 81 vadknqlrLLRTRLTMVFQH---FN-------LWSHMTVLENVMEAPIQVLGLSKQEArERAVKYLAKVGidERAqgkyp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALD---TSNERAIQASLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQG 228
|
250
....*....|...
gi 1169100883 755 CIVERGRHEALLS 767
Cdd:PRK10619 229 KIEEEGAPEQLFG 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
563-767 |
5.80e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSG--CIRIdGQDISQVTQ------ASLRSHIGVVPQDTVLF-NDT 633
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRV-GDEWVDMTKpgpdgrGRAKRYIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYGRVTAGNDEVeaaAQAAGIHDAIMA-FPEGYRTQVGER-GLKLSGGEKQRVAIARTILKAPGIILLDEATSAL 711
Cdd:TIGR03269 382 VLDNLTEAIGLELPDEL---ARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 712 DTSNERAIQASL--AKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:TIGR03269 459 DPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
555-752 |
8.65e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 76.76 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTI 634
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAGNDEVEAA-AQA--AGIHDAIMAfpegyrtqvgerglKLSGGEKQRVAIARTILKAPGIILLDEATSAL 711
Cdd:cd03231 91 LENLRFWHADHSDEQVEEAlARVglNGFEDRPVA--------------QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1169100883 712 DTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIK 752
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
556-754 |
9.53e-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: 82.37 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsQVTQASLRSHIGVVPQDTVLFND-TI 634
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRVTAGND------EVEAAAQAAGIHDaimafpegyrtQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:TIGR01257 1021 AEHILFYAQLKGRSweeaqlEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1169100883 709 SALDTSNERAIQASLAKVCANRTTIVVAHRLSTV-VNADQILVIKDG 754
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQG 1136
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
556-759 |
1.22e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVVPQDTVLF-NDT 633
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIpQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYGR--VTA--GNDEVEAAAQAagihDAIMA---FPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDE 706
Cdd:PRK10762 96 IAENIFLGRefVNRfgRIDWKKMYAEA----DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 707 ATSAL-DTSNEraiqaSLAKVC----ANRTTIV-VAHRLSTVVN-ADQILVIKDG-CIVER 759
Cdd:PRK10762 168 PTDALtDTETE-----SLFRVIrelkSQGRGIVyISHRLKEIFEiCDDVTVFRDGqFIAER 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
560-714 |
1.27e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHIGVVPQD---------T 627
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDpyasldprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VlfNDTIADNIRYGRVTAGNdevEAAAQAAGIHDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:PRK10261 420 V--GDSIMEPLRVHGLLPGK---AAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEA 490
|
....*..
gi 1169100883 708 TSALDTS 714
Cdd:PRK10261 491 VSALDVS 497
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
547-766 |
1.91e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQD 626
Cdd:PRK10575 15 RNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFND-TIADNIRYGRVTAgndeveaaaqaagiHDAIMAFPEGYRTQVGER----GLK---------LSGGEKQRVAIA 692
Cdd:PRK10575 94 LPAAEGmTVRELVAIGRYPW--------------HGALGRFGAADREKVEEAislvGLKplahrlvdsLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 693 RTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALL 766
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
544-760 |
2.07e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSY------------------ADGRET---LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIR 602
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrrRTRREEfwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 603 IDGqdisqvTQASLrshIGV----VPQDTVlfndtiADNIR-----YGRVTAGNDEVEAAAQA-AGIHDAIMAfPegYRT 672
Cdd:COG1134 85 VNG------RVSAL---LELgagfHPELTG------RENIYlngrlLGLSRKEIDEKFDEIVEfAELGDFIDQ-P--VKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTS-NERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILV 750
Cdd:COG1134 147 --------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIW 218
|
250
....*....|
gi 1169100883 751 IKDGCIVERG 760
Cdd:COG1134 219 LEKGRLVMDG 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
543-765 |
2.61e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.43 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRET----LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS--- 615
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 ---------------------LRSHIGVVPQ--DTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDaIMAFPEGYRt 672
Cdd:PRK13651 82 kvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIE-LVGLDESYL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgERG-LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVN-ADQIL 749
Cdd:PRK13651 160 ---QRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTI 236
|
250
....*....|....*..
gi 1169100883 750 VIKDGCIVERGR-HEAL 765
Cdd:PRK13651 237 FFKDGKIIKDGDtYDIL 253
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
559-763 |
2.98e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 559 TLQDVSFTV---MPGQTL-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----ASLRSHIGVVPQDTVLF 630
Cdd:PRK11144 9 QLGDLCLTVnltLPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclPPEKRRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 -NDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPegyrtqvgergLKLSGGEKQRVAIARTILKAPGIILLDEATS 709
Cdd:PRK11144 89 pHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 710 ALDTSNERAIQASLAKVCAN-RTTIV-VAHRLSTVVN-ADQILVIKDGCIVERGRHE 763
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLE 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
558-760 |
3.62e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqVTQASLRSH-IGVVPQDTvlfNDTIAD 636
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQrIRMIFQDP---STSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 NIRYGRVTAG----NDEVEAAAQAAGIHDAImafpegyrTQVGERG-------LKLSGGEKQRVAIARTILKAPGIILLD 705
Cdd:PRK15112 103 RQRISQILDFplrlNTDLEPEQREKQIIETL--------RQVGLLPdhasyypHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 706 EATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
531-740 |
3.97e-15 |
|
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: 79.41 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 531 LPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD--- 607
Cdd:TIGR00954 439 VPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklf 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 608 -ISQ---VTQASLRshigvvpqDTVLFNDTIADNIRYGrvtAGNDEVEAAAQAAGIHDAIMAfpEGYRTQVGERGLKLSG 683
Cdd:TIGR00954 519 yVPQrpyMTLGTLR--------DQIIYPDSSEDMKRRG---LSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSG 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 684 GEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKvcANRTTIVVAHRLS 740
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
540-761 |
4.25e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 540 QKGRIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAS-LRS 618
Cdd:PRK11614 2 EKVMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQDTVLFND-TIADNIRYGRVTAGNDEVEAAaqaagIHDAIMAFPEGYRTQVgERGLKLSGGEKQRVAIARTILK 697
Cdd:PRK11614 81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQER-----IKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRlstvvNADQILVIKD-GCIVERGR 761
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQ-----NANQALKLADrGYVLENGH 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
543-764 |
4.55e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSH-IG 621
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQD-----TVLfNDTIADNI---RYGRVTAGN----DEVEAAAQAAGIhdaIMAF---PEGYRTQVGerglKLSGGEK 686
Cdd:COG3845 337 YIPEDrlgrgLVP-DMSVAENLilgRYRRPPFSRggflDRKAIRAFAEEL---IEEFdvrTPGPDTPAR----SLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTI-VVAHRLSTVVN-ADQILVIKDGCIV-ERGRHE 763
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVlLISEDLDEILAlSDRIAVMYEGRIVgEVPAAE 488
|
.
gi 1169100883 764 A 764
Cdd:COG3845 489 A 489
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
560-760 |
6.19e-15 |
|
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: 74.88 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqaSLRSHIGVVPQDTVLfndtiaDNIR 639
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-----LLGLGGGFNPELTGR------ENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 -----YGRVTAGNDEVEaaaqaagihDAIMAFPE-GyrtQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:cd03220 107 lngrlLGLSRKEIDEKI---------DEIIEFSElG---DFIDLPVKtYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1169100883 713 TS-NERAIQASLAKVCANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERG 760
Cdd:cd03220 175 AAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
560-757 |
9.24e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.12 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVL---FNDTIAD 636
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 637 N--IRYGRvtagndeveaaAQAAGIHDAIM-AFPEGYRTQVGERGL-----------KLSGGEKQRVAIARTILKAPGII 702
Cdd:COG1101 102 NlaLAYRR-----------GKRRGLRRGLTkKRRELFRELLATLGLglenrldtkvgLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 703 LLDEATSALD--TSN------ERAIQASlakvcaNRTTIVVAHRLSTVVN-ADQILVIKDGCIV 757
Cdd:COG1101 171 LLDEHTAALDpkTAAlvleltEKIVEEN------NLTTLMVTHNMEQALDyGNRLIMMHEGRII 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
555-736 |
1.33e-14 |
|
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: 73.16 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTI 634
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 ADNIRYGRvtagndEVEAAAQAAgIHDAImafpegyrTQVGERGLK------LSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:TIGR01189 91 LENLHFWA------AIHGGAQRT-IEDAL--------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 1169100883 709 SALDTSNERAIQASLAKVCAnRTTIVVA 736
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLA-RGGIVLL 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
544-757 |
1.63e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslRSH---I 620
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHqlgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLF-NDTIADNIRYG--RVTAGNDEVEAAAQAAGIH---DAIMAfpegyrtqvgerglKLSGGEKQRVAIART 694
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQldlDSSAG--------------SLEVADRQIVEILRG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCIV 757
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIA 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
544-765 |
1.97e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASL---RSHI 620
Cdd:PRK11831 8 VDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 621 GVVPQDTVLFND-TIADNIRYGRvtagndEVEAAAQAAGIHDAIMAFPEGyrtqVGERGL------KLSGGEKQRVAIAR 693
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPL------REHTQLPAPLLHSTVMMKLEA----VGLRGAaklmpsELSGGMARRAALAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALDTsnerAIQASLAKVCANR------TTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEAL 765
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDP----ITMGVLVKLISELnsalgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
552-712 |
4.43e-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: 75.74 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 552 SYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQASLRSHIGVVPQD----- 626
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KDFNGEARPQPGIKVGYLPQEpqldp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 --TVLFN--DTIAD-----------NIRYGRVTAGND-------EVEAAAQAAGIHD-------AIMAF--PEGyRTQVG 675
Cdd:TIGR03719 82 tkTVRENveEGVAEikdaldrfneiSAKYAEPDADFDklaaeqaELQEIIDAADAWDldsqleiAMDALrcPPW-DADVT 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1169100883 676 erglKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:TIGR03719 161 ----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
543-768 |
5.22e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.81 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYAdgRETLQDVSFTVMPGQTLALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISqvtQASLRS 618
Cdd:PRK10418 4 QIELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 -HIGVVPQDT-VLFN--DTIADNIR-----YGRvTAGNDEVEAAAQAAGIHDAimafpegyrtqvgERGLKL-----SGG 684
Cdd:PRK10418 79 rKIATIMQNPrSAFNplHTMHTHARetclaLGK-PADDATLTAALEAVGLENA-------------ARVLKLypfemSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRT--TIVVAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGD 224
|
....*..
gi 1169100883 762 HEALLSR 768
Cdd:PRK10418 225 VETLFNA 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
542-712 |
6.78e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.37 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRI--EFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ-DISQVTQ--ASL 616
Cdd:PRK11147 316 GKIvfEMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQhrAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 RshigvvPQDTVLfnDTIADnirygrvtaGNDEVEAAAQAAGIHDAIMAF---PEGYRTQVGerglKLSGGEKQRVAIAR 693
Cdd:PRK11147 395 D------PEKTVM--DNLAE---------GKQEVMVNGRPRHVLGYLQDFlfhPKRAMTPVK----ALSGGERNRLLLAR 453
|
170
....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALD 712
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLD 472
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
548-763 |
1.10e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGR-ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ----------DISQVTQASL 616
Cdd:PRK10261 19 NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 617 R----SHIGVVPQD--TVL-----FNDTIADNIrygRVTAGNDEVEAAAQAAGIHDAIMaFPEGyRTQVGERGLKLSGGE 685
Cdd:PRK10261 99 RhvrgADMAMIFQEpmTSLnpvftVGEQIAESI---RLHQGASREEAMVEAKRMLDQVR-IPEA-QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 686 KQRVAIARTILKAPGIILLDEATSALDTSneraIQA---SLAKVCANRTT---IVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVT----IQAqilQLIKVLQKEMSmgvIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
....*
gi 1169100883 759 RGRHE 763
Cdd:PRK10261 250 TGSVE 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
555-754 |
1.16e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDI-SQVTQASLRSHIGVVPQDTVLFN 631
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqASNIRDTERAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 632 D-TIADNIRYGRvtagndEVEaaaqaagiHDAIMAFPEGYR----------------TQVGErglkLSGGEKQRVAIART 694
Cdd:PRK13549 96 ElSVLENIFLGN------EIT--------PGGIMDYDAMYLraqkllaqlkldinpaTPVGN----LGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 695 ILKAPGIILLDEATSALdTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK13549 158 LNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
544-741 |
2.00e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQaslrSHIGV 622
Cdd:TIGR03719 323 IEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ----SRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLfnDTIADNIRYGRVtaGNDEVEAAAQaagihdaIMAFP-EGYRTQ--VGErglkLSGGEKQRVAIARTiLKAP 699
Cdd:TIGR03719 398 DPNKTVW--EEISGGLDIIKL--GKREIPSRAY-------VGRFNfKGSDQQkkVGQ----LSGGERNRVHLAKT-LKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 700 G-IILLDEATSALDTSNERAIQASLAKV--CAnrttIVVAH------RLST 741
Cdd:TIGR03719 462 GnVLLLDEPTNDLDVETLRALEEALLNFagCA----VVISHdrwfldRIAT 508
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
543-706 |
2.03e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.47 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGV 622
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 623 VPQDTVLFNDTIADnirygrvtaGNDEVEAAAQAAGIHDAIMAfpEGYRTQVGE-RGLKLSGGEKQRVAIARTILKAPGI 701
Cdd:PRK10522 402 VFTDFHLFDQLLGP---------EGKPANPALVEKWLERLKMA--HKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470
|
....*
gi 1169100883 702 ILLDE 706
Cdd:PRK10522 471 LLLDE 475
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
563-767 |
2.09e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKSTilrLLFRFYDI--SSGCIRIDGQDISQVTQASLRSHIG-VVPQDTVLFNdtiADNIR 639
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFA---MPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 Y--------GRVTAGNDEVEAAAQAAGIHDAImafpegyrtqvgERGL-KLSGGEKQRVAIARTILK-APGI------IL 703
Cdd:PRK03695 89 YltlhqpdkTRTEAVASALNEVAEALGLDDKL------------GRSVnQLSGGEWQRVRLAAVVLQvWPDInpagqlLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLS-TVVNADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
558-754 |
5.58e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.66 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFY--DISSGC-IRIDGQDISQVTQASL-----RSHIGVVPQDTVL 629
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREGRLARdirksRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 FND-TIADNIRYGRVTA-----------GNDEVEAAAQAAgihdaimafpegyrTQVG------ERGLKLSGGEKQRVAI 691
Cdd:PRK09984 98 VNRlSVLENVLIGALGStpfwrtcfswfTREQKQRALQAL--------------TRVGmvhfahQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQG 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
563-754 |
1.06e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqvtqASLRSH----IGVVP--QDTVLFND-TIA 635
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-----EGLPGHqiarMGVVRtfQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 636 DNI---RYGRVTAG------------NDEVEAAAQAAGIHDAImafpeGYRTQVGERGLKLSGGEKQRVAIARTILKAPG 700
Cdd:PRK11300 99 ENLlvaQHQQLKTGlfsgllktpafrRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 701 IILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
560-761 |
1.71e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLfRFYDIS----SGCIRIDGQ--DISQVTQASlrshiGVVPQD------- 626
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMpiDAKEMRAIS-----AYVQQDdlfiptl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFNDTIADNIRYGRVTAGNDE---VEAAAQAAGIHDAimafpEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIIL 703
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKrerVDEVLQALGLRKC-----ANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 704 LDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVV--NADQILVIKDGCIVERGR 761
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELfeLFDKIILMAEGRVAYLGS 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
515-761 |
2.48e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 515 MENMFDLLkeetEVKDLpgagplrfqkgriefeNVHFSYADGRET-LQDVSFTVMPGQTLALVGPSGAGKS----TILRL 589
Cdd:PRK09473 6 QQQADALL----DVKDL----------------RVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSqtafALMGL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 590 LFRFYDISsGCIRIDGQDISQVTQASL---RSHigvvpQDTVLFNDTIADNIRYGRVTA----------GNDEVEAAAQA 656
Cdd:PRK09473 66 LAANGRIG-GSATFNGREILNLPEKELnklRAE-----QISMIFQDPMTSLNPYMRVGEqlmevlmlhkGMSKAEAFEES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 657 AGIHDAImAFPEGyRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASL--AKVCANRTTIV 734
Cdd:PRK09473 140 VRMLDAV-KMPEA-RKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIM 217
|
250 260
....*....|....*....|....*...
gi 1169100883 735 VAHRLSTVVN-ADQILVIKDGCIVERGR 761
Cdd:PRK09473 218 ITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
544-737 |
4.42e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQ--DISQVTQaslrSHIG 621
Cdd:PRK11819 325 IEAENLSKSFGD-RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVDQ----SRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDTVLfnDTIADNIRYGRVtaGNDEVEAAAQAAgihdaimAFpeGYRTQ-----VGErglkLSGGEKQRVAIARTiL 696
Cdd:PRK11819 399 LDPNKTVW--EEISGGLDIIKV--GNREIPSRAYVG-------RF--NFKGGdqqkkVGV----LSGGERNRLHLAKT-L 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1169100883 697 KAPG-IILLDEATSALDTSNERAIQASLAKV--CAnrttIVVAH 737
Cdd:PRK11819 461 KQGGnVLLLDEPTNDLDVETLRALEEALLEFpgCA----VVISH 500
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
560-772 |
7.20e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfYDI---SSGCIRIDGQDISQvTQASLRSHIGVV------------P 624
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKML---TGIlvpTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 625 QDTVLFNDTIadnirYgRVtagnDEVEAAAQAA------GIHDAImafpegyRTQVgeRglKLSGGEKQRVAIARTILKA 698
Cdd:COG4586 114 IDSFRLLKAI-----Y-RI----PDAEYKKRLDelvellDLGELL-------DTPV--R--QLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 699 PGIILLDEATSALDTSNERAIQASLAKVCANR-TTIVVA-HRLSTVVN-ADQILVIKDGCIVERGRHEALLSRGGVY 772
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
541-754 |
7.71e-12 |
|
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: 64.96 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 541 KGRIEFENVHFSYA---DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS--SGCIRIDGQDISQvtqaS 615
Cdd:cd03232 1 GSVLTWKNLNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHIGVVPQDTVLF-NDTIADNIRYgrvtagndeveaaaqAAGIhdaimafpegyrtqvgeRGLKLSggEKQRVAIART 694
Cdd:cd03232 77 FQRSTGYVEQQDVHSpNLTVREALRF---------------SALL-----------------RGLSVE--QRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 695 ILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVV--NADQILVIKDG 754
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSASIfeKFDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
553-712 |
8.11e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 553 YADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQASLRSHIGVVPQD------ 626
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KEFEGEARPAPGIKVGYLPQEpqldpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 -TVLFN---------------DTIADNirYGRVTAGND-------EVEAAAQAAGIHD-------AIMAF--PEGyRTQV 674
Cdd:PRK11819 85 kTVRENveegvaevkaaldrfNEIYAA--YAEPDADFDalaaeqgELQEIIDAADAWDldsqleiAMDALrcPPW-DAKV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1169100883 675 GerglKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PRK11819 162 T----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
219-502 |
1.42e-11 |
|
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: 65.92 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRR 298
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRG-------VFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVLRiadRGTSSVTGL---LSYLVFNVIPTLAdIIIGIIYFSMFFNAWFGLIVFLCM 375
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDKARTGDLMS---RCTSDVDTIrrfLAFGLVELVRAVL-LFIGALIIMFSINWKLTLISLAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 376 SLYLTLTIVVtewRTKFRRA----------MNT--QENATRARavdsllnfeTVKYYNAESYEVER-------YREAIIK 436
Cdd:cd18542 150 PFIALFSYVF---FKKVRPAfeeireqegeLNTvlQENLTGVR---------VVKAFAREDYEIEKfdkeneeYRDLNIK 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 437 YQGLEWKSSASLVLLNQTQNLVIGLGllagsllCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFG 502
Cdd:cd18542 218 LAKLLAKYWPLMDFLSGLQIVLVLWV-------GGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
548-730 |
1.63e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDT 627
Cdd:PRK13540 6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 VLFNDTIADNIRYgrvtagndEVEAAAQAAGIHDAIMAFPEGYRTQVgERGLkLSGGEKQRVAIARTILKAPGIILLDEA 707
Cdd:PRK13540 85 INPYLTLRENCLY--------DIHFSPGAVGITELCRLFSLEHLIDY-PCGL-LSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180
....*....|....*....|...
gi 1169100883 708 TSALDtsnERAIQASLAKVCANR 730
Cdd:PRK13540 155 LVALD---ELSLLTIITKIQEHR 174
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
557-765 |
2.21e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF-RFYDIS-SGCIRIDGQDIsqvTQASLRsHIGVVPQDTVLF-NDT 633
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKP---TKQILK-RTGFVTQDDILYpHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNI------RYGRVTAGNDEVEAAAQAAgihdAIMAFPEGYRTQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDE 706
Cdd:PLN03211 157 VRETLvfcsllRLPKSLTKQEKILVAESVI----SELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 707 ATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVNA--DQILVIKDG-CIVERGRHEAL 765
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSRVYQmfDSVLVLSEGrCLFFGKGSDAM 295
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
231-487 |
4.24e-11 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 64.77 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIV-NLLTEKApWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRRVELLIFSHLHE 309
Cdd:cd18570 16 LLGIAGSFFFQILIdDIIPSGD-INLLNIISIGLILLYLFQS-------LLSYIRSYLLLKLSQKLDIRLILGYFKHLLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 310 LSLRWHLGRRTGEVL-RIADrgTSSVTGLLSYLVFNV-IPTLADIIIGIIyfsMFFNAWF-GLIVFLCMSLYLTLTIVVT 386
Cdd:cd18570 88 LPLSFFETRKTGEIIsRFND--ANKIREAISSTTISLfLDLLMVIISGII---LFFYNWKlFLITLLIIPLYILIILLFN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 387 E-WRTKFRRAMntQENA-TRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLL 464
Cdd:cd18570 163 KpFKKKNREVM--ESNAeLNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
|
250 260
....*....|....*....|...
gi 1169100883 465 AGSLLCAYFVTEQKLQVGDYVLF 487
Cdd:cd18570 241 LILWIGSYLVIKGQLSLGQLIAF 263
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
569-741 |
4.72e-11 |
|
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: 61.62 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 569 PGQTLALVGPSGAGKSTILRLLFRFYDISS-GCIRIDGQDISQVTQASLRSHIgvvpqdtvlfndtiadnirygrvtagn 647
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 648 deveaaaqaagihdaimafpegyrtqVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASL---- 723
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
|
170 180
....*....|....*....|.
gi 1169100883 724 ---AKVCANRTTIVVAHRLST 741
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKD 128
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
560-758 |
5.93e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQ-----DISQvtqaSLRSHIGVVPQDTVLFND 632
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD----SEALGIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 633 -TIADNIRYGRVTAGN---DEVEAAAQAA------GIHDAimafPEgyrTQVGERGLklsgGEKQRVAIARTILKAPGII 702
Cdd:NF040905 93 lSIAENIFLGNERAKRgviDWNETNRRARellakvGLDES----PD---TLVTDIGV----GKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 703 LLDEATSALdtsNERAIQASLAKVCANR----TTIVVAHRLSTVVN-ADQILVIKDGCIVE 758
Cdd:NF040905 162 ILDEPTAAL---NEEDSAALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
544-760 |
7.80e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTqASLRSHIG 621
Cdd:CHL00131 8 LEIKNLHAS-VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 V------------VPQDTVLfndTIADNIRygRVTAGNDEVEAaaqaagihdaiMAFPEGYRTQVGERGLK--------- 680
Cdd:CHL00131 86 IflafqypieipgVSNADFL---RLAYNSK--RKFQGLPELDP-----------LEFLEIINEKLKLVGMDpsflsrnvn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 --LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAH--RLSTVVNADQILVIKDGC 755
Cdd:CHL00131 150 egFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
|
....*
gi 1169100883 756 IVERG 760
Cdd:CHL00131 230 IIKTG 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
559-754 |
9.38e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 559 TLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-------------VTQAslRSHIGVVPQ 625
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTEE--RRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFNDTIAdNIRYGRVTAG---NDEVEAAAQaaGIHDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGII 702
Cdd:PRK10982 341 LDIGFNSLIS-NIRNYKNKVGlldNSRMKSDTQ--WVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 703 LLDEATSALDTSNERAIQ---ASLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYqliAELAK--KDKGIIIISSEMPELLGiTDRILVMSNG 467
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
555-754 |
9.86e-11 |
|
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: 64.85 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDI-SQVTQASLRSHIGVVPQDTVLFN 631
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 632 D-TIADNIRYGRvtagndevEAAAQAAGIHDAIMAfpegYRTQVGERGLKLS------------GGEKQRVAIARTILKA 698
Cdd:TIGR02633 92 ElSVAENIFLGN--------EITLPGGRMAYNAMY----LRAKNLLRELQLDadnvtrpvgdygGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 699 PGIILLDEATSALdTSNERAIQASLAKVCANR--TTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:TIGR02633 160 ARLLILDEPSSSL-TEKETEILLDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
555-760 |
1.06e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS--------SGCIRIDGQDISQVTQASLRSHIGVVPQD 626
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TV-LFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPeGYRTQVGERGLKLSGGEKQRVAIARTILK-------- 697
Cdd:PRK13547 92 AQpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 698 -APGIILLDEATSALDTSNERAIQASLAKVCA--NRTTIVVAHRLSTVV-NADQILVIKDGCIVERG 760
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHG 237
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
219-509 |
1.47e-10 |
|
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: 62.91 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYR----NIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQF 294
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKilidDVLIQLGPGGNTSLLLLLVLGLAGAYVLSA-------LLGILRGRLLARLGER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 295 TSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIadrgTSSVTGLLSYLVFNVIPTLADII----IGIIYFSMffNAWFGL 369
Cdd:cd18563 74 ITADLRRDLYEHLQRLSLSFFDKRQTGSLMsRV----TSDTDRLQDFLSDGLPDFLTNILmiigIGVVLFSL--NWKLAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 370 IVFLCMSLYLTLTIVVteW---RTKFRR------AMNTQENatraravDSLLNFETVKYYNAESYEVERYREAIIKYQGL 440
Cdd:cd18563 148 LVLIPVPLVVWGSYFF--WkkiRRLFHRqwrrwsRLNSVLN-------DTLPGIRVVKAFGQEKREIKRFDEANQELLDA 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 441 EWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQ 509
Cdd:cd18563 219 NIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWIT 287
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
554-757 |
2.30e-10 |
|
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: 60.74 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 554 ADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQDISQVTQaSLRSHIGVVPQDTVLF 630
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAE-KYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 -NDTIADNIRYGRVTAGNDEVeaaaqaagihdaimafpegyrtqvgeRGLklSGGEKQRVAIARTILKAPGIILLDEATS 709
Cdd:cd03233 96 pTLTVRETLDFALRCKGNEFV--------------------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 710 ALDTSNerAIQ-ASLAKVCANRTtivvahRLSTVVNA-----------DQILVIKDGCIV 757
Cdd:cd03233 148 GLDSST--ALEiLKCIRTMADVL------KTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
557-754 |
3.53e-10 |
|
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: 63.31 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDIS-SGCIRIDGQDISQVT-QASLRSHIGVVPQDT------- 627
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgivp 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 628 ---VLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIH-----DAIMAFPEGyrtqvgerglKLSGGEKQRVAIARTILKAP 699
Cdd:TIGR02633 353 ilgVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQrlkvkTASPFLPIG----------RLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 700 GIILLDEATSALDTSNERAIQASLAKVCANRTT-IVVAHRLSTVVN-ADQILVIKDG 754
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEG 479
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
274-508 |
4.98e-10 |
|
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: 61.37 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 274 TGSTGFVSNLRTFLWIRV-QQFTSR-RVELliFSHLHELSLRWHLGRRTGEVLRiadRGTSSVTGLLSYLVFNVIPTLAD 351
Cdd:cd18564 64 ALLRGLASYAGTYLTALVgQRVVLDlRRDL--FAHLQRLSLSFHDRRRTGDLLS---RLTGDVGAIQDLLVSGVLPLLTN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 352 IIIGIIYFS-MFFNAW-FGLIVFLCMSLYLTLTIVVTEwrtKFRRAMNTQ---ENATRARAVDSLLNFETVKYYNAESYE 426
Cdd:cd18564 139 LLTLVGMLGvMFWLDWqLALIALAVAPLLLLAARRFSR---RIKEASREQrrrEGALASVAQESLSAIRVVQAFGREEHE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 427 VERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYR 506
Cdd:cd18564 216 ERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTG 295
|
..
gi 1169100883 507 MI 508
Cdd:cd18564 296 RI 297
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
556-754 |
1.02e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 556 GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIGVVPQD-TVLFNDT 633
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 IADNIRYGRVTAGNDEVEaaaQAAGIHDAIMAFPE-GYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALd 712
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFVD---QDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1169100883 713 TSNE-----RAIQASLAKVCAnrtTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK10982 166 TEKEvnhlfTIIRKLKERGCG---IVYISHKMEEIFQlCDEITILRDG 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
551-769 |
1.11e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQASLRSHIGVVPQD-- 626
Cdd:PRK13638 9 FRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 TVLFNDTIADNIRYGRVTAGNDEVEAAAQaagIHDAI-MAFPEGYRTQVGErglKLSGGEKQRVAIARTILKAPGIILLD 705
Cdd:PRK13638 88 QQIFYTDIDSDIAFSLRNLGVPEAEITRR---VDEALtLVDAQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 706 EATSALDTSNERAIQASLAKVCAN-RTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLSRG 769
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
543-764 |
1.39e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVhfsyaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQASLRSHIG 621
Cdd:PRK11288 257 RLRLDGL-----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 VVPQDT----VLFNDTIADNI----RYGRVTAG---NDEVEAAAQAAGIHDAIMAFPEGyRTQVGerglKLSGGEKQRVA 690
Cdd:PRK11288 332 LCPEDRkaegIIPVHSVADNInisaRRHHLRAGcliNNRWEAENADRFIRSLNIKTPSR-EQLIM----NLSGGNQQKAI 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 691 IARTILKAPGIILLDEATSALDTSNERAIQA---SLAKvcANRTTIVVAHRLSTVVN-ADQILVIKDGCIV-ERGRHEA 764
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDVGAKHEIYNviyELAA--QGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELAREQA 483
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
537-771 |
1.41e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 537 LRFQKGR------IEFENVHFSYaDGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIridgqdisq 610
Cdd:PRK15064 307 IRFEQDKklhrnaLEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 611 vtQASLRSHIGVVPQDTV--------LFN-----DTIADN---IR--YGRVTAGNDEVEAAAQAagihdaimafpegyrt 672
Cdd:PRK15064 377 --KWSENANIGYYAQDHAydfendltLFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSVKV---------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVcaNRTTIVVAHRLSTVVN-ADQILVI 751
Cdd:PRK15064 439 --------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EGTLIFVSHDREFVSSlATRIIEI 508
|
250 260
....*....|....*....|.
gi 1169100883 752 KDGCIVE-RGRHEALLSRGGV 771
Cdd:PRK15064 509 TPDGVVDfSGTYEEYLRSQGI 529
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
551-737 |
1.72e-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: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 551 FSYADGRETLQDVSFTVMPG-----QTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQAslrshigVVPQ 625
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFNDTIADNIR-YGRVTAGNDEVEAAAQAAGIHDaimafpegyrTQVGErglkLSGGEKQRVAIARTILKAPGIILL 704
Cdd:cd03237 74 YEGTVRDLLSSITKdFYTHPYFKTEIAKPLQIEQILD----------REVPE----LSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1169100883 705 DEATSALDtSNERAIQASLAKVCA---NRTTIVVAH 737
Cdd:cd03237 140 DEPSAYLD-VEQRLMASKVIRRFAennEKTAFVVEH 174
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
542-756 |
1.98e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 542 GRIEFENVHFSYAD----GRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYD-ISSGCIRIDGQ--DISQVTQA 614
Cdd:PRK13549 256 GEVILEVRNLTAWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 615 sLRSHIGVVPQD-----TVLFNDtIADNIR---YGRVTAGNdEVEAAAQAAGIHDAI------MAFPEgyrTQVGerglK 680
Cdd:PRK13549 336 -IAQGIAMVPEDrkrdgIVPVMG-VGKNITlaaLDRFTGGS-RIDDAAELKTILESIqrlkvkTASPE---LAIA----R 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 LSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQ---ASLAK--VCanrtTIVVAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYkliNQLVQqgVA----IIVISSELPEVLGlSDRVLVMHEG 481
|
..
gi 1169100883 755 CI 756
Cdd:PRK13549 482 KL 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
562-756 |
2.16e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 562 DVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QASLRSHIGVVPQD----------TVLF 630
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDrkrdglvlgmSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 631 NDTIAdNIRYGRVTAGNDEVEAAAQAAGihDAIMAFpeGYRTQVGER--GLkLSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:PRK10762 350 NMSLT-ALRYFSRAGGSLKHADEQQAVS--DFIRLF--NIKTPSMEQaiGL-LSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1169100883 709 SALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDGCI 756
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSIIlVSSEMPEVLGmSDRILVMHEGRI 473
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
563-767 |
2.44e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 563 VSFTVMPGQTLALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVvpQDTVLFNDTIAD-N 637
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGA--EVAMIFQDPMTSlN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 638 IRYgrvTAGNDEVEA------AAQAAGIHDAIMAFpegyrTQVG----ERGL-----KLSGGEKQRVAIARTILKAPGII 702
Cdd:PRK11022 104 PCY---TVGFQIMEAikvhqgGNKKTRRQRAIDLL-----NQVGipdpASRLdvyphQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 703 LLDEATSALDTSneraIQASLAKVC------ANRTTIVVAHRLSTVVN-ADQILVIKDGCIVERGRHEALLS 767
Cdd:PRK11022 176 IADEPTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
555-729 |
2.99e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 555 DGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRS------HIGVvpqDTV 628
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGI---KTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 629 LfndTIADNIR-YGRVTAGNDEvEAAAQAAGihdaimafpegyrtQVGERGLK------LSGGEKQRVAIARTILKAPGI 701
Cdd:PRK13538 89 L---TALENLRfYQRLHGPGDD-EALWEALA--------------QVGLAGFEdvpvrqLSAGQQRRVALARLWLTRAPL 150
|
170 180
....*....|....*....|....*...
gi 1169100883 702 ILLDEATSALDTSNERAIQASLAKVCAN 729
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQ 178
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
550-752 |
6.69e-09 |
|
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: 55.83 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 550 HFSYADGretlQDVSFTvmPGQTLALVGPSGAGKSTILRllfrfyDISSGCIRidgqdisqvTQASLRSHIGVVPQDTVl 629
Cdd:cd03227 7 FPSYFVP----NDVTFG--EGSLTIITGPNGSGKSTILD------AIGLALGG---------AQSATRRRSGVKAGCIV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 fndtiadnirygrvtagndeveaAAQAAGIHDAIMafpegyrtqvgerglKLSGGEKQRVAIA-----RTILKAPgIILL 704
Cdd:cd03227 65 -----------------------AAVSAELIFTRL---------------QLSGGEKELSALAlilalASLKPRP-LYIL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1169100883 705 DEATSALDTSNERAIQASLAK-VCANRTTIVVAHRLSTVVNADQILVIK 752
Cdd:cd03227 106 DEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
544-712 |
7.04e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCI--------------RIDGQDIS 609
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 610 Q------------VTQASLRSHIGvvpqdtvlfndtiadniRYGrvTAGNdeveaaaqaagihdaiMAFPEGYrtqvger 677
Cdd:PLN03073 589 SnpllymmrcfpgVPEQKLRAHLG-----------------SFG--VTGN----------------LALQPMY------- 626
|
170 180 190
....*....|....*....|....*....|....*
gi 1169100883 678 glKLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PLN03073 627 --TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
565-712 |
1.67e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.63 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 565 FTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQA---SLRSHIGVVPQDTVLFNDTIADNIRYG 641
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfmAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 642 RvtagndeveAAAQAAGIHDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:PRK13543 112 R---------RAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
217-515 |
1.95e-08 |
|
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: 56.69 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGlerALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQgggTGSTGFVSNLRTFLWIRVQqfTS 296
Cdd:cd18549 5 FLDLFCAVLIA---ALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILR---TLLNYFVTYWGHVMGARIE--TD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 297 RRVELliFSHLHELSLRWHLGRRTGEVLriadrgtSSVTGLLSYlvfnvIPTLA-----DIIIGIIYFS------MFFNA 365
Cdd:cd18549 77 MRRDL--FEHLQKLSFSFFDNNKTGQLM-------SRITNDLFD-----ISELAhhgpeDLFISIITIIgsfiilLTINV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 366 WFGLIVFLCMSLYLTLTIvvtewrtKFRRAMNTQENATR-------ARAVDSLLNFETVKYYNAESYEVERYREAIIKYQ 438
Cdd:cd18549 143 PLTLIVFALLPLMIIFTI-------YFNKKMKKAFRRVRekigeinAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 439 GLEWKS-------SASLVLLNQTQNLVIGLGLlagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNwfgtyyRMIqtN 511
Cdd:cd18549 216 ESKKKAykamayfFSGMNFFTNLLNLVVLVAG-------GYFIIKGEITLGDLVAFLLYVNVFIKPIR------RLV--N 280
|
....
gi 1169100883 512 FIDM 515
Cdd:cd18549 281 FTEQ 284
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
544-762 |
2.08e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSyADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDIS------------ 609
Cdd:PRK09580 2 LSIKDLHVS-VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLelspedragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 610 -------------------QVTQASLRSHIGVVPQDTVLFNDTIADNIRygrvtagndeveaaaqaagihdaIMAFPEGY 670
Cdd:PRK09580 81 fmafqypveipgvsnqfflQTALNAVRSYRGQEPLDRFDFQDLMEEKIA-----------------------LLKMPEDL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 671 RTQVGERGlkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKV-CANRTTIVVAH--RLSTVVNADQ 747
Cdd:PRK09580 138 LTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLrDGKRSFIIVTHyqRILDYIKPDY 215
|
250
....*....|....*
gi 1169100883 748 ILVIKDGCIVERGRH 762
Cdd:PRK09580 216 VHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
222-440 |
2.99e-08 |
|
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: 55.95 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 222 CLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRRVEL 301
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQA-------VFSFFRIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 302 LIFSHLHELSLRWHLGRRTGEVL-RIadrgTSSVTGLLSYLVFNVIPTLADIIIGIIyfsmffnawfGLIVFLCMSLYLT 380
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTsRL----SNDVTQIQDTLTTTLAEFLRQILTLIG----------GVVLLFFISWKLT 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 381 L--------TIVVTEWRTKFRRAMNTQENATRARAV----DSLLNFETVKYYNAESYEVERYREAIIKYQGL 440
Cdd:cd18576 140 LlmlatvpvVVLVAVLFGRRIRKLSKKVQDELAEANtiveETLQGIRVVKAFTREDYEIERYRKALERVVKL 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
538-737 |
5.24e-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: 56.33 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 538 RFQKGRIEFEnVH-----------FSYADGRETLQDVSFTVMPGQ-----TLALVGPSGAGKSTILRLLfrfydisSGCI 601
Cdd:COG1245 319 RIRDEPIEFE-VHaprrekeeetlVEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKIL-------AGVL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 602 RIDGQDISqvtqASLRshIGVVPQ----DtvlFNDTIADNIRygrvTAGNDEVEAAAqaagihdaimafpegYRTQVGER 677
Cdd:COG1245 391 KPDEGEVD----EDLK--ISYKPQyispD---YDGTVEEFLR----SANTDDFGSSY---------------YKTEIIKP 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 678 -GLK---------LSGGEKQRVAIARTILKAPGIILLDEATSALDtSNERAIQAS-LAKVCANR--TTIVVAH 737
Cdd:COG1245 443 lGLEklldknvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRLAVAKaIRRFAENRgkTAMVVDH 514
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
514-758 |
5.92e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 514 DMENMFDLLKEETEVKDlpgagplrfQKGRIEFENVhFSYADGRetLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRF 593
Cdd:PRK09700 245 ELQNRFNAMKENVSNLA---------HETVFEVRNV-TSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 594 YDISSGCIRIDGQDISQVTQ-ASLRSHIGVVPQ---DTVLF-NDTIADNI---------RYGRVTAGNDEVEAAAQAAGI 659
Cdd:PRK09700 313 DKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSIAQNMaisrslkdgGYKGAMGLFHEVDEQRTAENQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 660 HDAIMAFPEGYRTQVGErglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVC-ANRTTIVVAHR 738
Cdd:PRK09700 393 RELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSE 468
|
250 260
....*....|....*....|.
gi 1169100883 739 LSTVVNA-DQILVIKDGCIVE 758
Cdd:PRK09700 469 LPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
219-512 |
6.66e-08 |
|
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: 54.78 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQgggtgstgFVSNlrtFLWIRVQQFTSRR 298
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVN--------WVAS---RLRIYLMAKVGQR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLI----FSHLHELSLRWHLGRRTGEVL-R-IADrgTSSVTGLLSYLVFNVIPTLAdIIIGIIYFSMFFNAWFGLIVF 372
Cdd:cd18545 71 ILYDLrqdlFSHLQKLSFSFFDSRPVGKILsRvIND--VNSLSDLLSNGLINLIPDLL-TLVGIVIIMFSLNVRLALVTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLyltLTIVVTEWRTKFRRA----------MNT--QENATRARavdsllnfeTVKYYNAESYEVERYREAIIKYQGl 440
Cdd:cd18545 148 AVLPL---LVLVVFLLRRRARKAwqrvrkkisnLNAylHESISGIR---------VIQSFAREDENEEIFDELNRENRK- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 441 EWKSSASLV-LLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNF 512
Cdd:cd18545 215 ANMRAVRLNaLFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAM 287
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
548-712 |
9.42e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 548 NVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLF-RFY--DISsGCIRIDGQ--DISQVTQA-------- 614
Cdd:NF040905 264 TVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYgrNIS-GTVFKDGKevDVSTVSDAidaglayv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 615 -SLRSHIGVVPQDTVLFNDTIA--DNIRYGRVTAGNDEVEAAaqaagihdaimafpEGYRTQ-------VGERGLKLSGG 684
Cdd:NF040905 343 tEDRKGYGLNLIDDIKRNITLAnlGKVSRRGVIDENEEIKVA--------------EEYRKKmniktpsVFQKVGNLSGG 408
|
170 180
....*....|....*....|....*...
gi 1169100883 685 EKQRVAIARTILKAPGIILLDEATSALD 712
Cdd:NF040905 409 NQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
538-737 |
1.06e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 538 RFQKGRIEFE----------NVHFSYADGRETLQDVSFTVMPGQ-----TLALVGPSGAGKSTILRLLfrfydisSGCIR 602
Cdd:PRK13409 318 RIRPEPIEFEerpprdeserETLVEYPDLTKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLL-------AGVLK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 603 IDGQDISqvtqASLRshIGVVPQ-------DTV-LFNDTIADNIR---YgrvtagNDEVeaaAQAAGIHDaIMafpegyr 671
Cdd:PRK13409 391 PDEGEVD----PELK--ISYKPQyikpdydGTVeDLLRSITDDLGssyY------KSEI---IKPLQLER-LL------- 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 672 tqvgERGLK-LSGGEKQRVAIARTILKAPGIILLDEATSALDtSNERAIQAS-LAKVCANR--TTIVVAH 737
Cdd:PRK13409 448 ----DKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRLAVAKaIRRIAEEReaTALVVDH 512
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
569-741 |
1.33e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 569 PGQTLALVGPSGAGKSTILRLL-----------------------FR-------FYDISSGCIRIdgqdiSQVTQaslrs 618
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlkrFRgtelqdyFKKLANGEIKV-----AHKPQ----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 619 HIGVVPQdtvLFNDTIADnirygrVTAGNDE---VEAAAQAAGIhDAIMafpegyrtqvgERGLK-LSGGEKQRVAIART 694
Cdd:COG1245 168 YVDLIPK---VFKGTVRE------LLEKVDErgkLDELAEKLGL-ENIL-----------DRDISeLSGGELQRVAIAAA 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 695 ILKAPGIILLDEATSALDTsNER-----AIQaSLAKvcANRTTIVVAHRLST 741
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDI-YQRlnvarLIR-ELAE--EGKYVLVVEHDLAI 274
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
558-754 |
1.55e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 558 ETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV-TQASLRSHIGVVPQD---TVLFNDT 633
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYLPEDrqsSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 634 -IADNI---RYGRVTAGNDEVEAAAQAAGIHDAImafpeGYRTQVGERGLK-LSGGEKQRVAIARTILKAPGIILLDEAT 708
Cdd:PRK15439 357 pLAWNVcalTHNRRGFWIKPARENAVLERYRRAL-----NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1169100883 709 SALDTSNERAIQASLAKVCANRTTIV-VAHRLSTVVN-ADQILVIKDG 754
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQG 479
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
566-739 |
1.95e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 566 TVMPGQTLALVGPSGAGKSTILRLL-----------------------FR-------FYDISSGCIRIdgqdiSQVTQas 615
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlkrFRgtelqnyFKKLYNGEIKV-----VHKPQ-- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 lrsHIGVVPQdtvLFNDTIADNIRygrvtaGNDEveaaaqaAGIHDAImafpegyrtqVGERGLK---------LSGGEK 686
Cdd:PRK13409 168 ---YVDLIPK---VFKGKVRELLK------KVDE-------RGKLDEV----------VERLGLEnildrdiseLSGGEL 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 687 QRVAIARTILKAPGIILLDEATSALDTsNER-----AIQaSLAKvcaNRTTIVVAHRL 739
Cdd:PRK13409 219 QRVAIAAALLRDADFYFFDEPTSYLDI-RQRlnvarLIR-ELAE---GKYVLVVEHDL 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
544-790 |
2.22e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 544 IEFENVHFSYAdGRETLQDVSFTVMPGQTLALVGPSGAGKSTILR--LLFRFYDISSGCI------RIDGQDISqVTQAS 615
Cdd:PLN03073 178 IHMENFSISVG-GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQilhveqEVVGDDTT-ALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 616 LRSHI---------------------------GVVPQDTVLFNDTIADNIR--YGRVTAgNDEVEAAAQAAGIHDAIMAF 666
Cdd:PLN03073 256 LNTDIertqlleeeaqlvaqqrelefetetgkGKGANKDGVDKDAVSQRLEeiYKRLEL-IDAYTAEARAASILAGLSFT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 667 PEGYRtqvgERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKvcANRTTIVVAHR---LSTVV 743
Cdd:PLN03073 335 PEMQV----KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK--WPKTFIVVSHArefLNTVV 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 744 N-----ADQILVIKDGC--IVERGRHEALLSrggvyadmwqlQQGQEETSEDTK 790
Cdd:PLN03073 409 TdilhlHGQKLVTYKGDydTFERTREEQLKN-----------QQKAFESNERSR 451
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
278-487 |
2.49e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.98 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 278 GFVSNLRTFLWIrvqqFTSRRVEL----LIFSHLHELSLRWHLGRRTGEVL-RIADRGTssvtgLLSYLVFNVIPTLADI 352
Cdd:cd18782 56 AVLTALRTYLFT----DTANRIDLelggTIIDHLLRLPLGFFDKRPVGELStRISELDT-----IRGFLTGTALTTLLDV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 353 IIGIIYFS-MFFNAWF-GLIVFLCMSLYLTLTIVVTE-WRTKFRRAMnTQENATRARAVDSLLNFETVKYYNAESYEVER 429
Cdd:cd18782 127 LFSVIYIAvLFSYSPLlTLVVLATVPLQLLLTFLFGPiLRRQIRRRA-EASAKTQSYLVESLTGIQTVKAQNAELKARWR 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169100883 430 YREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLF 487
Cdd:cd18782 206 WQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
219-509 |
4.49e-07 |
|
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: 52.42 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGGGTgstgFVSNlrtFLWIRVQQFTSRR 298
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLAS----YLQT---YLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 299 VELLIFSHLHELSLRWHLGRRTGEVL-RI---ADRGTSSVTGLLSYLVFNVIptladIIIGIIYFSMFFNAWFGLIVFLC 374
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLIsRItndVNQVQNALTSALTVLVRDPL-----TVIGLLGVLFYLDWKLTLIALVV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 375 MSLyltLTIVVTEWRTKFRR-AMNTQENATR--ARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKS---SASL 448
Cdd:cd18552 149 LPL---AALPIRRIGKRLRKiSRRSQESMGDltSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIaraRALS 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 449 VLLNQTQN-----LVIGLGllagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQ 509
Cdd:cd18552 226 SPLMELLGaiaiaLVLWYG--------GYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQ 283
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
217-510 |
6.10e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 51.77 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGLeraLNVLVPIFYRNIVNLLTE-KAPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSNlrtflwiRVQQFT 295
Cdd:cd18778 2 ILTLLCALLSTL---LGLVPPWLIRELVDLVTIgSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNH-------VAEQKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 296 SRRVELLIFSHLHELSLRWHLGRRTGEVL-RIADrGTSSVTGLLSYLVFNVIPT-LADIIIGIIYFSMffNAWFGLIVFL 373
Cdd:cd18778 72 VADLRSDLYDKLQRLSLRYFDDRQTGDLMsRVIN-DVANVERLIADGIPQGITNvLTLVGVAIILFSI--NPKLALLTLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 374 CMSLYLTLTIVVTEW-RTKFRR------AMNtqenatrARAVDSLLNFETVKYYNAESYEVERYREAIIKYQ-------- 438
Cdd:cd18778 149 PIPFLALGAWLYSKKvRPRYRKvrealgELN-------ALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRkaqlramk 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 439 -------GLEWKSSASLVLlnqtqnlVIGLGllagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQT 510
Cdd:cd18778 222 lwaifhpLMEFLTSLGTVL-------VLGFG--------GRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQR 285
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
560-736 |
8.58e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLL----FRFYDISSGCIRIDG---QDISQ------VTQASLRSHIGVVP-Q 625
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGitpEEIKKhyrgdvVYNAETDVHFPHLTvG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 626 DTVLFndtiADNIRygrvTAGN-----DEVEAAAQAAGIHDAIMAFPEGYRTQVGE---RGLklSGGEKQRVAIARTILK 697
Cdd:TIGR00956 157 ETLDF----AARCK----TPQNrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1169100883 698 APGIILLDEATSALDTSNERAIQASLaKVCAN--RTTIVVA 736
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRAL-KTSANilDTTPLVA 266
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
231-498 |
1.60e-06 |
|
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: 50.49 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEK-APWNSLAWTVTSYVFLKFLQGGGTgstgfvsnlrtFLWiRVQQF-TSRRVELL----IF 304
Cdd:cd18541 13 LLQLLIPRIIGRAIDALTAGtLTASQLLRYALLILLLALLIGIFR-----------FLW-RYLIFgASRRIEYDlrndLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 305 SHLHELSLRWHLGRRTGEVlrIAdRGTSSVTGLLSYLVFNVIpTLADII---IGIIYFSMFFNAWFGLIVFLCMSLyltL 381
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDL--MA-RATNDLNAVRMALGPGIL-YLVDALflgVLVLVMMFTISPKLTLIALLPLPL---L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 382 TIVVTEW----RTKFRRAMNTQENATrARAVDSLLNFETVKYYNAESYEVERYREAIIKYQglewKSSASLV----LLNQ 453
Cdd:cd18541 154 ALLVYRLgkkiHKRFRKVQEAFSDLS-DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYV----EKNLRLArvdaLFFP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1169100883 454 TQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18541 229 LIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPM 273
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
231-494 |
2.11e-06 |
|
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: 50.25 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRRVELLIFSHLHEL 310
Cdd:cd18557 10 AAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQS-------VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 311 SLRWHLGRRTGEVL-RIA-DRGT--SSVTGLLSYLVFNVIptladIIIGIIYFsMFFNAW-FGLIVFLCMSLYLTLTIVV 385
Cdd:cd18557 83 EIAFFDKHKTGELTsRLSsDTSVlqSAVTDNLSQLLRNIL-----QVIGGLII-LFILSWkLTLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 386 TEWRTKFRRAMntQENATRARAV--DSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGL 463
Cdd:cd18557 157 GRYIRKLSKEV--QDALAKAGQVaeESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234
|
250 260 270
....*....|....*....|....*....|.
gi 1169100883 464 LAGSLLCAYFVTEQKLQVGDYVLFGTYIIQL 494
Cdd:cd18557 235 LLVLWYGGYLVLSGQLTVGELTSFILYTIMV 265
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
543-715 |
2.68e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRL--------------LFrfydissGCIRIDGQDI 608
Cdd:PRK10938 260 RIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltLF-------GRRRGSGETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 609 SQVTQaslrsHIGVVP-------------QDTVL--FNDTIadniryGRVTAGNDEVEAAAQA----AGIHDAIMAFPeg 669
Cdd:PRK10938 332 WDIKK-----HIGYVSsslhldyrvstsvRNVILsgFFDSI------GIYQAVSDRQQKLAQQwldiLGIDKRTADAP-- 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1169100883 670 YRTqvgerglkLSGGEKQRVAIARTILKAPGIILLDEATSALDTSN 715
Cdd:PRK10938 399 FHS--------LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
560-749 |
3.91e-06 |
|
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: 49.15 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTIL---------RLLFRFYDISSGCIRIDG-QDISQVTQASlRSHIGVVPQDTVL 629
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGlEHIDKVIVID-QSPIGRTPRSNPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 630 FNDTIADNIR--YGRVTAG---NDE------------------VEAAAQ----AAGIHDAIMAFPE---GYrTQVGERGL 679
Cdd:cd03271 90 TYTGVFDEIRelFCEVCKGkryNREtlevrykgksiadvldmtVEEALEffenIPKIARKLQTLCDvglGY-IKLGQPAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 680 KLSGGEKQRVAIARTILKA---PGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVA-HRLSTVVNADQIL 749
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWII 242
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
217-510 |
5.12e-06 |
|
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: 48.97 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGleRALNVLVPIFYRNIVNLLTEKAP-WNSLAWTVTSYVFLKFLQGGGT---GSTG--FVSNLRTFLWir 290
Cdd:cd18551 1 LILALLLSLLG--TAASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSyllGRTGerVVLDLRRRLW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 291 vqqftsrrvellifSHLHELSLRWHLGRRTGEVL-RIadrgtSSVTGLLSYLVFNVIPTLAD---IIIGIIYFSMFFNAW 366
Cdd:cd18551 77 --------------RRLLRLPVSFFDRRRSGDLVsRV-----TNDTTLLRELITSGLPQLVTgvlTVVGAVVLMFLLDWV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 367 FGLIVFLCMSLYLTLTIVVTewrTKFRRA-MNTQENATR--ARAVDSLLNFETVKYYNAESYEVERYREAI--IKYQGLe 441
Cdd:cd18551 138 LTLVTLAVVPLAFLIILPLG---RRIRKAsKRAQDALGElsAALERALSAIRTVKASNAEERETKRGGEAAerLYRAGL- 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 442 wKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQT 510
Cdd:cd18551 214 -KAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQK 281
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
217-499 |
8.67e-06 |
|
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: 48.55 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGlerALNVLVPIFYRNIVNLLTEkaPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSN-LRTFLWIRVQQFT 295
Cdd:cd18547 2 ILVIILAIIST---LLSVLGPYLLGKAIDLIIE--GLGGGGGVDFSGLLRILLLLLGLYLLSALFSyLQNRLMARVSQRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 296 SRRVELLIFSHLHELSLRWHLGRRTGEVL-RI---ADRGTSSVTGLLSYLVFNVIptladIIIGIIYFsMFF-NAWFGLI 370
Cdd:cd18547 77 VYDLRKDLFEKLQRLPLSYFDTHSHGDIMsRVtndVDNISQALSQSLTQLISSIL-----TIVGTLIM-MLYiSPLLTLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 371 VFLCMSLYLTLTIVVTEW-RTKFRR------AMN--TQENATraravdsllNFETVKYYNAESYEVERYREAIIKYQGLE 441
Cdd:cd18547 151 VLVTVPLSLLVTKFIAKRsQKYFRKqqkalgELNgyIEEMIS---------GQKVVKAFNREEEAIEEFDEINEELYKAS 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 442 WKSS--ASLV-----LLNQTQNLVIglgllagSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLN 499
Cdd:cd18547 222 FKAQfySGLLmpimnFINNLGYVLV-------AVVGGLLVINGALTVGVIQAFLQYSRQFSQPIN 279
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
569-740 |
9.28e-06 |
|
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: 48.13 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 569 PGQTLALVGPSGAGKSTILRLLfrfydisSG------CIRIDGQDISQVtqasLRSHIGVVPQD--TVLFNDTI------ 634
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKIL-------AGklkpnlGKFDDPPDWDEI----LDEFRGSELQNyfTKLLEGDVkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 635 --ADNIRygRVTAGN-DEVEAAAQAAGIHDAIMAFPEgyRTQVGERGL-KLSGGEKQRVAIARTILKAPGIILLDEATSA 710
Cdd:cd03236 94 qyVDLIP--KAVKGKvGELLKKKDERGKLDELVDQLE--LRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|....
gi 1169100883 711 LDT----SNERAIQaSLAKvcANRTTIVVAHRLS 740
Cdd:cd03236 170 LDIkqrlNAARLIR-ELAE--DDNYVLVVEHDLA 200
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
294-487 |
9.87e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 48.33 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 FTSRRVELLIFS----HLHELSLRWHLGRRTGEVL-RIADRGTssvtgLLSYLVFNVIPTLADIIIGIIYFSMFF--NAW 366
Cdd:cd18568 68 YFANRIDLSLLSdfykHLLSLPLSFFASRKVGDIItRFQENQK-----IRRFLTRSALTTILDLLMVFIYLGLMFyyNLQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 367 FGLIVFLCMSLYLTLTIVVtewrTKFRRAMNTQENATRARA----VDSLLNFETVKYYNAESYEVERYREAIIKYQGLEW 442
Cdd:cd18568 143 LTLIVLAFIPLYVLLTLLS----SPKLKRNSREIFQANAEQqsflVEALTGIATIKALAAERPIRWRWENKFAKALNTRF 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1169100883 443 KSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLF 487
Cdd:cd18568 219 RGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAF 263
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
560-752 |
1.10e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 560 LQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLrSHIGvvPQDTVLFNDTIADNIR 639
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 640 Y-GRVTAGNDEVEAAAQAAGIHDAImafpegyrtqvGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNeRA 718
Cdd:PRK13541 93 FwSEIYNSAETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN-RD 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1169100883 719 IQASLAKVCANRTTIVV--AHRLSTVVNAdQILVIK 752
Cdd:PRK13541 161 LLNNLIVMKANSGGIVLlsSHLESSIKSA-QILQLD 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
679-754 |
1.30e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 679 LKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNE----RAIQASLAKvcANRTTIVVAHRLSTVVNADQILVIKDG 754
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEE--GKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
657-749 |
1.51e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 657 AGIHdaIMAFPEGYRTQvgerGLK-LSGGEKQRVAIAR--TILK---APgIILLDEATSALDTSN-ERAiqASLAKVCAN 729
Cdd:TIGR02168 1071 AGIE--IFAQPPGKKNQ----NLSlLSGGEKALTALALlfAIFKvkpAP-FCILDEVDAPLDDANvERF--ANLLKEFSK 1141
|
90 100
....*....|....*....|.
gi 1169100883 730 RTT-IVVAHRLSTVVNADQIL 749
Cdd:TIGR02168 1142 NTQfIVITHNKGTMEVADQLY 1162
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
223-515 |
3.45e-05 |
|
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: 46.38 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 223 LGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLqgggtgsTGFVSNLRTFLWIRVQQFTSRRVELL 302
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVL-------SGLFSGLRGGCFSYAGTRLVRRLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 303 IFSHLHELSLRWHLGRRTGEVL-RI-ADrgTSSVTGLLSYLVFNVIPTLADIIIGIIYfsMFFNAWF-GLIVFLCMslyl 379
Cdd:cd18572 75 LFRSLLRQDIAFFDATKTGELTsRLtSD--CQKVSDPLSTNLNVFLRNLVQLVGGLAF--MFSLSWRlTLLAFITV---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 380 TLTIVVTEWRTKFRRAMNTQENATRAR----AVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQ 455
Cdd:cd18572 147 PVIALITKVYGRYYRKLSKEIQDALAEanqvAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 456 NLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFgtyiiQLYmpLNWFGTYYRMIQTNFIDM 515
Cdd:cd18572 227 TLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTF-----MLY--QQQLGEAFQSLGDVFSSL 279
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
547-723 |
5.48e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 547 ENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfydisSGciridgqdisqvTQASLRSHIGvvpqd 626
Cdd:PRK10636 316 EKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AG------------ELAPVSGEIG----- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 627 tvlfndtIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPE------------GYR-TQVGERGLKLSGGEKQRVAIAR 693
Cdd:PRK10636 371 -------LAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQEleqklrdylggfGFQgDKVTEETRRFSGGEKARLVLAL 443
|
170 180 190
....*....|....*....|....*....|
gi 1169100883 694 TILKAPGIILLDEATSALDTSNERAIQASL 723
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
352-498 |
9.03e-05 |
|
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: 45.08 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 352 IIIGIIYFSMFFNAWFGLIVFLCMSLyLTLTIVVTEWRT--KFRR------AMN--TQENATRARavdsllnfeTVKYYN 421
Cdd:cd18548 126 MLIGAIIMAFRINPKLALILLVAIPI-LALVVFLIMKKAipLFKKvqkkldRLNrvVRENLTGIR---------VIRAFN 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 422 AESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18548 196 REDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
231-502 |
1.14e-04 |
|
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: 44.78 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGGGTGstgfvsnLRTFLWIRVQQFTSRRVELLIFSHLHEL 310
Cdd:cd18543 13 LAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSF-------LRRYLAGRLSLGVEHDLRTDLFAHLQRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 311 SLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMffNAWFGLIVFLCMSLyltLTIVVTEWRT 390
Cdd:cd18543 86 DGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLVL--SPPLALVALASLPP---LVLVARRFRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 391 KFRRAMNT--QENATRARAVD-SLLNFETVKYYNAESYEVERYREAIIKYQGLEWKS-------SASLVLLNQ-TQNLVI 459
Cdd:cd18543 161 RYFPASRRaqDQAGDLATVVEeSVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAarlrarfWPLLEALPElGLAAVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1169100883 460 GLGllagsllcAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFG 502
Cdd:cd18543 241 ALG--------GWLVANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
251-502 |
1.19e-04 |
|
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: 44.86 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 251 APWNSLAWTVTS----YVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVL-- 324
Cdd:cd18565 37 LPLVPASLGPADprgqLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMsv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 325 ---------RIADRGTSSVTGLLSYLVFnviptladiiIGIIYFSMffNAWFGLIVFLCMSLyltlTIVVTEWrtkFRRA 395
Cdd:cd18565 117 lnndvnqleRFLDDGANSIIRVVVTVLG----------IGAILFYL--NWQLALVALLPVPL----IIAGTYW---FQRR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 396 MNTQENATR-------ARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEW---KSSASLVLLNQtqnLVIGLGLLA 465
Cdd:cd18565 178 IEPRYRAVReavgdlnARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWraiRLRAAFFPVIR---LVAGAGFVA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1169100883 466 GSLLCAYFVTE------QKLQVGDYVLFGTYIIQLYMPLNWFG 502
Cdd:cd18565 255 TFVVGGYWVLDgpplftGTLTVGTLVTFLFYTQRLLWPLTRLG 297
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
681-749 |
1.31e-04 |
|
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: 43.47 E-value: 1.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169100883 681 LSGGEKQRVAIARTILKAPG--IILLDEATSALDTSNERAIQASLAK-VCANRTTIVVAHRLSTVVNADQIL 749
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWII 159
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
549-767 |
1.83e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 549 VHFSYADGRETLQD-VSFTVMPGQTLALVGPSGAGKSTILRLL--------------FRFYDISSGCI------RIDGQD 607
Cdd:PRK15093 11 IEFKTSDGWVKAVDrVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDDIDLLRLsprerrKLVGHN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 608 ISQVTQAslrshigvvPQDTVLFNDTIADNIR------------YGRVTAGNDEVEAAAQAAGI--HDAIM-AFPegyrt 672
Cdd:PRK15093 91 VSMIFQE---------PQSCLDPSERVGRQLMqnipgwtykgrwWQRFGWRKRRAIELLHRVGIkdHKDAMrSFP----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 673 qvgergLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANR-TTI-VVAHRLSTVVN-ADQIL 749
Cdd:PRK15093 157 ------YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTIlLISHDLQMLSQwADKIN 230
|
250
....*....|....*...
gi 1169100883 750 VIKDGCIVERGRHEALLS 767
Cdd:PRK15093 231 VLYCGQTVETAPSKELVT 248
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
303-498 |
2.57e-04 |
|
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: 43.95 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 303 IFSHLHELSLRWHLGRRTGEVLriaDRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFS-MFFnawfgLIVFLCMSLYLTL 381
Cdd:cd18554 85 LFDHLQKLSLRYYANNRSGEII---SRVINDVEQTKDFITTGLMNIWLDMITIIIAICiMLV-----LNPKLTFVSLVIF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 382 TIVVTEWRTKFRRAMNTQENATRARAVDSLLNFE------TVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQ 455
Cdd:cd18554 157 PFYILAVKYFFGRLRKLTKERSQALAEVQGFLHEriqgmsVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAV 236
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1169100883 456 NLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18554 237 NTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPL 279
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
217-510 |
6.21e-04 |
|
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: 42.50 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 217 LVVLICLGLMGLErALNVLVPIFYRNIVN--LLTEKAPW-NSLAWTVTSYVFLKFLqgggtgstgfVSNLRTFLWIRVQQ 293
Cdd:cd18555 3 LLISILLLSLLLQ-LLTLLIPILTQYVIDnvIVPGNLNLlNVLGIGILILFLLYGL----------FSFLRGYIIIKLQT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 FTSRRVELLIFSHLHELSLRWHLGRRTGEVL-RIadrgtSSVTGLLSYLVFNVIPTLADIIIGIIYFSM--FFNAWFGLI 370
Cdd:cd18555 72 KLDKSLMSDFFEHLLKLPYSFFENRSSGDLLfRA-----NSNVYIRQILSNQVISLIIDLLLLVIYLIYmlYYSPLLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 371 VFLCMSLYLTLTIVVtewrTKFRRAMNTQENATRARA----VDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSA 446
Cdd:cd18555 147 VLLLGLLIVLLLLLT----RKKIKKLNQEEIVAQTKVqsylTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKER 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169100883 447 SLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQT 510
Cdd:cd18555 223 LSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFIL 286
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
283-452 |
6.37e-04 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 42.49 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 283 LRTFLWIRvqqfTSRRVELL----IFSHLHELSLRWHLGRRTGEVL-RIadRGTSSVTgllSYLVFNVIPTLADIIIGII 357
Cdd:cd18588 61 LRTYLFSH----TTNRIDAElgarLFRHLLRLPLSYFESRQVGDTVaRV--RELESIR---QFLTGSALTLVLDLVFSVV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 358 YFS-MFFNAWF-GLIVFLCMSLYLTLTIVVTEwrtKFRRAMNTQ-ENATRARA--VDSLLNFETVKYYNAESYEVERYRE 432
Cdd:cd18588 132 FLAvMFYYSPTlTLIVLASLPLYALLSLLVTP---ILRRRLEEKfQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEE 208
|
170 180
....*....|....*....|
gi 1169100883 433 AIIKYQglewKSSASLVLLN 452
Cdd:cd18588 209 LLARYV----KASFKTANLS 224
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
681-749 |
6.41e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.68 E-value: 6.41e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169100883 681 LSGGEKQRVAIAR--TILK---APgIILLDEATSALDTSN-ERAiqASLAKVCANRT-TIVVAHRLSTVVNADQIL 749
Cdd:cd03278 114 LSGGEKALTALALlfAIFRvrpSP-FCVLDEVDAALDDANvERF--ARLLKEFSKETqFIVITHRKGTMEAADRLY 186
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
555-613 |
7.42e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.61 E-value: 7.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 555 DGRETLQDVsftvMPGQTLALVGPSGAGKSTILRLLFrfydissGCIRIDGQDISQVTQ 613
Cdd:cd01854 74 EGLDELREL----LKGKTSVLVGQSGVGKSTLLNALL-------PELVLATGEISEKLG 121
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
569-604 |
1.28e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 1.28e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1169100883 569 PGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRID 604
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVRED 229
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
231-434 |
1.40e-03 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 41.46 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEkapWNSLAWTVTSYVFLKFLqggGTGSTGFVSNLRTFLWIRvqqftsRRVELLI--FSHLH 308
Cdd:cd18562 13 GVQFAEPVLFGRVVDALSS---GGDAFPLLALWAALGLF---SILAGVLVALLADRLAHR------RRLAVMAsyFEHVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 309 ELSLRWHLGRRTGEVLRIADRGTSSVTGL-LSYLVFNvIPTLADIIIgIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTE 387
Cdd:cd18562 81 TLPLSFHSQRGSGRLLRIMLRGTDALFGLwLGFFREH-LAALVSLIV-LLPVALWMNWRLALLLVVLAAVYAALNRLVMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1169100883 388 wRTKFR-RAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAI 434
Cdd:cd18562 159 -RTKAGqAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGIT 205
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
298-499 |
1.52e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 41.31 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 298 RVELliFSHLHELSLRWHLGRRTGEVL-RIA-DRG--TSSVTGLLSYLVFNVIPTLADIIIgiiyfsMFFNAW-FGLIVF 372
Cdd:cd18550 75 RVQL--YAHLQRMSLAFFTRTRTGEIQsRLNnDVGgaQSVVTGTLTSVVSNVVTLVATLVA------MLALDWrLALLSL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 373 LCMSLYLTLTIVVTEWRTKFRRAmnTQE-NATRARAVDSLLN---FETVKYYNAESYEVERYREAIIKYQGLEWKSSASL 448
Cdd:cd18550 147 VLLPLFVLPTRRVGRRRRKLTRE--QQEkLAELNSIMQETLSvsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAG 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1169100883 449 VLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLN 499
Cdd:cd18550 225 RWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLT 275
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
568-617 |
1.73e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 40.17 E-value: 1.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1169100883 568 MPGQTLALVGPSGAGKSTILRLL-----FRFYDissgcirIDgQDISQVTQASLR 617
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLakrlgYDFID-------TD-HLIEARAGKSIP 48
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
669-749 |
2.03e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 669 GYrTQVGERGLKLSGGEKQRVAIARTILK---APGIILLDEATSALDTSNERAIQASLAKVCANRTTIVV-AHRLSTVVN 744
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKT 897
|
....*
gi 1169100883 745 ADQIL 749
Cdd:TIGR00630 898 ADYII 902
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
543-754 |
2.14e-03 |
|
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: 40.28 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 543 RIEFENVHfSYADgretlqDVSFTVMPGQTLaLVGPSGAGKSTILR-LLFRFYDISSGCIRIDGQDISQVTQASLRSHIg 621
Cdd:cd03240 3 KLSIRNIR-SFHE------RSEIEFFSPLTL-IVGQNGAGKTTIIEaLKYALTGELPPNSKGGAHDPKLIREGEVRAQV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 622 vvpqdTVLFNDTIADNIRYGRvtagndEVEAAAQAAGIH----DAIMAFPEGYrtqvgerglkLSGGEKQ------RVAI 691
Cdd:cd03240 74 -----KLAFENANGKKYTITR------SLAILENVIFCHqgesNWPLLDMRGR----------CSGGEKVlasliiRLAL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 692 ARTILKAPGIILLDEATSALDTSNeraIQASLA------KVCANRTTIVVAHRLSTVVNADQIL-VIKDG 754
Cdd:cd03240 133 AETFGSNCGILALDEPTTNLDEEN---IEESLAeiieerKSQKNFQLIVITHDEELVDAADHIYrVEKDG 199
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
219-509 |
2.25e-03 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 40.83 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVN--LLTEKAPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSN---LRTFLWIRVQq 293
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQklgQRIIYDLRRD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 294 ftsrrvellIFSHLHELSLRWHLGRRTGEVL-RIA-DrgTSSVTGLLSYLVFNVIptlADI--IIGIIYFSMFFNAWFGL 369
Cdd:cd18544 80 ---------LFSHIQRLPLSFFDRTPVGRLVtRVTnD--TEALNELFTSGLVTLI---GDLllLIGILIAMFLLNWRLAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 370 IVFLCMSLYLTLTIVvtewrtkFRRAMNTQENATRAR--AVDSLLN-----FETVKYYNAESYEVERYRE---------- 432
Cdd:cd18544 146 ISLLVLPLLLLATYL-------FRKKSRKAYREVREKlsRLNAFLQesisgMSVIQLFNREKREFEEFDEinqeyrkanl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 433 AIIKYQGL-----EWKSSASLVLLnqtqnLVIglgllagsllCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRM 507
Cdd:cd18544 219 KSIKLFALfrplvELLSSLALALV-----LWY----------GGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNI 283
|
..
gi 1169100883 508 IQ 509
Cdd:cd18544 284 LQ 285
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
681-761 |
2.65e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 681 LSGGEKQRVAIARTI-LKAPGII-LLDEATSALDTSNERAIQASLAKV-CANRTTIVVAHRLSTVVNADQILVIKDGCIV 757
Cdd:cd03270 138 LSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIGPGAGV 217
|
....
gi 1169100883 758 ERGR 761
Cdd:cd03270 218 HGGE 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
681-749 |
3.69e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169100883 681 LSGGEKQRVAIARTIL---KAPGIILLDEATSALDTSNERA-IQASLAKVCANRTTIVVAHRLSTVVNADQIL 749
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
557-712 |
3.69e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 557 RETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLfrfydisSGCIRIDGQDISQVTQASLrshiGVVPQDTVLFN----D 632
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQL----AWVNQETPALPqpalE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 633 TIADNIRYGR-----VTAGNDEVE--AAAQAAGIHDAIMAFPEGYRTQVGERGL------------KLSGGEKQRVAIAR 693
Cdd:PRK10636 83 YVIDGDREYRqleaqLHDANERNDghAIATIHGKLDAIDAWTIRSRAASLLHGLgfsneqlerpvsDFSGGWRMRLNLAQ 162
|
170
....*....|....*....
gi 1169100883 694 TILKAPGIILLDEATSALD 712
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLD 181
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
219-498 |
4.17e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 39.93 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 219 VLICLGLMGLERALNVLVPIFYRNIVNLLTEKA--PWNSLAWTVTSYVFL----KFLQgggtgstgFVSN-LRTFLWIRV 291
Cdd:cd18556 4 FFSILFISLLSSILISISPVILAKITDLLTSSSsdSYNYIVVLAALYVITisatKLLG--------FLSLyLQSSLRVEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 292 QQFTSRRVELLIFSHLHELSLRwhlgRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIV 371
Cdd:cd18556 76 IISISSSYFRYLYEQPKTFFVK----ENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 372 FLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIK---YQGLEWKSSASL 448
Cdd:cd18556 152 LLYAVLFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNdrnSQKRYWKLTFKM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1169100883 449 VLLNQTQNLVIGLGLLAGSLlcaYFVTEQKLQVGDYVLFGTYIIQLYMPL 498
Cdd:cd18556 232 LILNSLLNVILFGLSFFYSL---YGVVNGQVSIGHFVLITSYILLLSTPI 278
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
231-436 |
4.38e-03 |
|
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: 39.77 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 231 ALNVLVPIFYRNIVNLLTEKAPWNS----LAWTVTSYVFLKFLQGGGTGSTGFVSnlrTFLWIRVQQFTSRRVELLIFSH 306
Cdd:cd18577 13 AALPLMTIVFGDLFDAFTDFGSGESspdeFLDDVNKYALYFVYLGIGSFVLSYIQ---TACWTITGERQARRIRKRYLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169100883 307 LHELSLRWHLGRRTGEVL-RIAD------RGTSSVTGLLsylvfnvIPTLADIIIGIIyFSMFFNAWFGLIVfLCMSLYL 379
Cdd:cd18577 90 LLRQDIAWFDKNGAGELTsRLTSdtnliqDGIGEKLGLL-------IQSLSTFIAGFI-IAFIYSWKLTLVL-LATLPLI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169100883 380 TLTIVVTEWRTKfRRAMNTQENATRARAV--DSLLNFETVKYYNAESYEVERYREAIIK 436
Cdd:cd18577 161 AIVGGIMGKLLS-KYTKKEQEAYAKAGSIaeEALSSIRTVKAFGGEEKEIKRYSKALEK 218
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
555-590 |
4.58e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 4.58e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1169100883 555 DGRETLQDVsftvMPGQTLALVGPSGAGKSTILRLL 590
Cdd:pfam03193 95 EGIEALKEL----LKGKTTVLAGQSGVGKSTLLNAL 126
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
544-610 |
5.67e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 5.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169100883 544 IEFENVHFSYADgRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 610
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD 67
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
573-620 |
6.27e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.71 E-value: 6.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1169100883 573 LALVGPSGAGKSTILRLLFRFYDI-SSGCIRIDGQdiSQVTQASLRSHI 620
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEvRDSVVFVDLP--SGTSPKDLLRAL 54
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
575-595 |
8.35e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 37.51 E-value: 8.35e-03
|
| |
