|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
232-830 |
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: 786.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 232 STDPRSTWRDLGRKLRLLSGYLWPRGSPSLQLTVLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLA--WTVTTY 309
Cdd:COG5265 5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVpvGLLLAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 310 VFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVF 389
Cdd:COG5265 85 GLLRLL------SVLF-GELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 390 NIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAE 469
Cdd:COG5265 158 NILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 470 GYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGT 549
Cdd:COG5265 238 AREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 550 YYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGK 629
Cdd:COG5265 318 VYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 630 STILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAI 709
Cdd:COG5265 398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 710 LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVV 789
Cdd:COG5265 478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 18034785 790 NADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQQQGQE 830
Cdd:COG5265 558 DADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
232-829 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 564.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 232 STDPRSTWRDLgrkLRLLSGYLWPrgspslqltVLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVF 311
Cdd:COG1132 2 SKSPRKLLRRL---LRYLRPYRGL---------LILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 312 LKFLQGggtgstgFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNI 391
Cdd:COG1132 70 LALLRA-------LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 392 IPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGY 471
Cdd:COG1132 143 VRSVV-TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREER 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 472 ELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYY 551
Cdd:COG1132 222 ELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 552 RMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKST 631
Cdd:COG1132 302 NQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKST 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 632 ILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILS 711
Cdd:COG1132 382 LVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 712 FPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNA 791
Cdd:COG1132 462 LPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNA 541
|
570 580 590
....*....|....*....|....*....|....*...
gi 18034785 792 DQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQQQGQ 829
Cdd:COG1132 542 DRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
268-564 |
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: 535.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSK---APWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18581 1 CLLLLAAGRVVNVLVPILYKKIVDSLTPDsadSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 345 VELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 424
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 425 LILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMV 504
Cdd:cd18581 161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 505 IGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18581 241 ITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
590-825 |
1.90e-156 |
|
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: 455.92 E-value: 1.90e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 750 LDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQ 825
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
231-826 |
7.74e-137 |
|
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: 423.09 E-value: 7.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 231 RSTDPRSTWRDLGRKLRLLSGYLWprgspslqlTVLLCMGLMGLdraLNVLVPIFYRDIVNLLTSKAPWSSLaWTVTtyv 310
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLL---------QVLLASLLINL---LALATPLFTQVVIDRVLPNQDLSTL-WVLA--- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 311 flkFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RIvdRGTSSVTGLLSYLVF 389
Cdd:COG2274 200 ---IGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAsRF--RDVESIREFLTGSLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 390 NiipTLADIIIGIIYFSM--FFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYN 467
Cdd:COG2274 275 T---ALLDLLFVLIFLIVlfFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 468 AEGYELERYREAILKFQGLEWKS---TASLVLLNQTQNMVIGFGLLAgslLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:COG2274 352 AESRFRRRWENLLAKYLNARFKLrrlSNLLSTLSGLLQQLATVALLW---LGAYLVIDGQLTLGQLIAFNILSGRFLAPV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 545 NWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYA-DGRETLQDVSFTVMPGQTVALVG 623
Cdd:COG2274 429 AQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 624 PSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAA 703
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 704 GIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAH 783
Cdd:COG2274 589 GLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 18034785 784 RLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQQ 826
Cdd:COG2274 669 RLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
268-564 |
6.75e-125 |
|
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: 376.95 E-value: 6.75e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSkAPWSSLAWTVTTYVFLKFLQGggtgSTGFVSNLRTFLWIRVQQFTSRGVEL 347
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTL-AKVKDLESAVTLILLYALLRF----SSKLLKELRSLLYRRVQQNAYRELSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLIL 427
Cdd:cd18560 76 KTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 428 TIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGF 507
Cdd:cd18560 156 TIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 508 GLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18560 236 GLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
590-822 |
8.96e-115 |
|
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: 348.45 E-value: 8.96e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMW 822
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
253-825 |
5.51e-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: 5.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 253 LWPRGSPSLQLTVLLCMGlMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgSTGFVSnlrTF 332
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVA-MILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRG----ICSFVS---TY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 333 LWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNiipTLadIIIGIIYFSMF 408
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLsRItfdSEQVASAATDAFIVLVRE---TL--TVIGLFIVLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 409 FNAWFGLIVFLcmsLYLILTIMVTEWRAKFRR-DMNTQE-NATRARAVDSLL-NFETVKYYNAEGYELERYREAILKFQG 485
Cdd:TIGR02203 152 YSWQLTLIVVV---MLPVLSILMRRVSKRLRRiSKEIQNsMGQVTTVAEETLqGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 486 LEWKSTASLVLLNQTQNMVIGFGLlAGSLLCAYFVSER-RLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLAL-AVVLFIALFQAQAgSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 565 FDLLKEETEVKDvpGAGPLRFHKGRVEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS 643
Cdd:TIGR02203 308 FTLLDSPPEKDT--GTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 644 SGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRV-TAGDSEIQAAAQAAGIHDAILSFPEGYETQVGE 722
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 723 RGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCI 802
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|...
gi 18034785 803 IERGRHEALLSRGGVYAEMWQLQ 825
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHNMQ 568
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
350-821 |
5.72e-110 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 348.87 E-value: 5.72e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 350 FSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLlsYLVF--NIIPTLADIIIgIIYFSMFFNAWFGLIVFLCMSLYLIL 427
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALFGL--WLEFmrEHLATLVALVV-LLPLALFMNWRLSLVLVVLGIVYTLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 428 TIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYN---AEGYELERYREAILKFQG--LEWKSTAS-LVLLNQTQ 501
Cdd:PRK13657 173 TTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIADNLLAAQMpvLSWWALASvLNRAASTI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 502 NMVIGFgllagsLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAG 581
Cdd:PRK13657 253 TMLAIL------VLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 582 PLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS 661
Cdd:PRK13657 327 DLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTI 741
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 742 LKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEM 821
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
590-825 |
3.46e-108 |
|
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: 331.43 E-value: 3.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAD--GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQ 825
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
268-564 |
2.30e-107 |
|
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: 331.42 E-value: 2.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 268 CMGLMGLDRALNVLVPIFYRDIVNLLT---SKAPWSSlawtVTTYVFLKFLQGGGtgstgFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLSggsGKSPWKE----IGLYVLLRFLQSGG-----GLGLLRSWLWIPVEQYSYRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 345 VELRLFSHLHELSLRWHLGRRTGEVLRIVDRGtSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 424
Cdd:cd18583 72 LSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQG-SSINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 425 LILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMV 504
Cdd:cd18583 151 VWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 505 IGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18583 231 LTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
588-816 |
1.91e-106 |
|
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: 326.49 E-value: 1.91e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGG 816
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
268-564 |
2.33e-102 |
|
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: 318.29 E-value: 2.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLA--WTVTTYVFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRGV 345
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVplLLLLAYGLARIL------SSLF-NELRDALFARVSQRAVRRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 346 ELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYL 425
Cdd:cd18582 74 ALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 426 ILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVI 505
Cdd:cd18582 154 AFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALII 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 506 GFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18582 234 SLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
348-816 |
1.37e-99 |
|
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: 320.55 E-value: 1.37e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGtssVTGLLSYLVfNIIP--TLADIIIGIIYFSMFFNAWF-GLIVFLCMSLy 424
Cdd:COG4988 96 RLLEKLLALGPAWLRGKSTGELATLLTEG---VEALDGYFA-RYLPqlFLAALVPLLILVAVFPLDWLsGLILLVTAPL- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 425 LILTIMVTEWRAKfrrDMNTQENATRARA----VDSLLNFETVKYYNAEGYEL-------ERYREA---ILKFQ-----G 485
Cdd:COG4988 171 IPLFMILVGKGAA---KASRRQWRALARLsghfLDRLRGLTTLKLFGRAKAEAeriaeasEDFRKRtmkVLRVAflssaV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 486 LEWKSTAS--LVLLnqtqnmVIGFGLLAGSLLcayfvserrLQVGDFVLFgtyitqL----YMPLNWFGTYY--RMIQTN 557
Cdd:COG4988 248 LEFFASLSiaLVAV------YIGFRLLGGSLT---------LFAALFVLL------LapefFLPLRDLGSFYhaRANGIA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 558 FidMENMFDLLkEETEVKDVPGAGPLRFHKG-RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL 636
Cdd:COG4988 307 A--AEKIFALL-DAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 637 FRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGY 716
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGL 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 717 ETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILV 796
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILV 543
|
490 500
....*....|....*....|
gi 18034785 797 IKDGCIIERGRHEALLSRGG 816
Cdd:COG4988 544 LDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
324-825 |
3.30e-98 |
|
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: 317.41 E-value: 3.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 324 GFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEvlrIVDRGTSSVTGLLSYLVFNIIPTLADIIIGII 403
Cdd:TIGR02204 72 ALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGE---VVSRLTTDTTLLQSVIGSSLSMALRNALMCIG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 404 YFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQEN--ATRARAVDSLLNFETVKYYNAEGYELERYREAIL 481
Cdd:TIGR02204 149 GLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRiaDAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 482 KFQGLEWKSTASLVLLNqTQNMVIGFGLLAGSL-LCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFID 560
Cdd:TIGR02204 229 KAYEAARQRIRTRALLT-AIVIVLVFGAIVGVLwVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 561 MENMFDLLKEETEVK--DVPGAGPLRFhKGRVEFENVHFSYADGRET--LQDVSFTVMPGQTVALVGPSGAGKSTILRLL 636
Cdd:TIGR02204 308 AERLIELLQAEPDIKapAHPKTLPVPL-RGEIEFEQVNFAYPARPDQpaLDGLNLTVRPGETVALVGPSGAGKSTLFQLL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 637 FRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGY 716
Cdd:TIGR02204 387 LRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGY 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 717 ETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILV 796
Cdd:TIGR02204 467 DTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVV 546
|
490 500
....*....|....*....|....*....
gi 18034785 797 IKDGCIIERGRHEALLSRGGVYAEMWQLQ 825
Cdd:TIGR02204 547 MDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MTABC_N |
pfam16185 |
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ... |
6-255 |
1.29e-96 |
|
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: 301.50 E-value: 1.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 6 NYCEAEGPAGPAWTQNGLSPCFFYTLVPSTLMTLGVLALVLVLPCRRRevpAGTEeLSWAAGPRVAPYALQLSLAILQMA 85
Cdd:pfam16185 1 SYCEPNVSLTPVWVDHGLSPCFYDTLVPSVLLGFLLLFGTIQLIMYRK---YGTP-MEPKFIPRSRLYVLQLFLALLLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 86 LPLASLAGRVGTARGVRLPGYLLLASVLESLASACGLWLLVVERSQARQSLAMgvwmkFRHSLGLLLLWTVTFAAENLVL 165
Cdd:pfam16185 77 LALARFILRAALIGGGRLYGYMVLYACLSLLAWPFSLALLRLERRYALPSLPT-----RGHGLVLLLFWTLAFVAENLAF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 166 VSWNSPQWWWSRADLGQQVQFGLWVLRYMTSGGLFILGLWAPGLRPQSYTLHVNEEDQDGGRNQ---GRSTDPRSTWRDL 242
Cdd:pfam16185 152 VSWNSPDWWWGLETLSDQVEFGLFVVRYVCTLLLFVLGLKAPGLPRKPYMLLINEDERDVESSQpllGDSEENGSTWRNF 231
|
250
....*....|...
gi 18034785 243 GRKLRLLSGYLWP 255
Cdd:pfam16185 232 GKKLRLLWPYLWP 244
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
347-824 |
7.74e-94 |
|
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: 305.54 E-value: 7.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 347 LRLFSHLHELSLRWHLGRRTGEVL-RIVdrgtSSVTGLLSYLVFNIIPTLADI--IIGIIYFSMFFNAWFGLIVFLCMSL 423
Cdd:COG4987 92 VRLYRRLEPLAPAGLARLRSGDLLnRLV----ADVDALDNLYLRVLLPLLVALlvILAAVAFLAFFSPALALVLALGLLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 424 YLILTIMVTEWRAKFR-RDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQN 502
Cdd:COG4987 168 AGLLLPLLAARLGRRAgRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 503 MVIGFGLLAGSLLCAYFVSERRLQVGDFVLFgtyitqLYMPLNWF-------GTYYRMIQTnfID-MENMFDLLKEETEV 574
Cdd:COG4987 248 LAAGLAVVAVLWLAAPLVAAGALSGPLLALL------VLAALALFealaplpAAAQHLGRV--RAaARRLNELLDAPPAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 575 KDvPGAGPLRFHKGRVEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD 653
Cdd:COG4987 320 TE-PAEPAPAPGGPSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 654 ISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQ 733
Cdd:COG4987 399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLS 813
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
490
....*....|.
gi 18034785 814 RGGVYAEMWQL 824
Cdd:COG4987 559 QNGRYRQLYQR 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
296-825 |
7.13e-90 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 295.39 E-value: 7.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 296 KAPWSSLAWTVTTYVFLKFLQGggtgSTGFVSNLrTFLWI--RVQQFTSRgvelRLFSHLHELSLRWHLGRRTGEVLRIV 373
Cdd:PRK11176 58 KADRSVLKWMPLVVIGLMILRG----ITSFISSY-CISWVsgKVVMTMRR----RLFGHMMGMPVSFFDKQSTGTLLSRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 374 DRGTSSVTGLLSYLVFNIIPTLADIIIgiIYFSMFFNAW-FGLIVFLCMSLYLILTIMVTEwraKFR---RDMNTQENAT 449
Cdd:PRK11176 129 TYDSEQVASSSSGALITVVREGASIIG--LFIMMFYYSWqLSLILIVIAPIVSIAIRVVSK---RFRnisKNMQNTMGQV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 450 RARAVDSLLNFETVKYYNAEGYELERYREAI--LKFQGLEWKSTASLvlLNQTQNMVIGFGLlAGSLLCAYFVSERR-LQ 526
Cdd:PRK11176 204 TTSAEQMLKGHKEVLIFGGQEVETKRFDKVSnrMRQQGMKMVSASSI--SDPIIQLIASLAL-AFVLYAASFPSVMDtLT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 527 VGDF-VLFGTYITqLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEvKDVpGAGPLRFHKGRVEFENVHFSYaDGRET 605
Cdd:PRK11176 281 AGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE-KDE-GKRVIERAKGDIEFRNVTFTY-PGKEV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 --LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANN 683
Cdd:PRK11176 357 paLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 684 IRYGRV-TAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNE 762
Cdd:PRK11176 437 IAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 763 RAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQ 825
Cdd:PRK11176 517 RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
590-825 |
1.01e-83 |
|
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: 267.43 E-value: 1.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQ 825
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
77-821 |
1.24e-81 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 276.99 E-value: 1.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 77 LSLAILQMALPLASLAGRVGT-------ARGVRLPGYLLLA----SVLESLASACGLWLLVVERSQARQSLAMGVWMKFR 145
Cdd:TIGR00958 10 FSLLLVDWALLRDLLQGIFGLllpfekgLYVLWLEGTLRLGvlwlGALGILLNKAGGLLAAVKPLVAALCLATPSLSSLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 146 hslgLLLLWTVTFAAENLVLVSWNSPQWWWSRADLGQqvqfGLWVlrymtsgglFILGLWAPGLrpqsytlhvneEDQDG 225
Cdd:TIGR00958 90 ----ALAFWEALDPAVRVALGLWSWFVWSYGAALPAA----ALWA---------VLSSAGASEK-----------EAEQG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 226 GRNQGrstdprstwrDLGRKLRLLSGYLWPRGSPSLQLTVLLCMGLMgldralnvLVPIFYRDIVNLLTSKAPWSSLAWT 305
Cdd:TIGR00958 142 QSETA----------DLLFRLLGLSGRDWPWLISAFVFLTLSSLGEM--------FIPFYTGRVIDTLGGDKGPPALASA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 306 VTtyvFLKFLQGGGTGSTGFVSNLRTFLWIRVQqftsRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLS 385
Cdd:TIGR00958 204 IF---FMCLLSIASSVSAGLRGGSFNYTMARIN----LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLS 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 386 YLVfNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDmnTQENATRARAV--DSLLNFETV 463
Cdd:TIGR00958 277 LNV-NVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEE--LQEAVAKANQVaeEALSGMRTV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 464 KYYNAEGYELERYREAILKFQGLEWKStASLVLLNQTQNMVIGFGLLAGSLLC-AYFVSERRLQVGDFVLFGTYITQLYM 542
Cdd:TIGR00958 354 RSFAAEEGEASRFKEALEETLQLNKRK-ALAYAGYLWTTSVLGMLIQVLVLYYgGQLVLTGKVSSGNLVSFLLYQEQLGE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 543 PLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFhKGRVEFENVHFSYAD--GRETLQDVSFTVMPGQTVA 620
Cdd:TIGR00958 433 AVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNL-EGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 621 LVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAA 700
Cdd:TIGR00958 512 LVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAA 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 701 QAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKvcTNRTTIV 780
Cdd:TIGR00958 592 KAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLL 669
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 18034785 781 VAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEM 821
Cdd:TIGR00958 670 IAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
350-821 |
1.19e-80 |
|
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: 270.99 E-value: 1.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 350 FSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGL-LSYLVFNIIPTLADIIIGIIYFSMffNAWFGLIVFLCMSLYLILT 428
Cdd:TIGR01192 96 FGRIISMPLSWHQQRGTSNALHTLLRATETLFGLwLEFMRQHLATFVALFLLIPTAFAM--DWRLSIVLMVLGILYILIA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 429 IMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYN---AEGYELERYREAILKFQG--LEWKSTASLvlLNQTQNM 503
Cdd:TIGR01192 174 KLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNrieAETSALKQFTNNLLSAQYpvLDWWALASG--LNRMAST 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 504 VigfGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPL 583
Cdd:TIGR01192 252 I---SMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPEL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 584 RFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLR 663
Cdd:TIGR01192 329 PNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILK 743
Cdd:TIGR01192 409 KSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILK 488
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 744 APDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEM 821
Cdd:TIGR01192 489 NAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
590-800 |
1.90e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 256.16 E-value: 1.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFNDTIANNIrygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
289-797 |
9.33e-71 |
|
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: 242.58 E-value: 9.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 289 IVNLLTSKAPWSSLAWTVTTY---VFLKFLQGGGTGSTGFVSNLRtflwIRVQqftsrgVELRLFSHLHELSLRWHLGRR 365
Cdd:TIGR02857 30 VDGLISAGEPLAELLPALGALalvLLLRALLGWLQERAAARAAAA----VKSQ------LRERLLEAVAALGPRWLQGRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 366 TGEVLRIVDRGTSSVTGLLS-YLVFNIiptLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNT 444
Cdd:TIGR02857 100 SGELATLALEGVEALDGYFArYLPQLV---LAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 445 QENATRARAV-DSLLNFETVKYYNAEGYEL-------ERYRE--------AILKFQGLEWKSTASLVLLNqtqnMVIGFG 508
Cdd:TIGR02857 177 AALSRLSGHFlDRLRGLPTLKLFGRAKAQAaairrssEEYRErtmrvlriAFLSSAVLELFATLSVALVA----VYIGFR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 509 LLAGSLLcayfvserrLQVGDFVLFgtYITQLYMPLNWFGTYY--RMIQTNFIdmENMFDLLKEET----EVKDVPGAGP 582
Cdd:TIGR02857 253 LLAGDLD---------LATGLFVLL--LAPEFYLPLRQLGAQYhaRADGVAAA--EALFAVLDAAPrplaGKAPVTAAPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 583 LRfhkgrVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL 662
Cdd:TIGR02857 320 SS-----LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTIL 742
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVI 797
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
588-806 |
2.56e-68 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 225.55 E-value: 2.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03245 1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERG 806
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
587-802 |
1.28e-67 |
|
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: 223.89 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 587 KGRVEFENVHFSYAD--GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS 664
Cdd:cd03248 9 KGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 665 HIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCI 802
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
567-826 |
1.87e-67 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 234.61 E-value: 1.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 567 LLKEETEVKDvpGAGPLRFHKGRVEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSG 645
Cdd:PRK10789 293 MLAEAPVVKD--GSEPVPEGRGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 646 CIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGL 725
Cdd:PRK10789 371 DIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGV 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 726 KLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIER 805
Cdd:PRK10789 451 MLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
250 260
....*....|....*....|.
gi 18034785 806 GRHEALLSRGGVYAEMWQLQQ 826
Cdd:PRK10789 531 GNHDQLAQQSGWYRDMYRYQQ 551
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
220-821 |
3.70e-67 |
|
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: 237.15 E-value: 3.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 220 EEDQDGGRnqgrstdPRSTWRDLGRKLRLLsgylwpRGSPSLQLTVLLCMGLMGLdrALNVLVPIFYRDIvnLLTSKAPW 299
Cdd:TIGR03796 130 PEFQKGGR-------KPSLLRALWRRLRGS------RGALLYLLLAGLLLVLPGL--VIPAFSQIFVDEI--LVQGRQDW 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 300 -----SSLAWTVTTYVFLKFLQGGGTgstgfvsnlrtflwIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEvlrIVD 374
Cdd:TIGR03796 193 lrpllLGMGLTALLQGVLTWLQLYYL--------------RRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGD---IAS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 375 RgTSSVTGLLSYLVFNIIPTLADIIIGIIYFS-MF-FNAWFGLIVfLCMSLyliLTIMVTEWRAKFRRDMNTQENATRAR 452
Cdd:TIGR03796 256 R-VQLNDQVAEFLSGQLATTALDAVMLVFYALlMLlYDPVLTLIG-IAFAA---INVLALQLVSRRRVDANRRLQQDAGK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 453 ----AVDSLLNFETVKYYNAE--------GYelerYREAILKFQGLEwKSTASL----VLLNQTQNMVIgfgLLAGSLLc 516
Cdd:TIGR03796 331 ltgvAISGLQSIETLKASGLEsdffsrwaGY----QAKLLNAQQELG-VLTQILgvlpTLLTSLNSALI---LVVGGLR- 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 517 ayfVSERRLQVGDFVLFGTYITQLYMPLN---WFGTYYRMIQTNFID----MENMFDLLKEETEVKDvPGAGPLRFHKGR 589
Cdd:TIGR03796 402 ---VMEGQLTIGMLVAFQSLMSSFLEPVNnlvGFGGTLQELEGDLNRlddvLRNPVDPLLEEPEGSA-ATSEPPRRLSGY 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:TIGR03796 478 VELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAM 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:TIGR03796 558 VDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSIL 637
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 749 LLDEATSALDTSNERAIQASLAKV-CTnrtTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEM 821
Cdd:TIGR03796 638 ILDEATSALDPETEKIIDDNLRRRgCT---CIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
588-806 |
8.66e-66 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 218.52 E-value: 8.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGEYS--DEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 746 DIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERG 806
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
509-830 |
3.82e-65 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 228.83 E-value: 3.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 509 LLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLkeetevkDVPGAG------P 582
Cdd:PRK10790 263 ILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM-------DGPRQQygnddrP 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 583 LRfhKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL 662
Cdd:PRK10790 336 LQ--SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVVPQDTVLFNDTIANNIRYGRvTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTIL 742
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMW 822
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
....*...
gi 18034785 823 QLQQQGQE 830
Cdd:PRK10790 573 QLQLAGEE 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
326-821 |
6.42e-62 |
|
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: 222.31 E-value: 6.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 326 VSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEvlrIVDRGTSsVTGLLSYLVFNIIPTLAD--IIIGII 403
Cdd:TIGR01193 212 LSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGE---IVSRFTD-ASSIIDALASTILSLFLDmwILVIVG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 404 YFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMnTQENATRARAV-DSLLNFETVKYYNAEG-------YELER 475
Cdd:TIGR01193 288 LFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDA-MQANAVLNSSIiEDLNGIETIKSLTSEAeryskidSEFGD 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 476 YREAILKFQGLEWKSTASLVLLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:TIGR01193 367 YLNKSFKYQKADQGQQAIKAVTKLILNVVI---LWTG----AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 556 TNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRL 635
Cdd:TIGR01193 440 AARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 636 LFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYG-RVTAGDSEIQAAAQAAGIHDAILSFPE 714
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 715 GYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVcTNRTTIVVAHRLSTVVNADQI 794
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKI 678
|
490 500
....*....|....*....|....*..
gi 18034785 795 LVIKDGCIIERGRHEALLSRGGVYAEM 821
Cdd:TIGR01193 679 IVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
587-814 |
1.74e-59 |
|
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: 212.30 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 587 KGRVEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSH 665
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 IGVVPQDTVLFNDTIANNI-RYGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIaRFGDAD--PEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCT-NRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSR 814
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
578-823 |
1.57e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 201.21 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 578 PGAGPLRFHKGRVEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 656
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 657 VTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIhDAILSFPEGYETQVGERGLKLSGGEKQRVA 736
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGG 816
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
....*..
gi 18034785 817 VYAEMWQ 823
Cdd:PRK11160 566 RYYQLKQ 572
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
588-807 |
1.63e-54 |
|
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: 187.23 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYA-DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03369 5 GEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFNDTIANNI-RYGRVTagDSEIQaaaqaagihdAILSFPEGyetqvgerGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDEYS--DEEIY----------GALRVSEG--------GLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 746 DIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGR 807
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
348-785 |
1.06e-51 |
|
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: 189.49 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 348 RLFSHLHELSLRWHLGRRTGEVLRIVdrgTSSVTGLLSYLVFNIIPTLADIIIGIIY--FSMFFNAWFGLIVFLCMSLYL 425
Cdd:TIGR02868 91 RVYERLARQALAGRRRLRRGDLLGRL---GADVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILAAGLLLAG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 426 ILTIMVTEWRAKFRRDMNTQENATRARAVDSLL-NFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMV 504
Cdd:TIGR02868 168 FVAPLVSLRAARAAEQALARLRGELAAQLTDALdGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 505 IGFGLLAGSLLCAYFVSERRLQ---VGDFVLFGTYITQLYMPL-NWFGTYYRMIQTnfidMENMFDLLKEETEVKDV--P 578
Cdd:TIGR02868 248 AGLAVLGALWAGGPAVADGRLApvtLAVLVLLPLAAFEAFAALpAAAQQLTRVRAA----AERIVEVLDAAGPVAEGsaP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 579 GAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT 658
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 659 QISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIA 738
Cdd:TIGR02868 404 QDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALA 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRL 785
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
525-830 |
1.90e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 186.97 E-value: 1.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 525 LQVGDFVLFgtYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLkeETEVKDVPGAGPLRFHKGRVEFENVH---FSYaD 601
Cdd:PRK11174 287 LFAGFFVLI--LAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFL--ETPLAHPQQGEKELASNDPVTIEAEDleiLSP-D 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRF--YdisSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDT 679
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 680 IANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDT 759
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 760 SNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMwqLQQQGQE 830
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL--LAHRQEE 587
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
591-802 |
6.65e-50 |
|
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: 173.17 E-value: 6.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03246 2 EVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFNDTIANNIrygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18034785 750 LDEATSALDTSNERAIQASLAKV-CTNRTTIVVAHRLSTVVNADQILVIKDGCI 802
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
591-802 |
1.37e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:COG4619 2 ELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLFNDTIANNI----RYGRVTAGDSEIQAAAQAAGIHDAILsfpegyETQVGErglkLSGGEKQRVAIARTILKAPD 746
Cdd:COG4619 81 QEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAH------RLstvvnADQILVIKDGCI 802
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
590-814 |
3.55e-45 |
|
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: 162.12 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQ--DTVLFNDTIANNIRYGRVTAG--DSEIQAAaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIAR 739
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGPENLGlpREEIRER-----VEEAL--------ELVGLEHLAdrppheLSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVV-NADQILVIKDGCIIERGRHEALLSR 814
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
590-806 |
6.64e-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: 159.40 E-value: 6.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRSHIGV 668
Cdd:cd03247 1 LSINNVSFSYPEQEQQvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFNDTIANNIrygrvtagdseiqaaaqaagihdailsfpegyetqvgerGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERG 806
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
591-800 |
1.92e-44 |
|
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: 159.17 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIARTI 741
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLGLPEEEIEER---VEEAL--------ELVGLEGLRdrspftLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 742 LKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVN-ADQILVIKDG 800
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
389-799 |
1.25e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 171.75 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 389 FNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEwRAKFRRDMNT-QENATRARAVDSLLNFETVKYYN 467
Cdd:PTZ00265 175 FITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNK-KVKINKKTSLlYNNNTMSIIEEALVGIRTVVSYC 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 468 AEGYELER-------YREAILKFQGLEwksTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQvGDF-------VLF 533
Cdd:PTZ00265 254 GEKTILKKfnlseklYSKYILKANFME---SLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPN-NDFhggsvisILL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 534 GTYITQ--LYMPLNWFGTYYRMIQ-TNfidmeNMFDLLKEETEVKDVPGAGPLRFHKgRVEFENVHFSYaDGR---ETLQ 607
Cdd:PTZ00265 330 GVLISMfmLTIILPNITEYMKSLEaTN-----SLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHY-DTRkdvEIYK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 608 DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRY 686
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKY 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 687 GRV---------------------------------------------------------TAGDSEIQAAAQAAGIHDAI 709
Cdd:PTZ00265 483 SLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFV 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 710 LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASL--AKVCTNRTTIVVAHRLST 787
Cdd:PTZ00265 563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLST 642
|
490
....*....|..
gi 18034785 788 VVNADQILVIKD 799
Cdd:PTZ00265 643 IRYANTIFVLSN 654
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
590-804 |
2.70e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 156.37 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT--QIS-LRSHI 666
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrrEIPyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFND-TIANNIRYG-RVT-AGDSEIQAAAQAA----GIHDAILSFPEgyetqvgerglKLSGGEKQRVAIAR 739
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPlRVTgKSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVNADQ-ILVIKDGCIIE 804
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
590-806 |
8.49e-43 |
|
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: 155.42 E-value: 8.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDI-----SSGCIRIDGQDI--SQVTQISL 662
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVVPQDTVLFNDTIANNIRYG-------RVTAGDSEIQAAAQAAGIHDailsfpegyetQVGER--GLKLSGGEKQ 733
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD-----------EVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAH------RLstvvnADQILVIKDGCIIERG 806
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
591-800 |
1.58e-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: 152.01 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QdtvlfndtiannirygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDIILL 750
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 751 DEATSALDTSNERAIQASLAKVC-TNRTTIVVAHRLSTVVNA-DQILVIKDG 800
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
589-813 |
3.66e-42 |
|
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: 154.43 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVL-FNDTIANNIRYGR---------VTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEK 732
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREA--------VEEAL--------ERTGLEHLAdrpvdeLSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 733 QRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHE 809
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPE 223
|
....
gi 18034785 810 ALLS 813
Cdd:COG1120 224 EVLT 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
590-814 |
6.47e-42 |
|
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: 160.84 E-value: 6.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET----LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---L 662
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVVPQDTVL-FNDtiannirygRVTAGDSeiqaaaqaagIHDAILSFPEGYETQVGER--------GLK------- 726
Cdd:COG1123 341 RRRVQMVFQDPYSsLNP---------RMTVGDI----------IAEPLRLHGLLSRAERRERvaellervGLPpdladry 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 727 ---LSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:COG1123 402 pheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 18034785 801 CIIERGRHEALLSR 814
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
590-814 |
2.14e-41 |
|
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: 151.88 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSY---ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQD---------TVlfNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILS-FPEgyetqvgerglKLSGGEKQRVA 736
Cdd:COG1124 82 QMVFQDpyaslhprhTV--DRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDrYPH-----------QLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQASLA--KVCTNRTTIVVAHRLStVVN--ADQILVIKDGCIIERGRHEALL 812
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLL 227
|
..
gi 18034785 813 SR 814
Cdd:COG1124 228 AG 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
455-826 |
3.83e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 163.66 E-value: 3.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 455 DSLLNFETVKYYNAEGYELERYREAI-LKFQGLEWKSTASLVL--LNQTQNMVI-GFGLLAGSLLcayfVSERRLQVGDF 530
Cdd:PTZ00265 1027 EAFYNMNTVIIYGLEDYFCNLIEKAIdYSNKGQKRKTLVNSMLwgFSQSAQLFInSFAYWFGSFL----IRRGTILVDDF 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 531 V--LF-----GTYITQLyMPLNWFGTYYRMiqtnfiDMENMFDLLKEETEVkDVPGAGPLRFH-----KGRVEFENVHFS 598
Cdd:PTZ00265 1103 MksLFtflftGSYAGKL-MSLKGDSENAKL------SFEKYYPLIIRKSNI-DVRDNGGIRIKnkndiKGKIEIMDVNFR 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 599 YADGRET--LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDI---------------------------------- 642
Cdd:PTZ00265 1175 YISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 643 --------------------SSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQA 702
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKF 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 703 AGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLA--KVCTNRTTIV 780
Cdd:PTZ00265 1335 AAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIIT 1414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 781 VAHRLSTVVNADQILVI----KDGCIIE-RGRHEALLS-RGGVYAEMWQLQQ 826
Cdd:PTZ00265 1415 IAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSvQDGVYKKYVKLAK 1466
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
606-755 |
6.58e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.02 E-value: 6.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFND-TIANNI 684
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 685 RYGRVTAGDSEIQAAAQaagIHDAI--LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATS 755
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR---AEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
590-806 |
6.70e-41 |
|
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: 149.96 E-value: 6.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---R 663
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVVPQD---------TVLfnDTIANNIRYGRVTAGDSEIQAAAQAA----GIHDAIL-SFPegYEtqvgerglkLSG 729
Cdd:cd03257 82 KEIQMVFQDpmsslnprmTIG--EQIAEPLRIHGKLSKKEARKEAVLLLlvgvGLPEEVLnRYP--HE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 730 GEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
590-807 |
1.34e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.04 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---- 662
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVVPQD-------TVLFNdtIANNIRYGRVTAGDSE--IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQ 733
Cdd:COG1136 85 RRHIGFVFQFfnllpelTALEN--VALPLLLAGVSRKERRerARELLERVGLGDRLDHRPS-----------QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVNADQILVIKDGCIIERGR 807
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNreLGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
591-816 |
1.34e-40 |
|
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: 149.62 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRSHIGVVP 670
Cdd:COG4555 3 EVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLF-NDTIANNIRYgrvTAGDSEIQAAAQAAGIHDAI--LSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:COG4555 81 DERGLYdRLTVRENIRY---FAELYGLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVN-ADQILVIKDGCIIERGRHEALLSRGG 816
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
514-821 |
1.79e-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: 161.65 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 514 LLCAYF--VSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVK-DVPGAGPLRF--HKG 588
Cdd:TIGR00957 1204 LFAALFavISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGwpPRG 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLDpFSQYS--DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEM 821
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
590-814 |
1.51e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.36 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHIGVV 669
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFND-TIANNIRYgrvTAGDSEIQAAAQAAGIHDAI--LSFPEGYETQVGerglKLSGGEKQRVAIARTILKAPD 746
Cdd:COG1131 79 PQEPALYPDlTVRENLRF---FARLYGLPRKEARERIDELLelFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVN-ADQILVIKDGCIIERGRHEALLSR 814
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
590-800 |
4.67e-39 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 143.76 E-value: 4.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRE----TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGciridgqdisqvtQISLRSH 665
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------------SVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 IGVVPQDTVLFNDTIANNI---------RYGRVtagdseiqaaaqaagIHDAILS-----FPEGYETQVGERGLKLSGGE 731
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgkpfdeeRYEKV---------------IKACALEpdleiLPDGDLTEIGEKGINLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 732 KQRVAIARTILKAPDIILLDEATSALD--TSN---ERAIQASLAKvctNRTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDahVGRhifENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
590-800 |
7.73e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 143.78 E-value: 7.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---- 662
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVVPQDTVLFND-TIANNIRYGRVTAGDSEIQAAAQAA------GIHDAILSFPEgyetqvgerglKLSGGEKQRV 735
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEellervGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
590-812 |
8.12e-39 |
|
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: 144.35 E-value: 8.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT---QISLRSHI 666
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFND-TIANNI-----RYGRVTagDSEIQAAAQAA----GIHDAILSFPegyetqvGErglkLSGGEKQRVA 736
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLS--EAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 737 IARTILKAPDIILLDEATSALD--TSNE-----RAIQASLakvctNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRH 808
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpiTSAVideliRELRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....
gi 18034785 809 EALL 812
Cdd:COG1127 227 EELL 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
590-806 |
9.31e-39 |
|
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: 143.43 E-value: 9.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIslRSHIGVV 669
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNIRYGRVTAGDSE------IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTIL 742
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLRGVPKaeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
590-800 |
7.87e-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: 139.24 E-value: 7.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS--LRSHIG 667
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLF-NDTIANNIRYGrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPD 746
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTN--RTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
591-806 |
8.10e-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: 139.49 E-value: 8.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QdtVLfndtiannirygrvtagdseiqaaaQAAGIHDaiLSfpegyetqvgERGL-KLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03214 80 Q--AL-------------------------ELLGLAH--LA----------DRPFnELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 750 LDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
590-803 |
8.27e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 141.73 E-value: 8.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHI 666
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQD-------TVLfndtiaNNI---RYGRVtagdseiqaaaqaaGIHDAILSF--PEGYET------QVG------E 722
Cdd:COG3638 83 GMIFQQfnlvprlSVL------TNVlagRLGRT--------------STWRSLLGLfpPEDRERalealeRVGladkayQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 723 RGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKD 799
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRD 222
|
....
gi 18034785 800 GCII 803
Cdd:COG3638 223 GRVV 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
590-814 |
3.72e-37 |
|
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: 139.25 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---R 663
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVVPQDTVLFND-TIANNIRYGRVTAG------DSEIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVA 736
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGvpkaeiEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQASLAKVctNR----TTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEAL 811
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 18034785 812 LSR 814
Cdd:cd03258 229 FAN 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
590-802 |
3.83e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 3.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHIGVV 669
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQD---------TVLfnDTIANNiRYG------RVTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LS 728
Cdd:COG1121 81 PQRaevdwdfpiTVR--DVVLMG-RYGrrglfrRPSRADREA--------VDEAL--------ERVGLEDLAdrpigeLS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 729 GGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC-TNRTTIVVAHRLSTVV-NADQILVIKDGCI 802
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
590-797 |
1.82e-36 |
|
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: 136.83 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHI 666
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFN-DTIANNIRYGRVTAG--DSEIQAAaqaagIHDAILSFpegyetqvgerGLK---------LSGGEKQR 734
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGvpKAEARER-----AEELLELV-----------GLSgfenayphqLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 735 VAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVI 797
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTHDIDEAVFlADRVVVL 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
590-806 |
2.27e-36 |
|
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: 137.25 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRSHI 666
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFND-TIANNIRYG---RVTAGDSEIQAAAQAA----GIHDAILSFPegyetqvGErglkLSGGEKQRVAIA 738
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEKleavGLRGAEDLYP-------AE----LSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQA---SLAKVcTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDlirSLKKE-LGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
563-816 |
3.13e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 148.20 E-value: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 563 NMFDLLKEETEV--KDVPGAG-PLRfhkGRVEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFR 638
Cdd:PLN03232 1208 NYIDLPSEATAIieNNRPVSGwPSR---GSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 639 FYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRyGRVTAGDSEIQAAAQAAGIHDAILSFPEGYET 718
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDA 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 719 QVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIK 798
Cdd:PLN03232 1364 EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
250
....*....|....*...
gi 18034785 799 DGCIIERGRHEALLSRGG 816
Cdd:PLN03232 1444 SGQVLEYDSPQELLSRDT 1461
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
590-814 |
3.14e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.05 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQISLRSHIG 667
Cdd:COG1126 2 IEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFND-TIANNIRYG---------------------RVtagdseiqaaaqaaGIHDAILSFPEgyetqvgergl 725
Cdd:COG1126 81 MVFQQFNLFPHlTVLENVTLApikvkkmskaeaeeramelleRV--------------GLADKADAYPA----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 726 KLSGGEKQRVAIARTILKAPDIILLDEATSALD--TSNE--RAIQaSLAKvcTNRTTIVVAHRLS---TVvnADQILVIK 798
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpeLVGEvlDVMR-DLAK--EGMTMVVVTHEMGfarEV--ADRVVFMD 210
|
250
....*....|....*.
gi 18034785 799 DGCIIERGRHEALLSR 814
Cdd:COG1126 211 GGRIVEEGPPEEFFEN 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
590-814 |
5.59e-36 |
|
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: 143.12 E-value: 5.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGR-ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS---SGCIRIDGQDISQVTQISLRSH 665
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 IGVVPQD--TVLFNDTIANNIRYGRVTAGDS------EIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAI 737
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALENLGLSraearaRVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 738 ARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSR 814
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
591-811 |
6.02e-36 |
|
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: 136.16 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHIG 667
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFND-TIANNIRYGRVtagdseiqaaaqaaGIHDAILSFPEGYE-----------TQVG------ERGLKLSG 729
Cdd:cd03256 82 MIFQQFNLIERlSVLENVLSGRL--------------GRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 730 GEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVV-NADQILVIKDGCIIERG 806
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDG 227
|
....*
gi 18034785 807 RHEAL 811
Cdd:cd03256 228 PPAEL 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
590-802 |
8.90e-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: 133.29 E-value: 8.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHIGVV 669
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFNDtiannirygrvtagdseiqaaaqaagihdaiLSfpeGYETqvgergLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03230 79 PEEPSLYEN-------------------------------LT---VREN------LKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 750 LDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVN-ADQILVIKDGCI 802
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
590-807 |
2.80e-35 |
|
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: 133.30 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV--TQIS-LRSHI 666
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgRAIPyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFND-TIANNIRYGRVTAGDS------EIQAAAQAAGIHDAILSFPEGyetqvgerglkLSGGEKQRVAIAR 739
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEVTGVPpreirkRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVikdgCIIERGR 807
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRV----IALERGK 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
590-814 |
5.19e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.77 E-value: 5.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRsHIGVV 669
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKR-NVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNIRYG----RVTAgdSEIQAAaqaagIHDAIlsfpegyeTQVGERGL------KLSGGEKQRVAIA 738
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGlrmrGVPK--AEIRAR-----VAELL--------ELVGLEGLadryphQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 739 RTILKAPDIILLDEATSALD------TSNE-RAIQASLakvctNRTTIVVAHRLS---TVvnADQILVIKDGCIIERGRH 808
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDaklreeMREElRRLQREL-----GITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTP 220
|
....*.
gi 18034785 809 EALLSR 814
Cdd:COG3842 221 EEIYER 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
572-821 |
6.23e-35 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 144.15 E-value: 6.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 572 TEVKDVPGAGPLRFHKGRVEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRID 650
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVN 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 651 GQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRyGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGG 730
Cdd:PTZ00243 1371 GREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVG 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 731 EKQRVAIARTILK-APDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGR-H 808
Cdd:PTZ00243 1450 QRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSpR 1529
|
250
....*....|...
gi 18034785 809 EALLSRGGVYAEM 821
Cdd:PTZ00243 1530 ELVMNRQSIFHSM 1542
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
590-814 |
1.24e-34 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 132.42 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNI-------RYGRVTAgDSEIQAAAQAAGIHDAilSFPEGYETQvgerglkLSGGEKQRVAIARTI 741
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkllKWPKEKI-RERADELLALVGLDPA--EFADRYPHE-------LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 742 LKAPDIILLDEATSALDTSNERAIQASLAKV--CTNRTTIVVAHRL-STVVNADQILVIKDGCIIERGRHEALLSR 814
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
588-819 |
1.83e-34 |
|
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: 132.34 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFNDTIANNIRYGRvTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSR-GGVYA 819
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFA 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
591-798 |
4.02e-34 |
|
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: 129.96 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHIGVVP 670
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 Q----DT---VLFNDTIANNiRYG------RVTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGE 731
Cdd:cd03235 75 QrrsiDRdfpISVRDVVLMG-LYGhkglfrRLSKADKAK--------VDEAL--------ERVGLSELAdrqigeLSGGQ 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 732 KQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC-TNRTTIVVAHRLSTVVN-ADQILVIK 798
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
589-813 |
4.48e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 131.37 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvtqisLRSH 665
Cdd:COG1116 7 ALELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 IGVVPQDTVLFN-DTIANNIRYGRVTAGDSeiqaaaqaagihdailsfpegyETQVGER--------GLK---------L 727
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVP----------------------KAERRERarellelvGLAgfedayphqL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 728 SGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAH------RLstvvnADQILVIKD 799
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHdvdeavFL-----ADRVVVLSA 214
|
250 260
....*....|....*....|...
gi 18034785 800 --GCIIE-------RGRHEALLS 813
Cdd:COG1116 215 rpGRIVEeidvdlpRPRDRELRT 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
590-802 |
1.11e-33 |
|
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: 128.80 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ--ISLRSHIG 667
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLF-NDTIANNIRYGRVTA-GDSEIQAAAQAA------GIHDAILSFPegyetqvgergLKLSGGEKQRVAIAR 739
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVkGMSKAEAEERALellekvGLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 740 TILKAPDIILLDEATSALD--TSNE-RAIQASLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCI 802
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDpeLVGEvLDVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
588-823 |
4.21e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 138.33 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:PLN03130 1236 GSIKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFNDTIANNIR-YGRvtAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDpFNE--HNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 746 DIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSR-GGVYAEMWQ 823
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNeGSAFSKMVQ 1472
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
590-807 |
6.44e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.57 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQ--DTVLFNDTIANNIRYG----RVTAGDseiqaaaqaagIHDAILSfpegYETQVG-ERGLK-----LSGGEKQRVA 736
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkKVPPKK-----------MKDIIDD----LAKKVGmEDYLDkepqnLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQA---SLAKVcTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGR 807
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKimvDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
590-807 |
1.40e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.43 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILR---LLFRFydiSSGCIRIDGQDISQVTQISL- 662
Cdd:COG1135 2 IELENLSKTFPTKGGPvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLERP---TSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 --RSHIGVVPQDtvlFN----DTIANNIRYGRVTAG--DSEIqaaaqaagihdailsfpegyETQVGER----GLK---- 726
Cdd:COG1135 79 aaRRKIGMIFQH---FNllssRTVAENVALPLEIAGvpKAEI--------------------RKRVAELlelvGLSdkad 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 727 -----LSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVctNRT---TIVVA-HRLStVVN--ADQIL 795
Cdd:COG1135 136 aypsqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRElglTIVLItHEMD-VVRriCDRVA 212
|
250
....*....|..
gi 18034785 796 VIKDGCIIERGR 807
Cdd:COG1135 213 VLENGRIVEQGP 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
580-806 |
1.98e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.69 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 580 AGPLRFHKGRVEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDI 654
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 655 --SQVTQISLRSHIGVVPQDTVLFNDTIANNIRYG-RVtagdseiqaaaqaAGIH-----DAILsfpEGYETQVG----- 721
Cdd:COG1117 81 ydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlRL-------------HGIKskselDEIV---EESLRKAAlwdev 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 722 -----ERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAH------RLStvvn 790
Cdd:COG1117 145 kdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS---- 220
|
250
....*....|....*.
gi 18034785 791 aDQILVIKDGCIIERG 806
Cdd:COG1117 221 -DYTAFFYLGELVEFG 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
593-803 |
4.38e-32 |
|
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: 123.91 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqisLRSHIGVVPQD 672
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 T--VLFNDTIANNIRYG--RVTAGDSEIQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03226 80 VdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HR---LSTVvnADQILVIKDGCII 803
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVItHDyefLAKV--CDRVLLLANGAIV 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
590-821 |
7.63e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.51 E-value: 7.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK13635 6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAIlsfpegyeTQVG------ERGLKLSGGEKQRVAIART 740
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGLENIG---VPREEMVERVDQAL--------RQVGmedflnREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASL--AKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVY 818
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHML 234
|
...
gi 18034785 819 AEM 821
Cdd:PRK13635 235 QEI 237
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
590-833 |
7.84e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 125.23 E-value: 7.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQ--DTVLFNDTIANNIRYGRVTAGDSEiqaaaqaagihDAILSFPEGYETQVGERGLK------LSGGEKQRVAIARTI 741
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGPVNMGLDK-----------DEVERRVEEALKAVRMWDFRdkppyhLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 742 LKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVN-ADQILVIKDGCIIERGRHEALLS------ 813
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDediveq 233
|
250 260
....*....|....*....|....
gi 18034785 814 ---RGGVYAEMW-QLQQQGQETVP 833
Cdd:PRK13647 234 aglRLPLVAQIFeDLPELGQSKLP 257
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
265-562 |
1.25e-31 |
|
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: 125.36 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRA-------LLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 345 VELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLY 424
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVL-TLIGALVILFYLNWKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 425 LILTIMVTEW-RAKFRRDMNTQENATrARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNM 503
Cdd:cd07346 153 VLILRYFRRRiRKASREVRESLAELS-AFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 504 VIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDME 562
Cdd:cd07346 232 LTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
606-814 |
3.07e-31 |
|
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: 122.44 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIslRSHIGVVPQDTVLF-NDTIANNI 684
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 685 RYG-------RVTAgDSEIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKAPDIILLDEATSAL 757
Cdd:cd03299 93 AYGlkkrkvdKKEI-ERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 758 DTSNERAIQASLAKV--CTNRTTIVVAHRLSTV-VNADQILVIKDGCIIERGRHEALLSR 814
Cdd:cd03299 161 DVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
277-544 |
6.96e-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: 122.75 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 277 ALNVLVPIFYRDIVNLLTSKA--PWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRGVELRLFSHLH 354
Cdd:pfam00664 13 AISPAFPLVLGRILDVLLPDGdpETQALNVYSLALLLLGLAQF-------ILSFLQSYLLNHTGERLSRRLRRKLFKKIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 355 ELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIyFSMFFNAWFGLIVFLCMSLYLILTIMVTEW 434
Cdd:pfam00664 86 RQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGII-VMFYYGWKLTLVLLAVLPLYILVSAVFAKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 435 RAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSL 514
Cdd:pfam00664 165 LRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALW 244
|
250 260 270
....*....|....*....|....*....|
gi 18034785 515 LCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:pfam00664 245 FGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
590-815 |
9.40e-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: 122.15 E-value: 9.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQIslRSH 665
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEI--RKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 IGVVPQD--------TVlfNDTIA---NNIRYGRvtagdSEIQAAaqaagIHDAIlsfpegyeTQVGERGLK------LS 728
Cdd:TIGR04520 79 VGMVFQNpdnqfvgaTV--EDDVAfglENLGVPR-----EEMRKR-----VDEAL--------KLVGMEDFRdrephlLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 729 GGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVNADQILVIKDGCIIERG 806
Cdd:TIGR04520 139 GGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
....*....
gi 18034785 807 RHEALLSRG 815
Cdd:TIGR04520 219 TPREIFSQV 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
589-806 |
1.82e-30 |
|
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: 118.81 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENV-----HFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL--FRFYDISSGCIRIDGQDISqvtQIS 661
Cdd:cd03213 3 TLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQDTVLF-NDTIANNIRYGrvtagdseiqaaaqaagihdAILsfpegyetqvgeRGlkLSGGEKQRVAIART 740
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMFA--------------------AKL------------RG--LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASLAKVC-TNRTTIVVAHRLSTVV--NADQILVIKDGCIIERG 806
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
606-812 |
2.96e-30 |
|
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: 120.44 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRSH-IGVVPQDTVLF-NDTI 680
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelRELRRKkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAG-DSEIQAAAQAAGIHDAILsfpEGYETQ-VGErglkLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:cd03294 120 LENVAFGLEVQGvPRAEREERAAEALELVGL---EGWEHKyPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 759 TSNERAIQASLAKVCTN--RTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALL 812
Cdd:cd03294 193 PLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
591-814 |
3.52e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYadGRETLQdVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRShIGVVP 670
Cdd:COG3840 3 RLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLFND-TIANNIRYG-----RVTAGDSEiqaaaqaaGIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIA 738
Cdd:COG3840 78 QENNLFPHlTVAQNIGLGlrpglKLTAEQRA--------QVEQAL--------ERVGLAGLLdrlpgqLSGGQRQRVALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSR 814
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCreRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
591-807 |
7.81e-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: 117.92 E-value: 7.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----- 665
Cdd:cd03224 2 EVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-----GLPPHerara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 -IGVVPQDTVLFND-TIANNIRYGRVTAGDSEIQAAAqaagihDAILS-FPEGYETQvGERGLKLSGGEKQRVAIARTIL 742
Cdd:cd03224 76 gIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARL------ERVYElFPRLKERR-KQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRlstvvNADQILVIKD-GCIIERGR 807
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQ-----NARFALEIADrAYVLERGR 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
588-802 |
1.50e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.95 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRsHIG 667
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL-PPKDR-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLF-NDTIANNIRYG----RVTAgdSEIqaaaqaagihdailsfpegyETQVGE-------------RGLKLSG 729
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrKVPK--AEI--------------------DRRVREaaellgledlldrKPKQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 730 GEKQRVAIARTILKAPDIILLDEATSALD------TSNE-RAIQASLakvctNRTTIVVAH------RLstvvnADQILV 796
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAV 206
|
....*.
gi 18034785 797 IKDGCI 802
Cdd:COG3839 207 MNDGRI 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
590-806 |
1.57e-29 |
|
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: 116.52 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTvALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQiSLRSHIGVV 669
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQD-------TVL-FNDTIA--NNIRYGRVtagDSEIQAAAQAAGIHDAilsfpegYETQVGerglKLSGGEKQRVAIAR 739
Cdd:cd03264 78 PQEfgvypnfTVReFLDYIAwlKGIPSKEV---KARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTV-VNADQILVIKDGCIIERG 806
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
593-813 |
2.22e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.57 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:PRK13548 6 RNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TVL-FNDTIANNIRYGRVTAGDSEiqaaaqaagIHDAILsfPEGYETQVGERGLK------LSGGEKQRVAIAR--TILK 743
Cdd:PRK13548 85 SSLsFPFTVEEVVAMGRAPHGLSR---------AEDDAL--VAAALAQVDLAHLAgrdypqLSGGEQQRVQLARvlAQLW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 744 APD----IILLDEATSALDTSNERAIqASLAKVCTNR---TTIVVAHRLstvvN-----ADQILVIKDGCIIERGRHEAL 811
Cdd:PRK13548 154 EPDgpprWLLLDEPTSALDLAHQHHV-LRLARQLAHErglAVIVVLHDL----NlaaryADRIVLLHQGRLVADGTPAEV 228
|
..
gi 18034785 812 LS 813
Cdd:PRK13548 229 LT 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
588-805 |
5.74e-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: 5.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYA-DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQISLRSHI 666
Cdd:TIGR01271 1216 GQMDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDpYEQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 746 DIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIkDGCIIER 805
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVI-EGSSVKQ 1431
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
590-807 |
6.99e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 118.75 E-value: 6.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGR---ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS-- 664
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 665 -HIGVVPQDtvlFN----DTIANNIRYGRVTAGDS--EIQAAAQ----AAGIHDAILSFPEgyetqvgerglKLSGGEKQ 733
Cdd:PRK11153 82 rQIGMIFQH---FNllssRTVFDNVALPLELAGTPkaEIKARVTelleLVGLSDKADRYPA-----------QLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVctNRT---TIV-VAHRLSTVVN-ADQILVIKDGCIIERGR 807
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRElglTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
590-814 |
1.24e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 117.94 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvTQISLR-SHIGV 668
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPPReRRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLF-NDTIANNIRYG-RV-TAGDSEIqaaaqaagihdailsfpegyETQVGE-------RGLK------LSGGEK 732
Cdd:COG1118 80 VFQHYALFpHMTVAENIAFGlRVrPPSKAEI--------------------RARVEEllelvqlEGLAdrypsqLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 733 QRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKV--CTNRTTIVVAH------RLstvvnADQILVIKDGCIIE 804
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
250
....*....|
gi 18034785 805 RGRHEALLSR 814
Cdd:COG1118 215 VGTPDEVYDR 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
590-814 |
2.32e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 116.31 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQ---DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYD---ISSGCIRIDGQDISQVTQISLR 663
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 ----SHIGVVPQD---------TVLfnDTIANNIRygrvtagdseiqaaaqaagIHDaILSFPEGYE------TQVG--- 721
Cdd:COG0444 82 kirgREIQMIFQDpmtslnpvmTVG--DQIAEPLR-------------------IHG-GLSKAEAREraiellERVGlpd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 722 -ERGLK-----LSGGEKQRVAIARTILKAPDIILLDEATSALDTSneraIQAS----LAKVCTNR-TTIV-VAHRLSTVV 789
Cdd:COG0444 140 pERRLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVT----IQAQilnlLKDLQRELgLAILfITHDLGVVA 215
|
250 260
....*....|....*....|....*.
gi 18034785 790 N-ADQILVIKDGCIIERGRHEALLSR 814
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
593-813 |
3.65e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.06 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:COG4559 5 ENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TVL-FNDTIANNIRYGR-----VTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIART 740
Cdd:COG4559 84 SSLaFPFTVEEVVALGRaphgsSAAQDRQI--------VREAL--------ALVGLAHLAgrsyqtLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 741 I--LKAPD-----IILLDEATSALDTSNERAIqASLAKVCTNRTTIVVA--HRLstvvN-----ADQILVIKDGCIIERG 806
Cdd:COG4559 148 LaqLWEPVdggprWLFLDEPTSALDLAHQHAV-LRLARQLARRGGGVVAvlHDL----NlaaqyADRILLLHQGRLVAQG 222
|
....*..
gi 18034785 807 RHEALLS 813
Cdd:COG4559 223 TPEEVLT 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
588-813 |
6.90e-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: 113.80 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYAD-GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISsGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03289 1 GQMTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 746 DIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLS 813
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
608-806 |
2.16e-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: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 608 DVSFTVmPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdISQVTQISL-----RSHIGVVPQDTVLF-NDTIA 681
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGLVFQQYALFpHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 NNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpegyeTQVGERG-LKLSGGEKQRVAIARTILKAPDIILLDEATSALDTS 760
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGL--------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18034785 761 NERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03297 166 LRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
599-806 |
2.85e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.41 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 599 YADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQISLRSHIGVVPQ 671
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 DTVLFNDTIANNIRYGRVTAG--DSEIQAAAQAAGIHDAilSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGikDKQVLDEAVEKSLKGA--SIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 750 LDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
606-813 |
3.00e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHIGVVPQDTvlfndtian 682
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 683 nirYG----RVTAGDseiqaaaqaagihdaILSFP-----EGYETQVGER--------GLK----------LSGGEKQRV 735
Cdd:COG4608 105 ---YAslnpRMTVGD---------------IIAEPlrihgLASKAERRERvaellelvGLRpehadrypheFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSneraIQA-------------SLakvctnrTTIVVAHRLStVVN--ADQILVIKDG 800
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVS----IQAqvlnlledlqdelGL-------TYLFISHDLS-VVRhiSDRVAVMYLG 234
|
250 260
....*....|....*....|....*
gi 18034785 801 CIIERG---------RH---EALLS 813
Cdd:COG4608 235 KIVEIAprdelyarpLHpytQALLS 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
606-814 |
3.18e-27 |
|
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: 117.09 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQ---ISLRSHIGVVPQDTvlfnd 678
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRralRPLRRRMQVVFQDP----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 679 tiannirYG----RVTAGD--SEiqaaaqaaG--IHDAILSfPEGYETQVG----ERGLK----------LSGGEKQRVA 736
Cdd:COG4172 372 -------FGslspRMTVGQiiAE--------GlrVHGPGLS-AAERRARVAealeEVGLDpaarhrypheFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 737 IART-ILKaPDIILLDEATSALDtsneRAIQAS----LAKVCTNR--TTIVVAHRLStVVNA--DQILVIKDGCIIERGR 807
Cdd:COG4172 436 IARAlILE-PKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGP 509
|
....*..
gi 18034785 808 HEALLSR 814
Cdd:COG4172 510 TEQVFDA 516
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
590-812 |
3.85e-27 |
|
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: 110.94 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGC-IRIDGQDISQVTQISLRSHIGV 668
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 V---------PQDTVL------FNDTIAnniRYGRVTAGDSEIQaaaqaagihDAILsfpegyeTQVGERGLK------L 727
Cdd:COG1119 83 VspalqlrfpRDETVLdvvlsgFFDSIG---LYREPTDEQRERA---------RELL-------ELLGLAHLAdrpfgtL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 728 SGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVNA-DQILVIKDGCIIE 804
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaeGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
....*...
gi 18034785 805 RGRHEALL 812
Cdd:COG1119 224 AGPKEEVL 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
591-807 |
4.29e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 110.46 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----- 665
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-----GLPPHriarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 -IGVVPQDTVLFND-TIANNIRYGRVTAGDSEiqaaaQAAGIHDAILS-FPEgyetqVGER----GLKLSGGEKQRVAIA 738
Cdd:COG0410 79 gIGYVPEGRRIFPSlTVEENLLLGAYARRDRA-----EVRADLERVYElFPR-----LKERrrqrAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVvahrlstVV--NADQILVIKD-GCIIERGR 807
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTIL-------LVeqNARFALEIADrAYVLERGR 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
590-816 |
5.56e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.36 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRE--TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAiLSFpegyetqVGERGLK------LSGGEKQRVAIAR 739
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENKG---IPHEEMKERVNEA-LEL-------VGMQDFKereparLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGG 816
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
590-803 |
5.57e-27 |
|
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: 107.90 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI-SLRSHIGV 668
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQdtvlfndtiannirygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTTIV-VAHRLSTVVN-ADQILVIKDGCII 803
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
590-806 |
7.23e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.94 E-value: 7.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQISLRSHIG 667
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQ--DTVLFNDTIANNIRYGRVTAGDSEiqaAAQAAGIHDAILSFP-EGYETQVGERglkLSGGEKQRVAIARTILKA 744
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGPLNLGLSK---EEVEKRVKEALKAVGmEGFENKPPHH---LSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTV-VNADQILVIKDGCIIERG 806
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
590-806 |
8.38e-27 |
|
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: 108.99 E-value: 8.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQ---DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHI 666
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFND-TIANNIRY-GRV--TAGDSeiqaaaqaagIHDAI--LSFPEGYETQVGERGLKLSGGEKQRVAIART 740
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfAGLygLKGDE----------LTARLeeLADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
590-815 |
1.65e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.84 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQ--DTVLFNDTIANNIRYG-RVTAGDSEIQAAAQAAGIHDAILSFPEGYETQvgerglKLSGGEKQRVAIARTILKAP 745
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGlENHAVPYDEMHRRVSEALKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 746 DIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRG 815
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
590-807 |
2.64e-26 |
|
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: 108.09 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP--PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFND-TIANNIRYGRVTAGDSEiqaAAQAAGIHDAI-LSFPEGYEtqvGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGLRLKKLPK---AEIKERVAEALdLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLS-TVVNADQILVIKDGCIIERGR 807
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
590-811 |
3.39e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDG------QDISQVTQISLR 663
Cdd:COG4161 3 IQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVV-------PQDTVLFNdTIANNIRYGRVT--AGDSEIQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQR 734
Cdd:COG4161 82 QKVGMVfqqynlwPHLTVMEN-LIEAPCKVLGLSkeQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 735 VAIARTILKAPDIILLDEATSALD---TSNERAIQASLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEA 810
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQ--TGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDASH 227
|
.
gi 18034785 811 L 811
Cdd:COG4161 228 F 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
590-814 |
4.20e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRL---LFRFYDISSGCIRIDGQDISQVTQISLRSH 665
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 IGVVPQ--DTVLFNDTIANNIRYGRVTAGDSE------IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAI 737
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLENRAVPRpemikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 738 ARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSR 814
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
590-802 |
4.21e-26 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 106.96 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRShIGVV 669
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRD-IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNIRYG--RVTAGDSEIqaaaqAAGIHDA--ILsfpeGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlkLRKVPKDEI-----DERVREVaeLL----QIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCTN--RTTIVVAH-RLSTVVNADQILVIKDGCI 802
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
589-799 |
4.81e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.41 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQiSLRSHIGV 668
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFND-TIANNIR-----YGRVTAGDSeiqaaaqaagIHDAILSF-PEGYE-TQVGerglKLSGGEKQRVAIART 740
Cdd:COG4133 80 LGHADGLKPElTVRENLRfwaalYGLRADREA----------IDEALEAVgLAGLAdLPVR----QLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKD 799
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
590-820 |
8.64e-26 |
|
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: 114.66 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDissgciRIDGQdisqvtqISLRSHIGV 668
Cdd:TIGR00957 637 ITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILsFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 749 LLDEATSALDTSNERAIQASL---AKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAE 820
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE 857
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
590-807 |
2.10e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.94 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDtvlfndtiaNNI-------------RY----GRVTAGDSEIqaaaqaagIHDAILSFP-EGYEtqvgERGLK-LSGG 730
Cdd:COG4604 81 RQE---------NHInsrltvrelvafgRFpyskGRLTAEDREI--------IDEAIAYLDlEDLA----DRYLDeLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 731 EKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGR 807
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGT 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
608-814 |
4.77e-25 |
|
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: 107.49 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 608 DVSFTVMPGQTVALVGPSGAGKSTILRL---LFRFydiSSGCIRIDG---QDISQvtQISLRSH---IGVVPQDTVLFND 678
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGevlQDSAR--GIFLPPHrrrIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 679 -TIANNIRYG--RVTAGDSEIqaaaqaagihdailSFPE-----GYETQVGERGLKLSGGEKQRVAIARTILKAPDIILL 750
Cdd:COG4148 92 lSVRGNLLYGrkRAPRAERRI--------------SFDEvvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 751 DEATSALDTSNERAIQASLAKVCTN-RTTIV-VAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSR 814
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDElDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
602-806 |
6.23e-25 |
|
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: 103.45 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqVTQISLRSHIGVVPQDTVLF-NDTI 680
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAG--DSEIQAAAQAAGIHDAilsfpegyetqVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:cd03268 90 RENLRLLARLLGirKKRIDEVLDVVGLKDS-----------AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 759 ---TSNERAIQASLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03268 159 pdgIKELRELILSLRD--QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
590-806 |
6.53e-25 |
|
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: 103.34 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAdgrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqVTQISLRShIGVV 669
Cdd:cd03298 1 VRLDKIRFSYG---EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-AAPPADRP-VSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFND-TIANNIRYGRV-----TAGDSE-IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTIL 742
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLSpglklTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
591-763 |
1.12e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.26 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:PRK10247 9 QLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLFNDTIANNIRYG---RVTAGDSE-IQAAAQAAGIHDAILsfpegyETQVGErglkLSGGEKQRVAIARTILKAPD 746
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPwqiRNQQPDPAiFLDDLERFALPDTIL------TKNIAE----LSGGEKQRISLIRNLQFMPK 157
|
170
....*....|....*..
gi 18034785 747 IILLDEATSALDTSNER 763
Cdd:PRK10247 158 VLLLDEITSALDESNKH 174
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
602-813 |
2.17e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.91 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIR-----ID-----GQDISQVTQisLRSHIGVVPQ 671
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDtarslSQQKGLIRQ--LRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 DTVLF-NDTIANNIRYGRV----------TAGDSEIQAAAQAAGIHDAilsFPEgyetqvgerglKLSGGEKQRVAIART 740
Cdd:PRK11264 93 NFNLFpHRTVLENIIEGPVivkgepkeeaTARARELLAKVGLAGKETS---YPR-----------RLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQA---SLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNtirQLAQ--EKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
590-800 |
2.28e-24 |
|
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: 102.20 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqVTQI-SLRSHIG 667
Cdd:cd03263 1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRkAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFND-TIANNIR-YGRV-----TAGDSEIQAAAQAAGIHDAIlsfpegyETQVGErglkLSGGEKQRVAIART 740
Cdd:cd03263 79 YCPQFDALFDElTVREHLRfYARLkglpkSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDG 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
590-806 |
2.59e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.97 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS--QVTQISLR 663
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVVPQ--DTVLFNDTIANNIRYGRVTAG--DSEIQAAaqaagIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIAR 739
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGlsEEEIENR-----VKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIqasLAKVCT-----NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEI---LNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
590-802 |
2.69e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.80 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--AENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNIRYG----RVTAgdSEIQAAaqaagIHDAI----LsfpegyETQVGERGLKLSGGEKQRVAIART 740
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqKTPA--AEITPR-----VMEALrmvqL------EEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASLAKV--CTNRTTIVVAH----RLSTvvnADQILVIKDGCI 802
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALqrKLGITFVFVTHdqeeALTM---SDRIVVMRDGRI 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
610-813 |
4.07e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 610 SFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRShIGVVPQDTVLFND-TIANNIRYG- 687
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRP-VSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 688 ----RVTAGDSE-IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNE 762
Cdd:PRK10771 97 npglKLNAAQREkLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18034785 763 RAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
590-758 |
4.93e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.10 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---LRSHI 666
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFND-TIANNIRYGRVTAGDSE------IQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQRVAIAR 739
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLIIAGASGddirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170
....*....|....*....
gi 18034785 740 TILKAPDIILLDEATSALD 758
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
606-804 |
6.21e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QISLRSHIGVVPQDTVLFND-TIANN 683
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 684 IRYGRvtagdseiqaAAQAAGIHD------------AILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLD 751
Cdd:COG1129 100 IFLGR----------EPRRGGLIDwramrrrarellARLGLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 752 EATSALdTSNE--------RAIQASlakvctNRTTIVVAHRLSTVVN-ADQILVIKDGCIIE 804
Cdd:COG1129 166 EPTASL-TEREverlfriiRRLKAQ------GVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
590-813 |
6.64e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.48 E-value: 6.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET--LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAILSFPE-GYETQVGERglkLSGGEKQRVAIARTILKA 744
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQG---IPREEMIKRVDEALLAVNMlDFKTREPAR---LSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
608-815 |
7.88e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 104.04 E-value: 7.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 608 DVSFTVmPGQTV-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDG---QDISQVTQISL-RSHIGVVPQDTVLFND-TIA 681
Cdd:TIGR02142 15 DADFTL-PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPPeKRRIGYVFQEARLFPHlSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 NNIRYG--RVTAGDSEIQAaaqaagihDAILSFpEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDT 759
Cdd:TIGR02142 94 GNLRYGmkRARPSERRISF--------ERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 760 SNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSRG 815
Cdd:TIGR02142 165 PRKYEILPYLERLHaeFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
590-785 |
8.27e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.78 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCiRIDGQDI--------SQVTQIS 661
Cdd:PRK14243 11 LRTENLNVYYGSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQDTVLFNDTIANNIRYGRVTAG-----DSEIQAAAQAAGIHDAIlsfpegyETQVGERGLKLSGGEKQRVA 736
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGARINGykgdmDELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRL 785
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
590-810 |
1.09e-23 |
|
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: 100.59 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLR 663
Cdd:COG4181 9 IELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 S-HIGVVPQD-------TVLFNdtiannirygrVT-----AGDSEiqaaaqAAGIHDAILsfpegyeTQVG--ERgLK-- 726
Cdd:COG4181 89 ArHVGFVFQSfqllptlTALEN-----------VMlplelAGRRD------ARARARALL-------ERVGlgHR-LDhy 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 727 ---LSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVctNR---TTIV-VAHRLSTVVNADQILVIKD 799
Cdd:COG4181 144 paqLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFEL--NRergTTLVlVTHDPALAARCDRVLRLRA 221
|
250
....*....|.
gi 18034785 800 GCIIERGRHEA 810
Cdd:COG4181 222 GRLVEDTAATA 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
590-800 |
1.29e-23 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 100.10 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCI----RIDGQDISQVTQISLRSH 665
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 IGVVPQDTVLFNDTIANNI---------RYGRVTAGDSeiqaaaqaagIHDAILSFPEGYETQVGERGLKLSGGEKQRVA 736
Cdd:cd03290 81 VAYAAQKPWLLNATVEENItfgspfnkqRYKAVTDACS----------LQPDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 737 IARTILKAPDIILLDEATSALDTS-NERAIQASLAKVCTN--RTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
590-806 |
1.88e-23 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 100.11 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:cd03296 3 IEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFND-TIANNIRYG-RVTAGDSEIQAAAQAAGIHDAI----LS-FPEGYETQvgerglkLSGGEKQRVAIARTIL 742
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqLDwLADRYPAQ-------LSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVG 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
606-807 |
3.45e-23 |
|
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: 99.05 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRSHIGVVP--QDTVLFND-TIAN 682
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGRtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 683 NIRYGRVTAGDSEIQAAAQAAGIHDA------ILSF---PEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLDEA 753
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAreraeeLLERvglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 754 TSALDTSNERAIQASLAKV-CTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGR 807
Cdd:cd03219 171 AAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
591-803 |
4.05e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.81 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL----R 663
Cdd:PRK10535 6 ELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVVPQDTVLFND-TIANNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERGLKLSGGEKQRVAIARTIL 742
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTN-RTTIVVAHRLSTVVNADQILVIKDGCII 803
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
606-800 |
4.62e-23 |
|
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: 98.66 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ----DISQVTQ---ISLRSH-IGVVPQdtvlFN 677
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPreiLALRRRtIGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 678 DTIAnnirygRVTAGDseiqaaaqaagihdaILSFP---EGYETQVG-ERGLKL------------------SGGEKQRV 735
Cdd:COG4778 103 RVIP------RVSALD---------------VVAEPlleRGVDREEArARARELlarlnlperlwdlppatfSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIV-VAHRLSTVVN-ADQILVIKDG 800
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
590-812 |
5.31e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.06 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISlRSHIGVV 669
Cdd:PRK13536 42 IDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQ-DTVLFNDTIANNI----RYGRVTAGDSEiqaaaqaaGIHDAILSFPEgYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMSTREIE--------AVIPSLLEFAR-LESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVV-------AHRLstvvnADQILVIKDGCIIERGRHEALL 812
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
590-813 |
1.20e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:PRK09536 4 IDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVL-FNDTIANNIRYGRV-------TAGDSEiqaaaqAAGIHDAIlsfPEGYETQVGERGL-KLSGGEKQRVAIART 740
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGRTphrsrfdTWTETD------RAAVERAM---ERTGVAQFADRPVtSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 741 ILKAPDIILLDEATSALDTSNE-RAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
570-804 |
1.72e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 570 EETEVKDVPGAGPLRFHKGR------VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS 643
Cdd:COG0488 290 EREEPPRRDKTVEIRFPPPErlgkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 644 SGCIRIdGQDIsqvtqislrsHIGVVPQDTVLF--NDTIANNIRYGRVTAGDSEIQaaaqaagihdAIL-SF---PEGYE 717
Cdd:COG0488 369 SGTVKL-GETV----------KIGYFDQHQEELdpDKTVLDELRDGAPGGTEQEVR----------GYLgRFlfsGDDAF 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 718 TQVGerglKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAK----VctnrttIVVAH-R--LSTVvn 790
Cdd:COG0488 428 KPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV-- 495
|
250
....*....|....
gi 18034785 791 ADQILVIKDGCIIE 804
Cdd:COG0488 496 ATRILEFEDGGVRE 509
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
588-800 |
1.79e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISqvtqislrshi 666
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 gVVPQDTVLFNDTIANNIRYGRVTA--GDSEIQAAAQAAGIHDAILSFpegyeTQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:COG4178 430 -FLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
590-800 |
3.74e-22 |
|
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: 95.43 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqvtQISLRSHIGVV 669
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFND-TIANNIRYGRVTAGdseiqaaaqaAGIHDA---ILSFPEGYEtqVGERGLK----LSGGEKQRVAIARTI 741
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYLAQLKG----------LKKEEArrrIDEWLERLE--LSEYANKrveeLSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 742 LKAPDIILLDEATSALDTSN----ERAIQASLAKvctNRTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNvellKDVIRELARA---GKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
606-800 |
4.46e-22 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 97.23 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqislrshIGVVPQDTVLFNDTIANNIR 685
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 686 YGrVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAI 765
Cdd:cd03291 120 FG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 18034785 766 -QASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:cd03291 199 fESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
590-807 |
4.69e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.12 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQI-S 661
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAA------GIHDAILSfpegyetqvgERGLKLSGGEKQ 733
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAReklalvGISESLFE----------KNPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIV-VAHRLSTVVN-ADQILVIKDGCIIERGR 807
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
590-814 |
4.77e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.93 E-value: 4.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQISLRSHIG 667
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFNDTIA-NNIRYG-RVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:PRK09493 81 MVFQQFYLFPHLTAlENVMFGpLRVRGASKEEAEKQARELLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 746 DIILLDEATSALDTS--NE--RAIQaSLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSR 814
Cdd:PRK09493 156 KLMLFDEPTSALDPElrHEvlKVMQ-DLAE--EGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
591-811 |
7.37e-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: 95.28 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----- 665
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT-----KLPPHerara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 -IGVVPQDTVLFND-TIANNIRYGRVTAGDSEiqaaaqaAGIHDAILS-FPEGYETQvGERGLKLSGGEKQRVAIARTIL 742
Cdd:TIGR03410 76 gIAYVPQGREIFPRlTVEENLLTGLAALPRRS-------RKIPDEIYElFPVLKEML-GRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEAL 811
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
591-806 |
7.85e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.52 E-value: 7.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL--FRFYDISSGCIRIDGQDISQVTqISLRSHIGV 668
Cdd:COG0396 2 EIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELS-PDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 ---------VPQDTVL-FNDTIANNIRYGRVTAGDS--EIQAAAQAAGIHDAILsfpegyetqvgERGL--KLSGGEKQR 734
Cdd:COG0396 80 flafqypveIPGVSVSnFLRTALNARRGEELSAREFlkLLKEKMKELGLDEDFL-----------DRYVneGFSGGEKKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 735 VAIARTILKAPDIILLDEATSALDTSnerAIQAsLAKVC-----TNRTTIVVAH--RLSTVVNADQILVIKDGCIIERG 806
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDID---ALRI-VAEGVnklrsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
591-809 |
1.15e-21 |
|
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: 93.75 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTqISLRSHIGV 668
Cdd:cd03217 2 EIKDLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 vpqdTVLFND-------TIANNIRYgrvtagdseiqaaaqaagihdailsfpegyetqVGErglKLSGGEKQRVAIARTI 741
Cdd:cd03217 80 ----FLAFQYppeipgvKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 742 LKAPDIILLDEATSALDTSNERAIQASLAKVCT-NRTTIVVAH--RLSTVVNADQILVIKDGCIIERGRHE 809
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
590-810 |
1.16e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQI----SLR 663
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVV-------PQDTVLFNDTIANNirygRVTAGDSEIQAAAQaagihDAILS----------FPegyetqvgergLK 726
Cdd:PRK11124 82 RNVGMVfqqynlwPHLTVQQNLIEAPC----RVLGLSKDQALARA-----EKLLErlrlkpyadrFP-----------LH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 727 LSGGEKQRVAIARTILKAPDIILLDEATSALD---TSNERAIQASLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCI 802
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAE--TGITQVIVTHEVEVARKtASRVVYMENGHI 219
|
....*...
gi 18034785 803 IERGRHEA 810
Cdd:PRK11124 220 VEQGDASC 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
590-802 |
1.77e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.08 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqiSLRS-HIGV 668
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFND-TIANNIRYG-----RVTAGDSEIQAAAQAAGIHDAILS-FPEGYETQvgerglkLSGGEKQRVAIARTI 741
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlpRRERPNAAAIKAKVTQLLEMVQLAhLADRYPAQ-------LSGGQKQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 742 LKAPDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCI 802
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
590-824 |
2.39e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.23 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----IS 661
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAILSFpeGYETQVGERG-LKLSGGEKQRVAIA 738
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFK---MNLDEVKNYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSRG 815
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237
|
....*....
gi 18034785 816 GvYAEMWQL 824
Cdd:PRK13646 238 K-KLADWHI 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
590-758 |
2.60e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.83 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNIRYG----RVTAGDSEIQAAAQAAGIHdaILSFPEGYETQvgerglkLSGGEKQRVAIARTILKA 744
Cdd:PRK11607 97 FQSYALFpHMTVEQNIAFGlkqdKLPKAEIASRVNEMLGLVH--MQEFAKRKPHQ-------LSGGQRQRVALARSLAKR 167
|
170
....*....|....
gi 18034785 745 PDIILLDEATSALD 758
Cdd:PRK11607 168 PKLLLLDEPMGALD 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
606-814 |
4.05e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQISLRSHIGVVPQDTvlfndtian 682
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 683 nirYG----RVTAGdseiqaaaqaagihdAILSFPEGYETQVG--ER-----------GLK----------LSGGEKQRV 735
Cdd:PRK11308 102 ---YGslnpRKKVG---------------QILEEPLLINTSLSaaERrekalammakvGLRpehydryphmFSGGQRQRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSneraIQAS-------------LAKVctnrttiVVAHRLSTVVN-ADQILVIKDGC 801
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVS----VQAQvlnlmmdlqqelgLSYV-------FISHDLSVVEHiADEVMVMYLGR 232
|
250
....*....|...
gi 18034785 802 IIERGRHEALLSR 814
Cdd:PRK11308 233 CVEKGTKEQIFNN 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
590-799 |
6.28e-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: 90.29 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIridgqdisqvtQISLRSHIGVV 669
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFNDTIANNIRY--GRVtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03223 70 PQRPYLPLGTLREQLIYpwDDV-------------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTnrTTIVVAHRLSTVVNADQILVIKD 799
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
590-806 |
7.40e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQISLRSHIG 667
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQ--DTVLFNDTIANNIRYGRVTAGDSEiqaaaqaagihDAILSFPEGYETQVGERGLK------LSGGEKQRVAIAR 739
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGAVNLKLPE-----------DEVRKRVDNALKRTGIEHLKdkpthcLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 740 TILKAPDIILLDEATSALD---TSNERAIQASLAKVcTNRTTIVVAHRLSTV-VNADQILVIKDGCIIERG 806
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDpmgVSEIMKLLVEMQKE-LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
597-813 |
9.25e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 597 FSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ------DISQVTQISLRSHIGVVP 670
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLF-NDTIANNIRYGRVTAGdseIQAAAQAAGIHDAILSfPEGYETQVGER----GLKLSGGEKQRVAIARTILKAP 745
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHG---IKEKREIKKIVEECLR-KVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 746 DIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
593-806 |
1.11e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:PRK11231 6 ENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TVLFND-TIANNIRYGRvtagdSEIQAAAQAAGIHDAILSFPEGYETQVGE----RGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK11231 85 HLTPEGiTVRELVAYGR-----SPWLSLWGRLSAEDNARVNQAMEQTRINHladrRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTN-RTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
590-832 |
1.68e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----IS 661
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEiqaaaqaagiHDAILSFPE-----GYETQVGERG-LKLSGGEKQ 733
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE----------EDAKQKAREmielvGLPEELLARSpFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEA 810
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
|
250 260
....*....|....*....|..
gi 18034785 811 LLSRGgvyAEMWQLQQQGQETV 832
Cdd:PRK13634 233 IFADP---DELEAIGLDLPETV 251
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
590-814 |
2.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.79 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQ--DTVLFNDTIANNIRYGRVTAG-DSEIQAAAQAAGIHDAILsfpEGYETQVGERglkLSGGEKQRVAIARTILKAPD 746
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGlDEETVAHRVSSALHMLGL---EELRDRVPHH---LSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTN--RTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSR 814
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
590-807 |
2.61e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETlQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQiSLRShIGVV 669
Cdd:PRK11000 4 VTLRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP-AERG-VGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNIRYGRVTAG--DSEIQAAAQAAGihdAILsfpegyetQVG---ERGLK-LSGGEKQRVAIARTIL 742
Cdd:PRK11000 81 FQSYALYpHLSVAENMSFGLKLAGakKEEINQRVNQVA---EVL--------QLAhllDRKPKaLSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAH-RLSTVVNADQILVIKDGCIIERGR 807
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
601-760 |
3.21e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL-------FRFydisSGCIRIDGQDISQVtQISLRsHIGVVPQDT 673
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFSA----SGEVLLNGRRLTAL-PAEQR-RIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 674 VLF-NDTIANNIRYG---RVTAGD--SEIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKAPDI 747
Cdd:COG4136 86 LLFpHLSVGENLAFAlppTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRA 154
|
170
....*....|...
gi 18034785 748 ILLDEATSALDTS 760
Cdd:COG4136 155 LLLDEPFSKLDAA 167
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
592-758 |
3.64e-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: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 592 FENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqisLRshIGVVPQ 671
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 D-------TVL-----------------------FNDTIANNIRYGRVT---------AGDSEIqaaaqaagihDAILS- 711
Cdd:COG0488 69 EppldddlTVLdtvldgdaelraleaeleeleakLAEPDEDLERLAELQeefealggwEAEARA----------EEILSg 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18034785 712 --FPEG-YETQVGErglkLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:COG0488 139 lgFPEEdLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
590-814 |
3.86e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISlRSHIGVV 669
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFND-TIANNIR-YGRVTAGDSEIQAAAQAAGIHDAILSfpEGYETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK13537 86 PQFDNLDPDfTVRENLLvFGRYFGLSAAAARALVPPLLEFAKLE--NKADAKVGE----LSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTNRTTIVV-------AHRLstvvnADQILVIKDGCIIERGRHEALLSR 814
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
457-836 |
4.74e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 96.20 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 457 LLNFETVKYYNAE-GYElerYREAILKFQGLEWKSTASLV------LLNQTQNMV--IGFG---LLAGSLLCAY-FVSER 523
Cdd:PLN03232 486 LASMDTVKCYAWEkSFE---SRIQGIRNEELSWFRKAQLLsafnsfILNSIPVVVtlVSFGvfvLLGGDLTPARaFTSLS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 524 RLQVgdfvlfgtyitqLYMPLNWFGTYYRMIQTNFIDMENMFDL-LKEETEVKDVPgagPLRFHKGRVEFENVHFSYADG 602
Cdd:PLN03232 563 LFAV------------LRSPLNMLPNLLSQVVNANVSLQRIEELlLSEERILAQNP---PLQPGAPAISIKNGYFSWDSK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RE--TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRfyDISSgciridgqdiSQVTQISLRSHIGVVPQDTVLFNDTI 680
Cdd:PLN03232 628 TSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--ELSH----------AETSSVVIRGSVAYVPQVSWIFNATV 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAGDSEIQAAAQAAGIHDAILsFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTS 760
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 761 NERAIQASLAK-VCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQQQGQETVPEDS 836
Cdd:PLN03232 775 VAHQVFDSCMKdELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNT 851
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
591-806 |
5.30e-20 |
|
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: 90.01 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDISQVtQISLRSHIGV 668
Cdd:TIGR01978 2 KIKDLHVSVED-KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLEL-EPDERARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 ---------VPQDTVL-FNDTIANNIRYGRvtaGDSEIQAAAQAAGIHD--AILSFPEGYEtqvgERGLK--LSGGEKQR 734
Cdd:TIGR01978 80 flafqypeeIPGVSNLeFLRSALNARRSAR---GEEPLDLLDFEKLLKEklALLDMDEEFL----NRSVNegFSGGEKKR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 735 VAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCT-NRTTIVVAH--RLSTVVNADQILVIKDGCIIERG 806
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREpDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
606-800 |
5.40e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.13 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqislrshIGVVPQDTVLFNDTIANNIR 685
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 686 YGrVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAI 765
Cdd:TIGR01271 509 FG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*.
gi 18034785 766 -QASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:TIGR01271 588 fESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
593-752 |
8.13e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.32 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTIlrllfrFYDI------SSGCIRIDGQDISQVTqISLRSH- 665
Cdd:COG1137 7 ENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIvglvkpDSGRIFLDGEDITHLP-MHKRARl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 -IGVVPQDTVLFND-TIANNIRygrvtagdseiqaaaqaagihdAILSF----PEGYETQVGE-------------RGLK 726
Cdd:COG1137 79 gIGYLPQEASIFRKlTVEDNIL----------------------AVLELrklsKKEREERLEElleefgithlrksKAYS 136
|
170 180
....*....|....*....|....*.
gi 18034785 727 LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDE 162
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
606-806 |
8.57e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 89.71 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-----QVTQISL-RS--HIGVVPQDTVLFN 677
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpphRIARLGIaRTfqNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 678 DTIANNIRYGRvtagdseiqaaaqaaGIHDAILSFPEGY--ETQVGER--------GLK---------LSGGEKQRVAIA 738
Cdd:COG0411 100 VLVAAHARLGR---------------GLLAALLRLPRARreEREARERaeellervGLAdradepagnLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLAKVC--TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEG 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
590-813 |
9.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.66 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----IS 661
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERG-LKLSGGEKQRVAIA 738
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV-----GLSEDLISKSpFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 739 RTILKAPDIILLDEATSALD-TSNERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
606-813 |
9.09e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 9.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS----HIGVVPQDTVLF-NDTI 680
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAGdseIQAAAQAAGIHDAILSFpeGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTS 760
Cdd:PRK10070 124 LDNTAFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 761 NERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK10070 199 IRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
603-815 |
1.56e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 94.42 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGciridgqdisqvTQISLRSHIGVVPQDTVLFNDTIAN 682
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD------------ASVVIRGTVAYVPQVSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 683 NIRYG------------RVTAGDseiqaaaqaagiHDAILsFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILL 750
Cdd:PLN03130 698 NILFGspfdperyeraiDVTALQ------------HDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 751 DEATSALDTSNERAI-QASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRG 815
Cdd:PLN03130 765 DDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
591-814 |
2.06e-19 |
|
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: 92.83 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYADGRETLQ---DVSFTVMPGQTVALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVTQISLR 663
Cdd:COG4172 8 SVEDLSVAFGQGGGTVEavkGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 ----SHIGVVPQD--TVLfND--TIANNI-----RYGRVTAGD--SEIQAAAQAAGIHDA---ILSFPEgyetqvgergl 725
Cdd:COG4172 88 rirgNRIAMIFQEpmTSL-NPlhTIGKQIaevlrLHRGLSGAAarARALELLERVGIPDPerrLDAYPH----------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 726 KLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTT--IVVAHRLSTVVN-ADQILVIKDGCI 802
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMalLLITHDLGVVRRfADRVAVMRQGEI 235
|
250
....*....|..
gi 18034785 803 IERGRHEALLSR 814
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
590-806 |
2.35e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRET-----LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI-SLR 663
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVVPQ--DTVLFNDTIANNIRYGRVTAG--DSEIQAAAqaagihDAILSFPEGYETQVGERGLkLSGGEKQRVAIAR 739
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGPENLGipPEEIRERV------DESLKKVGMYEYRRHAPHL-LSGGQKQRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVNADQILVIKDGCIIERG 806
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
599-800 |
2.94e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 599 YADGR---ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT---QISLRSH-IGVVPQ 671
Cdd:PRK11629 15 YQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 DTVLFND-TIANNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILL 750
Cdd:PRK11629 95 FHHLLPDfTALENVAMPLLIGKKKPAEINSRALEMLAAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 751 DEATSALDTSNERAIQASLAKVCTNRTT--IVVAHRLSTVVNADQILVIKDG 800
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
593-758 |
6.19e-19 |
|
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: 86.83 E-value: 6.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRSHIGV--VP 670
Cdd:cd03218 4 ENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-MHKRARLGIgyLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLFND-TIANNIRYGRVTAGDSEiqaaaqaAGIHDAILSFPE--GYETQVGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03218 82 QEASIFRKlTVEENILAVLEIRGLSK-------KEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170
....*....|.
gi 18034785 748 ILLDEATSALD 758
Cdd:cd03218 155 LLLDEPFAGVD 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
603-821 |
6.96e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.53 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDgqdisqvtqislRShIGVVPQDTVLFNDTIAN 682
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 683 NIRYGrvtagDSEiqaaaQAAGIHDAI---------LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEA 753
Cdd:PTZ00243 740 NILFF-----DEE-----DAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 754 TSALDTS-NERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLsRGGVYAEM 821
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATL 877
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
593-809 |
1.17e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLrshIGVVPQD 672
Cdd:PRK15056 10 NDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 T-------VLFNDTIANNiRYG------RVTAGDSEIQAAAQaagihdAILSFPEGYETQVGErglkLSGGEKQRVAIAR 739
Cdd:PRK15056 87 EevdwsfpVLVEDVVMMG-RYGhmgwlrRAKKRDRQIVTAAL------ARVDMVEFRHRQIGE----LSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKV-CTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHE 809
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
590-811 |
1.61e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.85 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDisqVTQISLRSH-IGV 668
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLF-NDTIANNIRYGRVTAGDS--EIQAAaqaagIHDAI-LSFPEGYEtqvgERGL-KLSGGEKQRVAIARTILK 743
Cdd:PRK11432 83 VFQSYALFpHMSLGENVGYGLKMLGVPkeERKQR-----VKEALeLVDLAGFE----DRYVdQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 744 APDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEAL 811
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQEL 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
590-816 |
2.01e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.70 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqislRSHIGVV 669
Cdd:COG4152 2 LELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLF-NDTIANNIRY-GR---VTAGDseiqaaaqaagIHDAILSFPEGYEtqVGERGLK----LSGGEKQRVAIART 740
Cdd:COG4152 77 PEERGLYpKMKVGEQLVYlARlkgLSKAE-----------AKRRADEWLERLG--LGDRANKkveeLSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVN-ADQILVIKDGCIIERGRHEALLSRGG 816
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
591-772 |
2.21e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.68 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVTQISLRShiG 667
Cdd:COG4525 5 TVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLF-----NDTIANNIRYGRVTAGDSEiqaaaqaaGIHDAILSfpegyetQVGERGL------KLSGGEKQRVA 736
Cdd:COG4525 80 VVFQKDALLpwlnvLDNVAFGLRLRGVPKAERR--------ARAEELLA-------LVGLADFarrriwQLSGGMRQRVG 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQASLAKV 772
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
589-809 |
2.73e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYADGrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDISQVTQISLR 663
Cdd:PRK14247 3 KIEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 664 SHIGVV-----PQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAaGIHDAILSfpEGYETQVGERGLKLSGGEKQRVAIA 738
Cdd:PRK14247 82 RRVQMVfqipnPIPNLSIFENVALGLKLNRLVKSKKELQERVRW-ALEKAQLW--DEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAH------RLStvvnaDQILVIKDGCIIERG------ 806
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGptrevf 233
|
....*.
gi 18034785 807 ---RHE 809
Cdd:PRK14247 234 tnpRHE 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
590-800 |
2.80e-18 |
|
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: 82.11 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQDISqvtqislrshIGVV 669
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQdtvlfndtiannirygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18034785 750 LDEATSALDTSNERAIQASLAKvcTNRTTIVVAH-R--LSTVvnADQILVIKDG 800
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
606-783 |
3.39e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 84.24 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQDISQVTqisLRSHIGVVPQ-DTVLFNDTIA 681
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKPDQ---FQKCVAYVRQdDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 NNIRY-----GRVTAGDSEIQAAAQAAGIHDAILsfpegyeTQVGERGLK-LSGGEKQRVAIARTILKAPDIILLDEATS 755
Cdd:cd03234 100 ETLTYtailrLPRKSSDAIRKKRVEDVLLRDLAL-------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|....*....
gi 18034785 756 ALDTSNERAIQASLAKVCT-NRTTIVVAH 783
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARrNRIVILTIH 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
606-813 |
3.52e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQ---ISLRSHIGVVPQD------ 672
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRrqlLPVRHRIQVVFQDpnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 ---TVLfnDTIANNIRygrvtagdseiqaaaqaagIHDAILSfPEGYETQV----GERGL----------KLSGGEKQRV 735
Cdd:PRK15134 377 prlNVL--QIIEEGLR-------------------VHQPTLS-AAQREQQViavmEEVGLdpetrhrypaEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLStVVNA--DQILVIKDGCIIERGRHEAL 811
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERV 513
|
..
gi 18034785 812 LS 813
Cdd:PRK15134 514 FA 515
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
590-813 |
1.39e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.88 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI-SLRSHIGV 668
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQ--DTVLFNDTIANNIRYG--RVTAGDSEIQAAAqaagihDAILSfpegyETQVGE---RGLK-LSGGEKQRVAIART 740
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRV------DRALA-----EIGLEKyrhRSPKtLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 741 ILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIV-VAHRLSTVVNADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
594-813 |
1.60e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 594 NVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDISQVTQI-SLRSHIG 667
Cdd:PRK14271 26 NLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFNDTIANNIRYGrVTAgdSEIQAAAQAAGIHDAILS---FPEGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAG-VRA--HKLVPRKEFRGVAQARLTevgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
606-806 |
2.21e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.13 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILR-----LLFRFYDISSGCIRIdGQDISQVTQIS------------LRSHIGV 668
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYI-GDKKNNHELITnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQ------AAGIHDAILsfpegyetqvgERG-LKLSGGEKQRVAIAR 739
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLakfylnKMGLDDSYL-----------ERSpFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 740 TILKAPDIILLDEATSALDTSNERA-IQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
590-811 |
2.33e-17 |
|
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: 81.65 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRSHIGVV 669
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFNDTIA--NNIRYGRVTAGDSEIQAAAQaagihDAILSFPEGYEtqVGERGLK-LSGGEKQRVAIARTILKAPD 746
Cdd:cd03265 79 FQDLSVDDELTGweNLYIHARLYGVPGAERRERI-----DELLDFVGLLE--AADRLVKtYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 747 IILLDEATSALDTSNERAIQASLAK-VCTNRTTIVV-------AHRLstvvnADQILVIKDGCIIERGRHEAL 811
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKlKEEFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGTPEEL 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
605-809 |
2.83e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.16 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 605 TLQDVSFTV---MPGQTV-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ-ISL---RSHIGVVPQDTVLF 676
Cdd:PRK11144 9 QLGDLCLTVnltLPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgICLppeKRRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 677 -NDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQRVAIARTILKAPDIILLDEATS 755
Cdd:PRK11144 89 pHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 756 ALDTSNERAIQASLAKVC-TNRTTIV-VAHRLSTVVN-ADQILVIKDGCIIERGRHE 809
Cdd:PRK11144 158 SLDLPRKRELLPYLERLArEINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLE 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
601-797 |
3.24e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.74 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGqdisqvtqislRSHIGVVPQDTVL---FN 677
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 678 DTIANNIRYG---------RVTAGD-SEIQAAAQAAGIHDaiLSfpegyETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:NF040873 72 LTVRDLVAMGrwarrglwrRLTRDDrAAVDDALERVGLAD--LA-----GRQLGE----LSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVC-TNRTTIVVAHRLSTVVNADQILVI 797
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
606-800 |
3.46e-17 |
|
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: 81.74 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV--TQISLRSHIGVVPQDTVLFNDTIA-N 682
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRMVVFQNYSLLPWLTVRENIALAvD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 683 NIRYGRVTAGDSEIQAAaqaagiHDAILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNE 762
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEE------HIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18034785 763 RAIQASLAKVCTNR--TTIVVAHRL-STVVNADQILVIKDG 800
Cdd:TIGR01184 151 GNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
602-771 |
4.04e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGvvPQDTVLFNDTIA 681
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 NNIRYGRVTAGDSEiqaaaqaAGIHDAILSF--------PEGYetqvgerglkLSGGEKQRVAIARTILKAPDIILLDEA 753
Cdd:PRK13539 92 ENLEFWAAFLGGEE-------LDIAAALEAVglaplahlPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180
....*....|....*....|..
gi 18034785 754 TSALDTSNERA----IQASLAK 771
Cdd:PRK13539 155 TAALDAAAVALfaelIRAHLAQ 176
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
597-804 |
4.45e-17 |
|
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: 82.16 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 597 FSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---LRSHIGVVPQD 672
Cdd:TIGR02769 17 LFGAKQRAPvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TV-LFN------DTIANNIR-YGRVTAGDSE--IQAAAQAAGIHDAILSfpegyetqvgERGLKLSGGEKQRVAIARTIL 742
Cdd:TIGR02769 97 SPsAVNprmtvrQIIGEPLRhLTSLDESEQKarIAELLDMVGLRSEDAD----------KLPRQLSGGQLQRINIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNRTT--IVVAHRLSTVVN-ADQILVIKDGCIIE 804
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
585-803 |
4.46e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.06 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 585 FHKGRVEfENVhfsyadgreTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS 664
Cdd:COG1101 11 FNPGTVN-EKR---------ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 665 HIGVVPQDTVL---FNDTIANNI--------RYG---RVTAGDSEIqaaaqaagIHDAILSFPEGYETQVGER-GLkLSG 729
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENLalayrrgkRRGlrrGLTKKRREL--------FRELLATLGLGLENRLDTKvGL-LSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 730 GEKQRVAIARTILKAPDIILLDEATSALD--TSN------ERAIQASlakvctNRTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDpkTAAlvleltEKIVEEN------NLTTLMVTHNMEQALDyGNRLIMMHEG 225
|
...
gi 18034785 801 CII 803
Cdd:COG1101 226 RII 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
590-788 |
4.69e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS-----GCIRIDGQDI--SQVTQISL 662
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVVPQDTVLFNDTIANNIRYGRVTAG-------DSEIQAAAQAAGIHDAIlsfpegyETQVGERGLKLSGGEKQRV 735
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSNERAIQASL--AKVCTNRTTIVVAHRLSTV 788
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQV 214
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
265-555 |
6.90e-17 |
|
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: 82.17 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 265 VLLCMGLMGLDRALNVLVPIFYR----DIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQF 340
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKilidDVLIQLGPGGNTSLLLLLVLGLAGAYVLSA-------LLGILRGRLLARLGER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 341 TSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLS----YLVFNIIpTLadIIIGIIYFSMffNAWFGLI 416
Cdd:cd18563 74 ITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSdglpDFLTNIL-MI--IGIGVVLFSL--NWKLALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 417 VFLCMSLYLILTIMV-----TEWRAKFRR--DMNTQENatraravDSLLNFETVKYYNAEGYELERYREAILKFQglewK 489
Cdd:cd18563 149 VLIPVPLVVWGSYFFwkkirRLFHRQWRRwsRLNSVLN-------DTLPGIRVVKAFGQEKREIKRFDEANQELL----D 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 490 STASLVLLNQTQNMVIGFGLLAGSLLCAYF----VSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:cd18563 218 ANIRAEKLWATFFPLLTFLTSLGTLIVWYFggrqVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWIT 287
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
588-828 |
7.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.98 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYADGR----ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSG-------CIRIDGQDISQ 656
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 657 VTQisLRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDaILSFPEGYetqVGERGLKLSGGEKQR 734
Cdd:PRK13645 85 VKR--LRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLK-LVQLPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 735 VAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTN--RTTIVVAHRLSTVVN-ADQILVIKDGCIIERG----- 806
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGspfei 238
|
250 260
....*....|....*....|....*...
gi 18034785 807 -RHEALLSR-----GGVYAEMWQLQQQG 828
Cdd:PRK13645 239 fSNQELLTKieidpPKLYQLMYKLKNKG 266
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
603-784 |
8.75e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.00 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFY--DISSGCIRIDGQDISQVTQISlrshigvvpqDTVLFNDTI 680
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLI----------DAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRY-GRVtagdseiqaaaqaaGIHDAIL---SFPEgyetqvgerglkLSGGEKQRVAIARTILKAPDIILLDEATSA 756
Cdd:COG2401 113 KDAVELlNAV--------------GLSDAVLwlrRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|
gi 18034785 757 LDTSNERAIQASLAKVCT-NRTTIVVA-HR 784
Cdd:COG2401 167 LDRQTAKRVARNLQKLARrAGITLVVAtHH 196
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
590-758 |
1.25e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.20 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDisqVTQISLRSH-IGV 668
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV---VNELEPADRdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLF-NDTIANNIRYGRVTAGDS--EIQAAaqaagIHDA--ILSFpegyETQVGERGLKLSGGEKQRVAIARTILK 743
Cdd:PRK11650 81 VFQNYALYpHMSVRENMAYGLKIRGMPkaEIEER-----VAEAarILEL----EPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 18034785 744 APDIILLDEATSALD 758
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
590-806 |
1.84e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQISL 662
Cdd:PRK14267 5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 RSHIGVV-----PQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAaGIHDAILSfpEGYETQVGERGLKLSGGEKQRVAI 737
Cdd:PRK14267 84 RREVGMVfqypnPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEW-ALKKAALW--DEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 738 ARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
606-800 |
1.98e-16 |
|
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: 77.86 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-VTQISLRSHIGVVPQD---TVLFND-TI 680
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIAYVPEDrkrEGLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIrygrvtagdseiqaaaqaagihdAILSFpegyetqvgerglkLSGGEKQRVAIARTILKAPDIILLDEATSALDTS 760
Cdd:cd03215 96 AENI-----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18034785 761 NERAIQASLAKVCTNRTTIVVahrLST-----VVNADQILVIKDG 800
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEG 180
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
606-804 |
2.83e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRS-HIGVVPQDTVLFNDTIA 681
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAkHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 -NNIRYGRVTAGDSEIQAAAQAAgihdAILSfpegyETQVGER----GLKLSGGEKQRVAIARTILKAPDIILLDEATSA 756
Cdd:PRK10584 106 lENVELPALLRGESSRQSRNGAK----ALLE-----QLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 757 LDTSNERAIQASLAKVctNR----TTIVVAHRLSTVVNADQILVIKDGCIIE 804
Cdd:PRK10584 177 LDRQTGDKIADLLFSL--NRehgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
603-813 |
4.59e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKS----TILRLLFR---FYdiSSGCIRIDGQDISQVTQISLR----SHIGVVPQ 671
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY--PSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 D-TVLFN--DTIANNI-------RYGRVTAGDSEIQAAAQAAGIHDA---ILSFPEgyetqvgerglKLSGGEKQRVAIA 738
Cdd:PRK15134 100 EpMVSLNplHTLEKQLyevlslhRGMRREAARGEILNCLDRVGIRQAakrLTDYPH-----------QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLA--KVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
606-803 |
4.80e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVT----QISLRSHIGVVPQDTVLFND-TI 680
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRirspRDAIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAGdseiQAAAQAAGIHDAILSFPEGYetqvgerGLK---------LSGGEKQRVAIARTILKAPDIILLD 751
Cdd:COG3845 98 AENIVLGLEPTK----GGRLDRKAARARIRELSERY-------GLDvdpdakvedLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 752 EATSALdTSNE-RAIQASLAKVCTNRTTIV-VAHRLSTVV-NADQILVIKDGCII 803
Cdd:COG3845 167 EPTAVL-TPQEaDELFEILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
606-806 |
5.63e-16 |
|
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: 77.96 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSHIGVVPQDTVLfndtiaNNIR 685
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-----LLGLGGGFNPELTGR------ENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 686 -----YGRVTAGDSEIQaaaqaagihDAILSFPE-G--YETQVGErglkLSGGEKQRVAIARTILKAPDIILLDEATSAL 757
Cdd:cd03220 107 lngrlLGLSRKEIDEKI---------DEIIEFSElGdfIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18034785 758 DTS-NERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03220 174 DAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
265-548 |
5.80e-16 |
|
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: 79.40 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRG-------VFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 345 VELRLFSHLHELSLRWHLGRRTGEvlrIVDRGTSSVTGL---LSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLIVFLCM 421
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDKARTGD---LMSRCTSDVDTIrrfLAFGLVELVRAVL-LFIGALIIMFSINWKLTLISLAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 422 SLYLILTI-MVTEWRAKFRR------DMNT--QENATRARavdsllnfeTVKYYNAEGYELER-------YREAILKFQG 485
Cdd:cd18542 150 PFIALFSYvFFKKVRPAFEEireqegELNTvlQENLTGVR---------VVKAFAREDYEIEKfdkeneeYRDLNIKLAK 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 486 LEWKSTASLVLLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFG 548
Cdd:cd18542 221 LLAKYWPLMDFLSGLQIVLV---LWVG----GYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
604-806 |
6.54e-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: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHIGVV------------PQ 671
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgqktqlwwdlpVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 DTVLFNDTIAnNIRYGRVTAGDSEIQaaaqaagihdAILSFPEGYETQVgeRglKLSGGEKQRVAIARTILKAPDIILLD 751
Cdd:cd03267 114 DSFYLLAAIY-DLPPARFKKRLDELS----------ELLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18034785 752 EATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
590-806 |
8.09e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.01 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAD----GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---- 661
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYEtqvgERGLKLSGGEKQRVAIAR 739
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWE----KSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKV-CTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
601-831 |
8.33e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRetLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQISLRSHIGVVPQDTV------ 674
Cdd:COG4138 9 AGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 675 ------LFNDTIANnirygrVTAGDSEIQAAAQAAGIHDAilsfpegYETQVGerglKLSGGEKQRVAIARTILKA-PDI 747
Cdd:COG4138 86 vfqylaLHQPAGAS------SEAVEQLLAQLAEALGLEDK-------LSRPLT----QLSGGEWQRVRLAAVLLQVwPTI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 748 ------ILLDEATSALDTSNERAIQASLAKVCT-NRTTIVVAHRLS-TVVNADQILVIKDGCIIERGR-----HEALLSR 814
Cdd:COG4138 149 npegqlLLLDEPMNSLDVAQQAALDRLLRELCQqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGEtaevmTPENLSE 228
|
250
....*....|....*..
gi 18034785 815 ggVYAEMWQLQQQGQET 831
Cdd:COG4138 229 --VFGVKFRRLEVEGHR 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
595-811 |
1.41e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.98 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 595 VHFSYADGR-------ETLQ---DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS 664
Cdd:PRK15079 16 VHFDIKDGKqwfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 665 higvVPQD-TVLFNDTIAN-NiryGRVTAGDSeiqaaaqaagIHDAILSF-PEGYETQVGER--------GL-------- 725
Cdd:PRK15079 96 ----VRSDiQMIFQDPLASlN---PRMTIGEI----------IAEPLRTYhPKLSRQEVKDRvkammlkvGLlpnlinry 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 726 --KLSGGEKQRVAIARTILKAPDIILLDEATSALDTSneraIQASLAKVCTN------RTTIVVAHRLSTVVN-ADQILV 796
Cdd:PRK15079 159 phEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQQlqremgLSLIFIAHDLAVVKHiSDRVLV 234
|
250
....*....|....*
gi 18034785 797 IKDGCIIERGRHEAL 811
Cdd:PRK15079 235 MYLGHAVELGTYDEV 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
593-812 |
1.44e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQ- 671
Cdd:PRK10575 15 RNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 ----DTVLFNDTIANNiRY------GRVTAGDSEiqaaaqaaGIHDAIlsfpegyeTQVGERGL------KLSGGEKQRV 735
Cdd:PRK10575 94 lpaaEGMTVRELVAIG-RYpwhgalGRFGAADRE--------KVEEAI--------SLVGLKPLahrlvdSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALL 812
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
602-806 |
1.52e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.27 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---------RSHIGVV--- 669
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVhqh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFNDTIANNI----------RYGRV--TAGD----SEIQAAAqaagIHDAILSFpegyetqvgerglklSGGEKQ 733
Cdd:PRK11701 98 PRDGLRMQVSAGGNIgerlmavgarHYGDIraTAGDwlerVEIDAAR----IDDLPTTF---------------SGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSneraIQASLAKVCTNRTT------IVVAHRLSTV-VNADQILVIKDGCIIERG 806
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVArLLAHRLLVMKQGRVVESG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
590-807 |
3.95e-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: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-VTQISLRSHIGV 668
Cdd:PRK11614 6 LSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFND-TIANNIRYGRVTAGDSEIQAAaqaagIHDAILSFPEGYETQVgERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQER-----IKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRlstvvNADQILVIKD-GCIIERGR 807
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQ-----NANQALKLADrGYVLENGH 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
606-806 |
4.30e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdISQVtqISLRShiGVVPQDT----VLFNDTIa 681
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL--LELGA--GFHPELTgrenIYLNGRL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 nnirYGRVTAgdsEIQAaaqaagIHDAILSFpegyeTQVGE---RGLK-LSGGEKQRVAIARTILKAPDIILLDEATSAL 757
Cdd:COG1134 116 ----LGLSRK---EIDE------KFDEIVEF-----AELGDfidQPVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18034785 758 DTS-NERAIQASLAKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:COG1134 178 DAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDG 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
590-800 |
4.85e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QISLRSHIGV 668
Cdd:PRK09700 6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFND-TIANNIRYGRVTA----GDSEIQAAAQAagIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILK 743
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGRHLTkkvcGVNIIDWREMR--VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 744 APDIILLDEATSALDTSNERAIQASLAKVCTNRTTIV-VAHRLSTVVN-ADQILVIKDG 800
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
606-804 |
5.22e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-----------QISLRSHIGVV-PQDT 673
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdiQMVFQDSISAVnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 674 VlfNDTIANNIRYgrVTAGDSE-----IQAAAQAAGIHDAILSfpegyetqvgERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:PRK10419 108 V--REIIREPLRH--LLSLDKAerlarASEMLRAVDLDDSVLD----------KRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTT--IVVAHRLSTVVN-ADQILVIKDGCIIE 804
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
583-800 |
7.58e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 583 LRFHKGRVEFENVhfsyadgrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQIS 661
Cdd:PRK11288 5 LSFDGIGKTFPGV--------KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQDTVLFND-TIANNI-------RYGRVTAGD--SEIQAAAQAAGIH-DAilsfpegyETQVGErglkLSGG 730
Cdd:PRK11288 77 LAAGVAIIYQELHLVPEmTVAENLylgqlphKGGIVNRRLlnYEAREQLEHLGVDiDP--------DTPLKY----LSIG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 731 EKQRVAIARTILKAPDIILLDEATSALdTSNE-----RAIQASLAKvctNRTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSL-SAREieqlfRVIRELRAE---GRVILYVSHRMEEIFAlCDAITVFKDG 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
591-772 |
8.81e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqislrSHIGVVP 670
Cdd:PRK11248 3 QISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLFN-DTIANNIRYGRVTAGDSEIQAAAQAAGIhdAILSFPEGYETQvgeRGLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGLQLAGVEKMQRLEIAHQM--LKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180
....*....|....*....|...
gi 18034785 750 LDEATSALDTSNERAIQASLAKV 772
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKL 174
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
604-813 |
1.02e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV------------TQI-SLRSHIGVVP 670
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadkNQLrLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLFND-TIANNIRYGRVtagdsEIQAAAQAAGIHDAILsfpegYETQVG--ERG-----LKLSGGEKQRVAIARTIL 742
Cdd:PRK10619 99 QHFNLWSHmTVLENVMEAPI-----QVLGLSKQEARERAVK-----YLAKVGidERAqgkypVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 743 KAPDIILLDEATSALD---TSNERAIQASLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK10619 169 MEPEVLLFDEPTSALDpelVGEVLRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
593-758 |
1.16e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QISLRSHIGVVPQ 671
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 DTVLFND-TIANNIrygrvtAGDSEIQAAAQAAGIHDAILSFPEGYETQ--VGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:PRK10895 86 EASIFRRlSVYDNL------MAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170
....*....|
gi 18034785 749 LLDEATSALD 758
Cdd:PRK10895 160 LLDEPFAGVD 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
590-765 |
1.29e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqisLRshIGVV 669
Cdd:PRK09544 5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLfNDTIANNI-RYGRVTAGDSEIQAAAQAAGIHDA-ILSFPEGyetqvgerglKLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK09544 73 PQKLYL-DTTLPLTVnRFLRLRPGTKKEDILPALKRVQAGhLIDAPMQ----------KLSGGETQRVLLARALLNRPQL 141
|
170
....*....|....*...
gi 18034785 748 ILLDEATSALDTSNERAI 765
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVAL 159
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
593-802 |
1.45e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHIGVVPQD 672
Cdd:PRK11247 16 NAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TVLFN-DTIANNIRYG-----RVTAgdseiqaaaqaagiHDAILSFpeGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGlkgqwRDAA--------------LQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCI 802
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
601-758 |
2.69e-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: 72.39 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTI 680
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAGDSEIQaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIARTILKAPDIILLDEAT 754
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRT-------IEDAL--------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....
gi 18034785 755 SALD 758
Cdd:TIGR01189 156 TALD 159
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
602-800 |
2.73e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.75 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsQVTQISLRSHIGVVPQDTVLFND-TI 680
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAGDS------EIQAAAQAAGIHDailsfpegyetQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEAT 754
Cdd:TIGR01257 1021 AEHILFYAQLKGRSweeaqlEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18034785 755 SALDTSNERAIQASLAKVCTNRTTIVVAHRLSTV-VNADQILVIKDG 800
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQG 1136
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
601-798 |
3.28e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.14 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTI 680
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIRYGRVTAGDSeiqaaaqaaGIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIARTILKAPDIILLDEAT 754
Cdd:cd03231 91 LENLRFWHADHSDE---------QVEEAL--------ARVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18034785 755 SALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIK 798
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
577-786 |
4.45e-14 |
|
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: 76.33 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 577 VPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD--- 653
Cdd:TIGR00954 439 VPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklf 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 654 -ISQVTQISLRSHigvvpQDTVLFNDTIANNIRYGrvtAGDSEIQAAAQAAGIHDaILSFPEGYETqVGERGLKLSGGEK 732
Cdd:TIGR00954 519 yVPQRPYMTLGTL-----RDQIIYPDSSEDMKRRG---LSDKDLEQILDNVQLTH-ILEREGGWSA-VQDWMDVLSGGEK 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18034785 733 QRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVctNRTTIVVAHRLS 786
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
590-811 |
6.02e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHI 666
Cdd:PRK11831 8 VDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLFND-TIANNIRYG--RVTAGDSEIqaaaqaagIHDAILSFPEGyetqVGERGL------KLSGGEKQRVAI 737
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPlrEHTQLPAPL--------LHSTVMMKLEA----VGLRGAaklmpsELSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 738 ARTILKAPDIILLDEATSALDTsnerAIQASLAKVCTNR------TTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEA 810
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDP----ITMGVLVKLISELnsalgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQA 230
|
.
gi 18034785 811 L 811
Cdd:PRK11831 231 L 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
601-800 |
6.39e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDIsQVTQI--SLRSHIGVVPQDTVLF 676
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEEL-QASNIrdTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 677 ND-TIANNIRYGRvtagdsEIQaaaqaagiHDAILSFPEGY----------------ETQVGErglkLSGGEKQRVAIAR 739
Cdd:PRK13549 95 KElSVLENIFLGN------EIT--------PGGIMDYDAMYlraqkllaqlkldinpATPVGN----LGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 740 TILKAPDIILLDEATSALdTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
606-818 |
8.89e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 8.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfYDI---SSGCIRIDGQDISQvTQISLRSHIGVV------------P 670
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKML---TGIlvpTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 671 QDTVLFNDTIannirYgRVTAGD--------SEIqaaaqaAGIHDaILSfpegyeTQVgeRglKLSGGEKQRVAIARTIL 742
Cdd:COG4586 114 IDSFRLLKAI-----Y-RIPDAEykkrldelVEL------LDLGE-LLD------TPV--R--QLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQASLAKVCTNR-TTIVVA-HRLSTVVN-ADQILVIKDGCIIERGRHEALLSRGGVY 818
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
606-811 |
1.09e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.81 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD--------------------------ISQVTQ 659
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrfkkIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 660 IslRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDaILSFPEGYetqVGERGLKLSGGEKQRVAI 737
Cdd:PRK13651 103 I--RRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIE-LVGLDESY---LQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 738 ARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTN-RTTIVVAHRLSTVVN-ADQILVIKDGCIIERGR-HEAL 811
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDtYDIL 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
609-813 |
1.14e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.45 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 609 VSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSG--CIRIdGQDISQVTQISL------RSHIGVVPQDTVLF-NDT 679
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRV-GDEWVDMTKPGPdgrgraKRYIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 680 IANNIRygrvtagdseiqaaaqaagihDAI-LSFPE--------------GYETQVGERGL-----KLSGGEKQRVAIAR 739
Cdd:TIGR03269 382 VLDNLT---------------------EAIgLELPDelarmkavitlkmvGFDEEKAEEILdkypdELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASL--AKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
589-806 |
1.44e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYadGRETL-QDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:PRK10253 7 RLRGEQLTLGY--GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVLFND-TIANNIRYGRV----------TAGDSEIQAAAQAAGIHDAILsfpEGYETqvgerglkLSGGEKQRVA 736
Cdd:PRK10253 85 LLAQNATTPGDiTVQELVARGRYphqplftrwrKEDEEAVTKAMQATGITHLAD---QSVDT--------LSGGQRQRAW 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQASLAKVctNR----TTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL--NRekgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
602-810 |
1.70e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQiSLRSHIGVVPQD----TVL 675
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRD-AIRAGIAYVPEDrkgeGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 676 FNDTIANNI---RYGRVTAGdseiqaaaqaaGI--HDAILSFPEGY-----------ETQVGErglkLSGGEKQRVAIAR 739
Cdd:COG1129 343 LDLSIRENItlaSLDRLSRG-----------GLldRRRERALAEEYikrlriktpspEQPVGN----LSGGNQQKVVLAK 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 740 TILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAhrlST----VV-NADQILVIKDGCII-ERGRHEA 810
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpeLLgLSDRILVMREGRIVgELDREEA 481
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
604-806 |
2.09e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.20 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFY--DISSGC-IRIDGQDISQVTQISL-----RSHIGVVPQDTVL 675
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREGRLARdirksRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 676 FND-TIANNIRYGRV--TAGDSEIQAAAQAAGIHDAILSFpegyeTQVG------ERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:PRK09984 98 VNRlSVLENVLIGALgsTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 747 IILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHVFYDG 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
606-760 |
2.09e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI---SLRSHIGVVPQDTVLFNDTian 682
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYASLDP--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 683 nirygRVTAGDSeIQAAAQAAGIHDAilsfpEGYETQVG---ER-GLK----------LSGGEKQRVAIARTILKAPDII 748
Cdd:PRK10261 417 -----RQTVGDS-IMEPLRVHGLLPG-----KAAAARVAwllERvGLLpehawrypheFSGGQRQRICIARALALNPKVI 485
|
170
....*....|..
gi 18034785 749 LLDEATSALDTS 760
Cdd:PRK10261 486 IADEAVSALDVS 497
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
320-554 |
2.98e-13 |
|
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: 71.39 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 320 TGSTGFVSNLRTFLWIRV-QQFTSRgVELRLFSHLHELSLRWHLGRRTGEVLRivdRGTSSVTGLLSYLVFNIIPTLADI 398
Cdd:cd18564 64 ALLRGLASYAGTYLTALVgQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLS---RLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 399 IIGIIYFS-MFFNAW-FGLIVFLCMSLYLILTimvtewrAKFRRDMNTQENATR-------ARAVDSLLNFETVKYYNAE 469
Cdd:cd18564 140 LTLVGMLGvMFWLDWqLALIALAVAPLLLLAA-------RRFSRRIKEASREQRrregalaSVAQESLSAIRVVQAFGRE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 470 GYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGT 549
Cdd:cd18564 213 EHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAK 292
|
....*
gi 18034785 550 YYRMI 554
Cdd:cd18564 293 LTGRI 297
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
590-814 |
4.55e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL--FRFYDISSG-----------CIRIDGQdiSQ 656
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekCGYVERP--SK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 657 VTQISLRSHIGVVPQDTVLFN--DTIANNIR------YGRVTA--GDSEIqaaaqaagIHDAILSFPE-GYE-------- 717
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWNlsDKLRRRIRkriaimLQRTFAlyGDDTV--------LDNVLEALEEiGYEgkeavgra 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 718 ------TQVGER----GLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAK-VCTNRTTIVVAHRLS 786
Cdd:TIGR03269 150 vdliemVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|
gi 18034785 787 TVVN--ADQILVIKDGCIIERGRHEALLSR 814
Cdd:TIGR03269 230 EVIEdlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
598-758 |
5.04e-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: 72.66 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 598 SYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQISLRSHIGVVPQDTVL-F 676
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KDFNGEARPQPGIKVGYLPQEPQLdP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 677 NDTIANNI------------RYGRVTAG----DSEIQAAAQAAG-IHDAI------------------LSFPEGyETQVG 721
Cdd:TIGR03719 82 TKTVRENVeegvaeikdaldRFNEISAKyaepDADFDKLAAEQAeLQEIIdaadawdldsqleiamdaLRCPPW-DADVT 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 18034785 722 erglKLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:TIGR03719 161 ----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
589-752 |
7.76e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.93 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLFNDTIAnniryGRVTAGDSEIQAAAQaagihdAILSFPEGYETQVGE-RGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK10522 402 VFTDFHLFDQLLG-----PEGKPANPALVEKWL------ERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470
|
....*
gi 18034785 748 ILLDE 752
Cdd:PRK10522 471 LLLDE 475
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
603-800 |
8.15e-13 |
|
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: 67.65 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS--SGCIRIDGQDIsqvtQISLRSHIGVVPQdtvlfNDti 680
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQRSTGYVEQ-----QD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 annirygrvtagdseiqaaaqaagIHDAILSFPEGYETQVGERGLKLSggEKQRVAIARTILKAPDIILLDEATSALDTs 760
Cdd:cd03232 89 ------------------------VHSPNLTVREALRFSALLRGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDS- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18034785 761 neraiQASLAKVC-------TNRTTIVVAHRLSTVV--NADQILVIKDG 800
Cdd:cd03232 142 -----QAAYNIVRflkkladSGQAILCTIHQPSASIfeKFDRLLLLKRG 185
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
329-533 |
9.12e-13 |
|
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: 69.78 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 329 LRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RIVDrgTSSVTGLLSYLVFN-IIPTLADIIIGIIYFs 406
Cdd:cd18570 61 IRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIIsRFND--ANKIREAISSTTISlFLDLLMVIISGIILF- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 407 mFFNAWFGLIVFLCMSLYLILTIMVTE-WRAKFRRDMntQENA-TRARAVDSLLNFETVKYYNAEGYELERYREAILKFQ 484
Cdd:cd18570 138 -FYNWKLFLITLLIIPLYILIILLFNKpFKKKNREVM--ESNAeLNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLL 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18034785 485 glewKSTASLVLLNQTQNMVIGFGLLAGSLL----CAYFVSERRLQVGDFVLF 533
Cdd:cd18570 215 ----KKSFKLGKLSNLQSSIKGLISLIGSLLilwiGSYLVIKGQLSLGQLIAF 263
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
602-803 |
1.98e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQISLRSHIGVVPQDTVLF-NDT 679
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIpQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 680 IANNIRYGRvtagdsEIqaaAQAAGIHD------------AILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK10762 96 IAENIFLGR------EF---VNRFGRIDwkkmyaeadkllARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 748 ILLDEATSAL-DTSNEraiqaSLAKVCT-----NRTTIVVAHRLSTVVN-ADQILVIKDGCII 803
Cdd:PRK10762 163 IIMDEPTDALtDTETE-----SLFRVIRelksqGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
277-556 |
2.03e-12 |
|
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: 68.72 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 277 ALNVLVPIFYRDIVNLLT-SKAPWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNlrtflwiRVQQFTSRGVELRLFSHLHE 355
Cdd:cd18778 13 LLGLVPPWLIRELVDLVTiGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNH-------VAEQKVVADLRSDLYDKLQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 356 LSLRWHLGRRTGEVL-RIVDrGTSSVTGLLSYLVFNIIPT-LADIIIGIIYFSMffNAWFGLIVFLCMSLYLILTIMVTE 433
Cdd:cd18778 86 LSLRYFDDRQTGDLMsRVIN-DVANVERLIADGIPQGITNvLTLVGVAIILFSI--NPKLALLTLIPIPFLALGAWLYSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 434 W-RAKFRR------DMNtqenatrARAVDSLLNFETVKYYNAEGYELER-------YREAILK--------FQGLEWKST 491
Cdd:cd18778 163 KvRPRYRKvrealgELN-------ALLQDNLSGIREIQAFGREEEEAKRfealsrrYRKAQLRamklwaifHPLMEFLTS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 492 ASLVLlnqtqnmVIGFGllagsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQT 556
Cdd:cd18778 236 LGTVL-------VLGFG--------GRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQR 285
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
591-758 |
2.45e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfydissgciridgqdISQVTQISLRSHIG--- 667
Cdd:PRK11147 321 EMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM-----------------LGQLQADSGRIHCGtkl 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 -----------VVPQDTVLFNdtiannirygrVTAGDSEIqaaaQAAGIHDAILSF-------PEGYETQVGerglKLSG 729
Cdd:PRK11147 383 evayfdqhraeLDPEKTVMDN-----------LAEGKQEV----MVNGRPRHVLGYlqdflfhPKRAMTPVK----ALSG 443
|
170 180
....*....|....*....|....*....
gi 18034785 730 GEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
604-806 |
2.66e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDG-------------------QDISqvTQISLRS 664
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqrirmifQDPS--TSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 665 HIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAaaqaagIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKA 744
Cdd:PRK15112 105 RISQILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPDHASYYPH-----------MLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 745 PDIILLDEATSALDTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDGCIIERG 806
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
590-769 |
2.73e-12 |
|
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: 70.35 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQislrSHIGV 668
Cdd:TIGR03719 323 IEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ----SRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 VPQDTVLfnDTIANNIRYGRVtaGDSEIQAAaqaagihdAILS---FpEGYETQ--VGErglkLSGGEKQRVAIARTILK 743
Cdd:TIGR03719 398 DPNKTVW--EEISGGLDIIKL--GKREIPSR--------AYVGrfnF-KGSDQQkkVGQ----LSGGERNRVHLAKTLKS 460
|
170 180
....*....|....*....|....*.
gi 18034785 744 APDIILLDEATSALDTSNERAIQASL 769
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
263-561 |
3.53e-12 |
|
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: 67.86 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 263 LTVLLCMGLMGldrALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQgggTGSTGFVSNLRTFLWIRVQQFTS 342
Cdd:cd18549 5 FLDLFCAVLIA---ALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILR---TLLNYFVTYWGHVMGARIETDMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 343 RgvelRLFSHLHELSLRWHLGRRTGEVL-RIV-DrgTSSVTGLLSY----LVFNIIptladIIIGIIYFSMFFNAWFGLI 416
Cdd:cd18549 79 R----DLFEHLQKLSFSFFDNNKTGQLMsRITnD--LFDISELAHHgpedLFISII-----TIIGSFIILLTINVPLTLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 417 VFLCMSLYLILTImvtewraKFRRDMNTQENATR-------ARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWK 489
Cdd:cd18549 148 VFALLPLMIIFTI-------YFNKKMKKAFRRVRekigeinAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 490 S-------TASLVLLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNwfgtyyRMIqtNFIDM 561
Cdd:cd18549 221 AykamayfFSGMNFFTNLLNLVV---LVAG----GYFIIKGEITLGDLVAFLLYVNVFIKPIR------RLV--NFTEQ 284
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
606-807 |
7.67e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLfRFYDIS----SGCIRIDGQ--DISQVTQISlrshiGVVPQD------- 672
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMpiDAKEMRAIS-----AYVQQDdlfiptl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TVLFNDTIANNIRYGRVTAGDSEIQAaaqaagIHDAI--LSFPEGYETQVGERGLK--LSGGEKQRVAIARTILKAPDII 748
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRER------VDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18034785 749 LLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVV--NADQILVIKDGCIIERGR 807
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELfeLFDKIILMAEGRVAYLGS 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
590-802 |
1.02e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSH---I 666
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHqlgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQDTVLF-NDTIANNIRYG--RVTAGDSEIQAAAQAAGIHdaiLSFpegyETQVGerglKLSGGEKQRVAIARTILK 743
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDL----DSSAG----SLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 744 APDIILLDEATSAL---DTSNE-RAIQASLAKvctnRTTIV-VAHRLSTVVN-ADQILVIKDGCI 802
Cdd:PRK15439 158 DSRILILDEPTASLtpaETERLfSRIRELLAQ----GVGIVfISHKLPEIRQlADRISVMRDGTI 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
615-787 |
1.28e-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: 63.16 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 615 PGQTVALVGPSGAGKSTILRLLFRFYDISS-GCIRIDGQDISQVTQISLRshigvvpqdtvlfndtiannirygrvtagd 693
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 694 seiqaaaqaagihdailsfpegyETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASL---- 769
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
|
170 180
....*....|....*....|.
gi 18034785 770 ---AKVCTNRTTIVVAHRLST 787
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKD 128
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
266-555 |
1.67e-11 |
|
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: 65.91 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 266 LLCMGLMGldrALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTgstgFVSNlrtFLWIRVQQFTSRGV 345
Cdd:cd18552 5 ILGMILVA---ATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLAS----YLQT---YLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 346 ELRLFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNIIptladIIIGIIYFSMFFNAWFGLIVFLCM 421
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDRNSSGDLIsRItndVNQVQNALTSALTVLVRDPL-----TVIGLLGVLFYLDWKLTLIALVVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 422 SLYLILTIMVTEwraKFRRDM-NTQENATR--ARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLN 498
Cdd:cd18552 150 PLAALPIRRIGK---RLRKISrRSQESMGDltSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 499 QTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:cd18552 227 PLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQ 283
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
591-806 |
1.86e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 591 EFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTQiSLRSHIGV 668
Cdd:CHL00131 9 EIKNLHAS-VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEP-EERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 669 ------------VPQDTVLfndTIANNIRygRVTAGDSEIqaaaqaagihDAiLSFPEGYETQVGERGLK---------- 726
Cdd:CHL00131 87 flafqypieipgVSNADFL---RLAYNSK--RKFQGLPEL----------DP-LEFLEIINEKLKLVGMDpsflsrnvne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 727 -LSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIV-VAH--RLSTVVNADQILVIKDGCI 802
Cdd:CHL00131 151 gFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKI 230
|
....
gi 18034785 803 IERG 806
Cdd:CHL00131 231 IKTG 234
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
268-555 |
2.66e-11 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 65.20 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRGVEL 347
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQA-------VFSFFRIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 348 RLFSHLHELSLRWHLGRRTGEVL-RIvdrgTSSVTGLLSYLVFNI---IPTLADIIIGIIYfsMFFNAW-FGLIVFLCMS 422
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTsRL----SNDVTQIQDTLTTTLaefLRQILTLIGGVVL--LFFISWkLTLLMLATVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 423 LYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQtqn 502
Cdd:cd18576 148 VVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSS--- 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 503 mVIGFGLLAGSLLCAYF----VSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:cd18576 225 -FIIFLLFGAIVAVLWYggrlVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQ 280
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
277-544 |
3.32e-11 |
|
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: 65.13 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 277 ALNVLVPIFYRDIVNLLTSK-APWSSLAWTVTTYVFLKFLQGGGTgstgfvsnlrtFLWiRVQQF-TSRGVE--LR--LF 350
Cdd:cd18541 13 LLQLLIPRIIGRAIDALTAGtLTASQLLRYALLILLLALLIGIFR-----------FLW-RYLIFgASRRIEydLRndLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 351 SHLHELSLRWHLGRRTGEvlrIVDRGTSSVTGLLSYLVFNIIpTLADII---IGIIYFSMFFNAWFGLIVFLCMslyLIL 427
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGD---LMARATNDLNAVRMALGPGIL-YLVDALflgVLVLVMMFTISPKLTLIALLPL---PLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 428 TIMVTEW----RAKFRR------DMN--TQENATRARavdsllnfeTVKYYNAEGYELERYREAILKFQglewKSTASLV 495
Cdd:cd18541 154 ALLVYRLgkkiHKRFRKvqeafsDLSdrVQESFSGIR---------VIKAFVQEEAEIERFDKLNEEYV----EKNLRLA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 18034785 496 ----LLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18541 221 rvdaLFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPM 273
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
609-811 |
3.50e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 609 VSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----IGVVP--QDTVLFND-TIA 681
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-----GLPGHqiarMGVVRtfQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 NNI---RYGRVTAgdseiqaaaqaaGIHDAILSFPeGY---ETQVGER--------GLK---------LSGGEKQRVAIA 738
Cdd:PRK11300 99 ENLlvaQHQQLKT------------GLFSGLLKTP-AFrraESEALDRaatwlervGLLehanrqagnLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 739 RTILKAPDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEAL 811
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
277-545 |
4.30e-11 |
|
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: 64.73 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 277 ALNVLVPIFYRDIVNLLTSKAP------WSSLAWTVTTYVFLKFLqgggtgstGFVSN-LRTFLWIRVQQFTSRgvELR- 348
Cdd:cd18547 13 LLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLLGLYLL--------SALFSyLQNRLMARVSQRTVY--DLRk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 349 -LFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNIIptladIIIGIIYFsMFF-NAWFGLIVFLCMS 422
Cdd:cd18547 83 dLFEKLQRLPLSYFDTHSHGDIMsRVtndVDNISQALSQSLTQLISSIL-----TIVGTLIM-MLYiSPLLTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 423 LYLILTIMVTEW-RAKFRR------DMN--TQENATraravdsllNFETVKYYNAEGYELERYREAILKFQGLEWKSTAS 493
Cdd:cd18547 157 LSLLVTKFIAKRsQKYFRKqqkalgELNgyIEEMIS---------GQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 18034785 494 LVLLNQTQNMV--IGFGLLAgsLLCAYFVSERRLQVGDFVLFGTYITQLYMPLN 545
Cdd:cd18547 228 SGLLMPIMNFInnLGYVLVA--VVGGLLVINGALTVGVIQAFLQYSRQFSQPIN 279
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
609-813 |
5.62e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 609 VSFTVMPGQTVALVGPSGAGKSTilrLLFRFYDI--SSGCIRIDGQDISQVTQISLRSHIG-VVPQDTVLFNDTIannIR 685
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPV---FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 686 Y--------GRVTAGDSEIQAAAQAAGIHDAIlsfpegyETQVGErglkLSGGEKQRVAIARTILK-APDI------ILL 750
Cdd:PRK03695 89 YltlhqpdkTRTEAVASALNEVAEALGLDDKL-------GRSVNQ----LSGGEWQRVRLAAVVLQvWPDInpagqlLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 751 DEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLS-TVVNADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
597-783 |
6.56e-11 |
|
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: 63.58 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 597 FSYADGRETLQDVSFTVMPG-----QTVALVGPSGAGKSTILRLLfrfydisSGCIRIDGQDISqvtqislrshigvvpq 671
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIE---------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 dtvLFNDTIANNIRY------GRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03237 58 ---IELDTVSYKPQYikadyeGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18034785 746 DIILLDEATSALDtSNERAIQASLAK---VCTNRTTIVVAH 783
Cdd:cd03237 135 DIYLLDEPSAYLD-VEQRLMASKVIRrfaENNEKTAFVVEH 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
589-810 |
1.07e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ--VTQIsLRSHI 666
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsPRER-RRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 667 GVVPQD-----TVLfNDTIANNI---RYGRvtagdseiqAAAQAAGIHD--AILSF-----------PEGYETQVGergl 725
Cdd:COG3845 336 AYIPEDrlgrgLVP-DMSVAENLilgRYRR---------PPFSRGGFLDrkAIRAFaeelieefdvrTPGPDTPAR---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 726 KLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTI-VVAHRLSTVVN-ADQILVIKDGCII 803
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVlLISEDLDEILAlSDRIAVMYEGRIV 481
|
....*...
gi 18034785 804 -ERGRHEA 810
Cdd:COG3845 482 gEVPAAEA 489
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
269-551 |
1.37e-10 |
|
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: 62.95 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 269 MGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLqgggtgsTGFVSNLRTFLWIRVQQFTSRGVELR 348
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVL-------SGLFSGLRGGCFSYAGTRLVRRLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 349 LFSHLHELSLRWHLGRRTGEvlrIVDRGTS---SVTGLLSYLVFNIIPTLADIIIGIIYfsMFFNAWF-GLIVFLCMsly 424
Cdd:cd18572 75 LFRSLLRQDIAFFDATKTGE---LTSRLTSdcqKVSDPLSTNLNVFLRNLVQLVGGLAF--MFSLSWRlTLLAFITV--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 425 lILTIMVTEWRAKFRRDMNTQENATRAR----AVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKStASLVLLNQT 500
Cdd:cd18572 147 -PVIALITKVYGRYYRKLSKEIQDALAEanqvAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQ-ALAYAGYVA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 501 QNMVIGFGLLAGSLL-CAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYY 551
Cdd:cd18572 225 VNTLLQNGTQVLVLFyGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVF 276
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
601-806 |
1.55e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS--------SGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TV-LFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPeGYETQVGERGLKLSGGEKQRVAIARTILK-------- 743
Cdd:PRK13547 92 AQpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 744 -APDIILLDEATSALDTSNERAIQASLAKVCT--NRTTIVVAHRLSTVV-NADQILVIKDGCIIERG 806
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHG 237
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
603-811 |
1.79e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF-RFYDIS-SGCIRIDGQDISQvtQISLRshIGVVPQDTVLF---- 676
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK--QILKR--TGFVTQDDILYphlt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 677 -NDTI--ANNIRYGRVTAGDSEIQAAAQAAgihdAILSFPEGYETQVGERGLK-LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PLN03211 157 vRETLvfCSLLRLPKSLTKQEKILVAESVI----SELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 753 ATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVNA--DQILVIKDG-CIIERGRHEAL 811
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSRVYQmfDSVLVLSEGrCLFFGKGSDAM 295
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
263-558 |
2.14e-10 |
|
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: 62.49 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 263 LTVLLCMGLMGldrALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQgggtgstgFVSNlrtFLWIRVQQFTS 342
Cdd:cd18545 3 LLALLLMLLST---AASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVN--------WVAS---RLRIYLMAKVG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 343 RGV--ELR--LFSHLHELSLRWHLGRRTGEVL-RIV-DrgTSSVTGLLSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLI 416
Cdd:cd18545 69 QRIlyDLRqdLFSHLQKLSFSFFDSRPVGKILsRVInD--VNSLSDLLSNGLINLIPDLL-TLVGIVIIMFSLNVRLALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 417 VFLCMSLyLILTIMVTEWRAK--FRR------DMNT--QENATRARavdsllnfeTVKYYNAEGYELERYREAILKFQGl 486
Cdd:cd18545 146 TLAVLPL-LVLVVFLLRRRARkaWQRvrkkisNLNAylHESISGIR---------VIQSFAREDENEEIFDELNRENRK- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 487 EWKSTASLV-LLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNF 558
Cdd:cd18545 215 ANMRAVRLNaLFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAM 287
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
599-758 |
2.39e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 599 YADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQISLRSHIGVVPQD------ 672
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KEFEGEARPAPGIKVGYLPQEpqldpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 -TVLFN------DTIANNIRYGRVTAG------------------------------DSEIQAAAqaagihDAiLSFPEG 715
Cdd:PRK11819 85 kTVRENveegvaEVKAALDRFNEIYAAyaepdadfdalaaeqgelqeiidaadawdlDSQLEIAM------DA-LRCPPW 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18034785 716 yETQVGerglKLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:PRK11819 158 -DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
594-776 |
2.62e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 594 NVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-----VTQISLRSH-IG 667
Cdd:PRK13540 6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyQKQLCFVGHrSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPqdtvlfNDTIANNIRYG-RVTAGDSEIQAAAQAAGIhDAILSFPEGYetqvgerglkLSGGEKQRVAIARTILKAPD 746
Cdd:PRK13540 85 INP------YLTLRENCLYDiHFSPGAVGITELCRLFSL-EHLIDYPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|
gi 18034785 747 IILLDEATSALDtsnERAIQASLAKVCTNR 776
Cdd:PRK13540 148 LWLLDEPLVALD---ELSLLTIITKIQEHR 174
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
601-800 |
4.51e-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: 62.92 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDI-SQVTQISLRSHIGVVPQDTVLFN 677
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 678 D-TIANNIRYG-RVTAGDSEIQAAAQAAGIHDAI--LSFPEGYETQ-VGERGlklsGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR02633 92 ElSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLreLQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18034785 753 ATSALdTSNERAIQASLAKVCTNR--TTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
594-809 |
5.13e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 594 NVHFSYADGR-ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCI------------------------- 647
Cdd:PRK10261 19 NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 648 -RIDGQDISQVTQISLRSHIGVVPqdtvlFNDTIANNIRYGRVTAGDSEIQAAAQAAgihdAILSFPEGyETQVGERGLK 726
Cdd:PRK10261 99 rHVRGADMAMIFQEPMTSLNPVFT-----VGEQIAESIRLHQGASREEAMVEAKRML----DQVRIPEA-QTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 727 LSGGEKQRVAIARTILKAPDIILLDEATSALDTSneraIQA---SLAKVCTNRTT---IVVAHRLSTVVN-ADQILVIKD 799
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVT----IQAqilQLIKVLQKEMSmgvIFITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|
gi 18034785 800 GCIIERGRHE 809
Cdd:PRK10261 245 GEAVETGSVE 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
584-783 |
5.19e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 584 RFHKGRVEFE----------NVHFSYADGRETLQDVSFTVMPGQ-----TVALVGPSGAGKSTILRLLfrfydisSGCIR 648
Cdd:PRK13409 318 RIRPEPIEFEerpprdeserETLVEYPDLTKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLL-------AGVLK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 649 IDGQDISQVTQISLR-SHIGVVPQDTV-LFNDTIANNIrygrvtaGDS----EIQAAaqaagihdaiLSFPEGYETQVGE 722
Cdd:PRK13409 391 PDEGEVDPELKISYKpQYIKPDYDGTVeDLLRSITDDL-------GSSyyksEIIKP----------LQLERLLDKNVKD 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 723 rglkLSGGEKQRVAIARTILKAPDIILLDEATSALDtSNERAIQAS-LAKVCTNR--TTIVVAH 783
Cdd:PRK13409 454 ----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRLAVAKaIRRIAEEReaTALVVDH 512
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
605-800 |
7.48e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 605 TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-------------VTQisLRSHIGVVPQ 671
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTE--ERRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLD 751
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18034785 752 EATSALDTSNERAIQ---ASLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:PRK10982 417 EPTRGIDVGAKFEIYqliAELAK--KDKGIIIISSEMPELLGiTDRILVMSNG 467
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
582-783 |
8.27e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 582 PLRFHK---GRVEFENVHFSYADGRETLQDVSFTVMPGQ-----TVALVGPSGAGKSTILRLLfrfydisSGCIRIDGQD 653
Cdd:COG1245 324 PIEFEVhapRREKEEETLVEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 654 ISQVTQISLRshigvvPQ----DtvlFNDTIANNIRYGRVTAGDSeiqaaaqaagihdailSFpegYETQVGER-GLK-- 726
Cdd:COG1245 397 VDEDLKISYK------PQyispD---YDGTVEEFLRSANTDDFGS----------------SY---YKTEIIKPlGLEkl 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 727 -------LSGGEKQRVAIARTILKAPDIILLDEATSALDtSNERaiqASLAKVC------TNRTTIVVAH 783
Cdd:COG1245 449 ldknvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQR---LAVAKAIrrfaenRGKTAMVVDH 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
590-769 |
9.95e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQ--DISQVTQislrSHIG 667
Cdd:PRK11819 325 IEAENLSKSFGD-RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVDQ----SRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 VVPQDTVlF------NDTIannirygrvTAGDSEIQAAaqaagihdAILS---FpEGYETQ--VGErglkLSGGEKQRVA 736
Cdd:PRK11819 399 LDPNKTV-WeeisggLDII---------KVGNREIPSR--------AYVGrfnF-KGGDQQkkVGV----LSGGERNRLH 455
|
170 180 190
....*....|....*....|....*....|...
gi 18034785 737 IARTILKAPDIILLDEATSALDTSNERAIQASL 769
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVETLRALEEAL 488
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
277-548 |
1.32e-09 |
|
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: 60.19 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 277 ALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTGstgfvsnLRTFLWIRVQQFTSRGVELRLFSHLHEL 356
Cdd:cd18543 13 LAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSF-------LRRYLAGRLSLGVEHDLRTDLFAHLQRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 357 SLRWHLGRRTGEVLrivDRGTS---SVTGLLSYLVFNIIPTLADIIIGIIYFSMffNAWFGLIVFLCMSLYLILTimvte 433
Cdd:cd18543 86 DGAFHDRWQSGQLL---SRATSdlsLVQRFLAFGPFLLGNLLTLVVGLVVMLVL--SPPLALVALASLPPLVLVA----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 434 wrAKFRRDMNT------QENATRARAVD-SLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIG 506
Cdd:cd18543 156 --RRFRRRYFPasrraqDQAGDLATVVEeSVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 18034785 507 FGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFG 548
Cdd:cd18543 234 LGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
590-808 |
2.59e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDISQVTQiSLRSHIG 667
Cdd:PRK09580 2 LSIKDLHVS-VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSP-EDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 668 V---------VPQ-DTVLFNDTIANNIRYGRvtaGDSEIQAAAQAAGIHDAI--LSFPEGYETQVGERGlkLSGGEKQRV 735
Cdd:PRK09580 80 IfmafqypveIPGvSNQFFLQTALNAVRSYR---GQEPLDRFDFQDLMEEKIalLKMPEDLLTRSVNVG--FSGGEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 736 AIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCT-NRTTIVVAH--RLSTVVNADQILVIKDGCIIERGRH 808
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
600-803 |
2.92e-09 |
|
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: 57.66 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 600 ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQDISQVTQIslrshigvvPQDTVLF 676
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEK---------YPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 677 NdtiannirygrvTAGDseiqaaaqaagIHDAILSFPEGYETQVGERG----LKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03233 88 V------------SEED-----------VHFPTLTVRETLDFALRCKGnefvRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 753 ATSALDTSNerAIQ-ASLAKVCTNRTtivvahRLSTVVNA-----------DQILVIKDGCII 803
Cdd:cd03233 145 STRGLDSST--ALEiLKCIRTMADVL------KTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
612-785 |
3.86e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 612 TVMPGQTVALVGPSGAGKSTILRLLfrfydisSGCIRIDgqdisqvtqisLRSHIGVVPQDTVL-----------FNDTI 680
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKIL-------SGELIPN-----------LGDYEEEPSWDEVLkrfrgtelqnyFKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 681 ANNIR------Y---------GRVtagdSEIQAAAQAAGIHDAILSFPEgyETQVGERGLK-LSGGEKQRVAIARTILKA 744
Cdd:PRK13409 157 NGEIKvvhkpqYvdlipkvfkGKV----RELLKKVDERGKLDEVVERLG--LENILDRDISeLSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18034785 745 PDIILLDEATSALDTsNER-----AIQaSLAKvctNRTTIVVAHRL 785
Cdd:PRK13409 231 ADFYFFDEPTSYLDI-RQRlnvarLIR-ELAE---GKYVLVVEHDL 271
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
606-804 |
4.32e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQ-----DISQvtqiSLRSHIGVVPQDTVLFND 678
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD----SEALGIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 679 -TIANNIRYGRVTAgdseiqaaaqAAGIHD------------AILSFPEGYETQVGERGLklsgGEKQRVAIARTILKAP 745
Cdd:NF040905 93 lSIAENIFLGNERA----------KRGVIDwnetnrrarellAKVGLDESPDTLVTDIGV----GKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 746 DIILLDEATSALdtsNERAIQASLAKVCTNR----TTIVVAHRLSTVVN-ADQILVIKDGCIIE 804
Cdd:NF040905 159 KLLILDEPTAAL---NEEDSAALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
589-814 |
4.33e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYAdgRETLQDVSFTVMPGQTVALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVtqiSLRS 664
Cdd:PRK10418 4 QIELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPC---ALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 665 -HIGVVPQDT-VLFN--DTIANNIR-----YGRvTAGDSEIQAAAQAAGIHDAilsfpegyetqvgERGLKL-----SGG 730
Cdd:PRK10418 79 rKIATIMQNPrSAFNplHTMHTHARetclaLGK-PADDATLTAALEAVGLENA-------------ARVLKLypfemSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 731 EKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRT--TIVVAHRLSTVVN-ADQILVIKDGCIIERGR 807
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGD 224
|
....*..
gi 18034785 808 HEALLSR 814
Cdd:PRK10418 225 VETLFNA 231
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
265-545 |
5.08e-09 |
|
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: 58.26 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGgtgstgfVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASAL-------LGVVQTYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 345 VELRLFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNIIPTLADIIIgiiyfsMFFNAW-FGLIVFL 419
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQsRLnndVGGAQSVVTGTLTSVVSNVVTLVATLVA------MLALDWrLALLSLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 420 CMSLYLILTIMVTEWRAKFRRDmnTQE-NATRARAVDSLLN---FETVKYYNAEGYELERYREAILKFQGLEWKStaslV 495
Cdd:cd18550 148 LLPLFVLPTRRVGRRRRKLTRE--QQEkLAELNSIMQETLSvsgALLVKLFGREDDEAARFARRSRELRDLGVRQ----A 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 18034785 496 LLNQTQNMVIGFGLLAGS----LLCAYFVSERRLQVGDFVLFGTYITQLYMPLN 545
Cdd:cd18550 222 LAGRWFFAALGLFTAIGPalvyWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLT 275
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
594-807 |
9.64e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.81 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 594 NVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKS----TILRLLFRFYDISsGCIRIDGQDISQVTQISL---RSH 665
Cdd:PRK09473 19 RVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLPEKELnklRAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 666 igvvpQDTVLFNDTIANNIRYGRVTAGDSEIQAaaqaagIHDAiLSFPEGYETQVgeRGL-----------------KLS 728
Cdd:PRK09473 98 -----QISMIFQDPMTSLNPYMRVGEQLMEVLM------LHKG-MSKAEAFEESV--RMLdavkmpearkrmkmyphEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 729 GGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASL--AKVCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIER 805
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEY 243
|
..
gi 18034785 806 GR 807
Cdd:PRK09473 244 GN 245
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
583-817 |
9.78e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 583 LRF------HKGRVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIridgqdisq 656
Cdd:PRK15064 307 IRFeqdkklHRNALEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 657 vtQISLRSHIGVVPQDTV--LFND-TIANNIRYGRvTAGDSEiqaaAQAAGIHDAILsFPegyETQVGERGLKLSGGEKQ 733
Cdd:PRK15064 377 --KWSENANIGYYAQDHAydFENDlTLFDWMSQWR-QEGDDE----QAVRGTLGRLL-FS---QDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 734 RVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVctNRTTIVVAHRLSTVVN-ADQILVIKDGCIIE-RGRHEAL 811
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EGTLIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEY 523
|
....*.
gi 18034785 812 LSRGGV 817
Cdd:PRK15064 524 LRSQGI 529
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
263-556 |
1.03e-08 |
|
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: 57.44 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 263 LTVLLCMGLMGldRALNVLVPIFYRDIVNLLTSKAP-WSSLAWTVTTYVFLKFLQGGGT---GSTG--FVSNLRTflwir 336
Cdd:cd18551 1 LILALLLSLLG--TAASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSyllGRTGerVVLDLRR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 337 vqqftsrgvelRLFSHLHELSLRWHLGRRTGEVL-RIVdrgtsSVTGLLSYLVFNIIPTLAD---IIIGIIYFSMFFNAW 412
Cdd:cd18551 74 -----------RLWRRLLRLPVSFFDRRRSGDLVsRVT-----NDTTLLRELITSGLPQLVTgvlTVVGAVVLMFLLDWV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 413 FGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTA 492
Cdd:cd18551 138 LTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAK 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 493 SLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQT 556
Cdd:cd18551 218 IEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQK 281
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
609-813 |
1.44e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 609 VSFTVMPGQTVALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG----VVPQD-------- 672
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDpmtslnpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 -TVLFNDTIANNIRYG--RVTAGDSEIQAAAQAaGIHDAIlSFPEGYETQvgerglkLSGGEKQRVAIARTILKAPDIIL 749
Cdd:PRK11022 106 yTVGFQIMEAIKVHQGgnKKTRRQRAIDLLNQV-GIPDPA-SRLDVYPHQ-------LSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18034785 750 LDEATSALDTSneraIQASLAKVC------TNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGRHEALLS 813
Cdd:PRK11022 177 ADEPTTALDVT----IQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
277-538 |
2.20e-08 |
|
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: 56.41 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 277 ALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRGVELRLFSHLHEL 356
Cdd:cd18557 10 AAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQS-------VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 357 SLRWHLGRRTGEvlrIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYF-SMFFNAW-FGLIVFLCMSLYLILTIMVTEW 434
Cdd:cd18557 83 EIAFFDKHKTGE---LTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLiILFILSWkLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 435 RAKFRRDMntQENATRARAV--DSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAG 512
Cdd:cd18557 160 IRKLSKEV--QDALAKAGQVaeESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260
....*....|....*....|....*....
gi 18034785 513 SLLCAYFVSERRLQVGD---FVLFGTYIT 538
Cdd:cd18557 238 LWYGGYLVLSGQLTVGEltsFILYTIMVA 266
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
552-804 |
3.04e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 552 RMIQTNFIDMENMFDLLKEET--EVKDVpgagpLRFHKGRVefenvhfsyadgretlQDVSFTVMPGQTVALVGPSGAGK 629
Cdd:PRK09700 244 RELQNRFNAMKENVSNLAHETvfEVRNV-----TSRDRKKV----------------RDISFSVCRGEILGFAGLVGSGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 630 STILRLLFRFYDISSGCIRIDGQDISQVTQ-ISLRSHIGVVPQ---DTVLF-NDTIANNIrygrvtagdsEIQAAAQAAG 704
Cdd:PRK09700 303 TELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSIAQNM----------AISRSLKDGG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 705 IHDAILSFPEGYETQVGERGLK---------------LSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASL 769
Cdd:PRK09700 373 YKGAMGLFHEVDEQRTAENQREllalkchsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVM 452
|
250 260 270
....*....|....*....|....*....|....*..
gi 18034785 770 AKVCTN-RTTIVVAHRLSTVVNA-DQILVIKDGCIIE 804
Cdd:PRK09700 453 RQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
615-787 |
3.05e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 615 PGQTVALVGPSGAGKSTILRLL-----------------------FR-------FYDISSGCIRIdGQDISQVTQISlRS 664
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlkrFRgtelqdyFKKLANGEIKV-AHKPQYVDLIP-KV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 665 HIGVVpqdtvlfndtiannirygrvtagdSEIQAAAQAAGIHDAILSFPEgyETQVGERGLK-LSGGEKQRVAIARTILK 743
Cdd:COG1245 176 FKGTV------------------------RELLEKVDERGKLDELAEKLG--LENILDRDISeLSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18034785 744 APDIILLDEATSALDTsNER-----AIQaSLAKvcTNRTTIVVAHRLST 787
Cdd:COG1245 230 DADFYFFDEPSSYLDI-YQRlnvarLIR-ELAE--EGKYVLVVEHDLAI 274
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
597-828 |
3.22e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 597 FSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQISLRSHIGVVPQDTv 674
Cdd:PRK13638 9 FRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 675 lfndtiANNIRYgrvTAGDSEIQAAAQAAGIHDA-ILSFPEGYETQVGERGLK------LSGGEKQRVAIARTILKAPDI 747
Cdd:PRK13638 87 ------EQQIFY---TDIDSDIAFSLRNLGVPEAeITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 748 ILLDEATSALDTSNERAIQASLAK-VCTNRTTIVVAHRLSTVVN-ADQILVIKDGCIIERGrheallSRGGVYAEMWQLQ 825
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG------APGEVFACTEAME 231
|
...
gi 18034785 826 QQG 828
Cdd:PRK13638 232 QAG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
603-800 |
4.80e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-SGCIRIDGQDISQVT-QISLRSHIGVVPQDT------- 673
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgivp 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 674 ---VLFNDTIANNIRYGRVTAGDSEIQAaaqaagihDAILSFPEGYETQVGERGL---KLSGGEKQRVAIARTILKAPDI 747
Cdd:TIGR02633 353 ilgVGKNITLSVLKSFCFKMRIDAAAEL--------QIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 748 ILLDEATSALDTSNERAIQASLAKVCTNRTT-IVVAHRLSTVVN-ADQILVIKDG 800
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEG 479
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
348-544 |
5.22e-08 |
|
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: 55.50 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIiptLADIIIGIIYFS-MFFnawfgLIVFLCMSLYLI 426
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNI---WLDMITIIIAICiMLV-----LNPKLTFVSLVI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 427 LTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFE------TVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQT 500
Cdd:cd18554 156 FPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHEriqgmsVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSA 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18034785 501 QNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18554 236 VNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPL 279
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
295-548 |
5.65e-08 |
|
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: 55.26 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 295 SKAPWSSLAWTVTT----YVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL 370
Cdd:cd18565 35 SFLPLVPASLGPADprgqLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 371 RIVDRGTSSVTGLLSYLVFNIIPTLADII-IGIIYFSMffNAWFGLIVFLCMSLYLILTIMVTEW-RAKFRR------DM 442
Cdd:cd18565 115 SVLNNDVNQLERFLDDGANSIIRVVVTVLgIGAILFYL--NWQLALVALLPVPLIIAGTYWFQRRiEPRYRAvreavgDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 443 NtqenatrARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSE 522
Cdd:cd18565 193 N-------ARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLD 265
|
250 260 270
....*....|....*....|....*....|..
gi 18034785 523 RR------LQVGDFVLFGTYITQLYMPLNWFG 548
Cdd:cd18565 266 GPplftgtLTVGTLVTFLFYTQRLLWPLTRLG 297
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
398-544 |
5.73e-08 |
|
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: 55.10 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 398 IIIGIIYFSMFFNAWFGLIVFLCMSLyLILTIMVTEWRA--KFRR------DMN--TQENATRARavdsllnfeTVKYYN 467
Cdd:cd18548 126 MLIGAIIMAFRINPKLALILLVAIPI-LALVVFLIMKKAipLFKKvqkkldRLNrvVRENLTGIR---------VIRAFN 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 468 AEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18548 196 REDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
590-758 |
6.09e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfydisSGciriDGQDISQVTQISLRSHIGVV 669
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------SG----ELQPSSGTVFRSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 670 PQDTVLFNDTIANNIRYgrvtagdseiqAAAQAAGIHDAILSFPEGYETQVGERGLK----LSGGEKQRVAIARTILKAP 745
Cdd:PLN03073 578 SQHHVDGLDLSSNPLLY-----------MMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKP 646
|
170
....*....|...
gi 18034785 746 DIILLDEATSALD 758
Cdd:PLN03073 647 HILLLDEPSNHLD 659
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
277-556 |
8.54e-08 |
|
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: 54.82 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 277 ALNVLVPIFYR---DIVNLLTSKAPWSSLAWTVTTYVFLKFLqgggtgstgfVSNLRTFLWIRVQQFTSRGVELRLFSHL 353
Cdd:cd18555 16 LLTLLIPILTQyviDNVIVPGNLNLLNVLGIGILILFLLYGL----------FSFLRGYIIIKLQTKLDKSLMSDFFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 354 HELSLRWHLGRRTGEVL-RIvdrgtSSVTGLLSYLVFNIIPTLADIIIGIIYFSM--FFNAWFGLIVFLCMSLYLILTIM 430
Cdd:cd18555 86 LKLPYSFFENRSSGDLLfRA-----NSNVYIRQILSNQVISLIIDLLLLVIYLIYmlYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 431 VTewraKFRRDMNTQENATRARA----VDSLLNFETVKYYNAEGYE----LERYREAILKFQGLEwKSTASLVLLNQTQN 502
Cdd:cd18555 161 TR----KKIKKLNQEEIVAQTKVqsylTETLYGIETIKSLGSEKNIykkwENLFKKQLKAFKKKE-RLSNILNSISSSIQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 18034785 503 MVIGFGLLagsLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQT 556
Cdd:cd18555 236 FIAPLLIL---WIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFIL 286
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
265-544 |
1.01e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 54.42 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLkflqgggTGSTGFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAV-------VLAGWVAQRAQTRLTGRTGERLLYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 345 VELRLFSHLHELSLRWHLGRRTGevlRIVDRGTS---SVTGLLSY-LVFNIIPTLADIIIGIIYFSMffNAWFGLIVFLC 420
Cdd:cd18546 74 LRLRVFAHLQRLSLDFHERETSG---RIMTRMTSdidALSELLQTgLVQLVVSLLTLVGIAVVLLVL--DPRLALVALAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 421 mslyLILTIMVTEWrakFRRDMNTQENATRARAVDSLLNF-ET------VKYYNAEGYELER-------YREAILK---- 482
Cdd:cd18546 149 ----LPPLALATRW---FRRRSSRAYRRARERIAAVNADLqETlagirvVQAFRRERRNAERfaelsddYRDARLRaqrl 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 483 ----FQGLEWKSTASLVLlnqtqnmVIGFGllagsllcAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18546 222 vaiyFPGVELLGNLATAA-------VLLVG--------AWRVAAGTLTVGVLVAFLLYLRRFFAPI 272
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
588-802 |
1.27e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 588 GRVEFENVHFSYAD----GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYD-ISSGCIRIDGQDIS-QVTQIS 661
Cdd:PRK13549 256 GEVILEVRNLTAWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHIGVVPQD----------TVLFNDTIANNIRYgrvtAGDSEIQAAAQAAGIHDAIL------SFPEgyeTQVGergl 725
Cdd:PRK13549 336 IAQGIAMVPEDrkrdgivpvmGVGKNITLAALDRF----TGGSRIDDAAELKTILESIQrlkvktASPE---LAIA---- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 726 KLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQ---ASLAK--VCtnrtTIVVAHRLSTVVN-ADQILVIKD 799
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYkliNQLVQqgVA----IIVISSELPEVLGlSDRVLVMHE 480
|
...
gi 18034785 800 GCI 802
Cdd:PRK13549 481 GKL 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
608-758 |
1.42e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 608 DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QISLRSHIGVVPQD----------TVLF 676
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDrkrdglvlgmSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 677 NDTIANnIRYGRVTAGdsEIQAAAQAAGIHDAILSF----PeGYETQVGerglKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK10762 350 NMSLTA-LRYFSRAGG--SLKHADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDE 421
|
....*.
gi 18034785 753 ATSALD 758
Cdd:PRK10762 422 PTRGVD 427
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
602-800 |
2.22e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQISLRSHIGVVPQD-TVLFNDT 679
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 680 IANNIRYGRV-TAGdseiQAAAQAAGIHDAILSFPE-GYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSAL 757
Cdd:PRK10982 90 VMDNMWLGRYpTKG----MFVDQDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18034785 758 dTSNE-----RAIQASLAKVCtnrTTIVVAHRLSTVVN-ADQILVIKDG 800
Cdd:PRK10982 166 -TEKEvnhlfTIIRKLKERGC---GIVYISHKMEEIFQlCDEITILRDG 210
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
324-539 |
2.25e-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: 53.37 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 324 GFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RIVDRGTssvtgLLSYLVFNIIPTLADIIIGI 402
Cdd:cd18782 56 AVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELStRISELDT-----IRGFLTGTALTTLLDVLFSV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 403 IYFS-MFFNAWF-GLIVFLCMSLYLILTIMVT-----EWRAKFRRDMNTQenatrARAVDSLLNFETVKYYNAEGYELER 475
Cdd:cd18782 131 IYIAvLFSYSPLlTLVVLATVPLQLLLTFLFGpilrrQIRRRAEASAKTQ-----SYLVESLTGIQTVKAQNAELKARWR 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 476 YREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLF---GTYITQ 539
Cdd:cd18782 206 WQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFrilSGYVTG 272
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
611-758 |
2.52e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 611 FTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRSHIGVVPQD-TVLFNDTIANNI-- 684
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsrfMAYLGHLPGLKADlSTLENLHFLCGLhg 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18034785 685 RYGRVTAGDSEiqaaaqaagihdAILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:PRK13543 112 RRAKQMPGSAL------------AIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
596-798 |
3.11e-07 |
|
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: 50.82 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 596 HFSYADGretlQDVSFTvmPGQTVALVGPSGAGKSTILR--LLFRFYDISSGCIRIDGQDISQVTQISLRSHIgVVPQdt 673
Cdd:cd03227 7 FPSYFVP----NDVTFG--EGSLTIITGPNGSGKSTILDaiGLALGGAQSATRRRSGVKAGCIVAAVSAELIF-TRLQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 674 vlfndtiannirygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIA-----RTILKAPdII 748
Cdd:cd03227 78 -----------------------------------------------------LSGGEKELSALAlilalASLKPRP-LY 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18034785 749 LLDEATSALDTSNERAIQASLAK-VCTNRTTIVVAHRLSTVVNADQILVIK 798
Cdd:cd03227 104 ILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
589-758 |
3.23e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF-RFY--DISsGCIRIDGQ--DISQVTQ-ISL 662
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYgrNIS-GTVFKDGKevDVSTVSDaIDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 663 --------RSHIGVVPQDTVLFNDTIANnirYGRVTAGdseiqaaaqaaGIHDailsfpEGYETQVGER----------- 723
Cdd:NF040905 338 glayvtedRKGYGLNLIDDIKRNITLAN---LGKVSRR-----------GVID------ENEEIKVAEEyrkkmniktps 397
|
170 180 190
....*....|....*....|....*....|....*....
gi 18034785 724 ----GLKLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:NF040905 398 vfqkVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
615-786 |
4.03e-07 |
|
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: 51.98 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 615 PGQTVALVGPSGAGKSTILRLL-----------------------FRFYDISSGCIRIDGQDISQVtqislrshigVVPQ 671
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdwdeildeFRGSELQNYFTKLLEGDVKVI----------VKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 672 dtvlFNDTIANNIRyGRVtagdSEIQAAAQAAGIHDAILSFPEgyETQVGERGL-KLSGGEKQRVAIARTILKAPDIILL 750
Cdd:cd03236 95 ----YVDLIPKAVK-GKV----GELLKKKDERGKLDELVDQLE--LRHVLDRNIdQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18034785 751 DEATSALDT----SNERAIQaSLAKvcTNRTTIVVAHRLS 786
Cdd:cd03236 164 DEPSSYLDIkqrlNAARLIR-ELAE--DDNYVLVVEHDLA 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
607-810 |
4.70e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 607 QDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQISLRSHIGVVPQDT----VLFNDTIA 681
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDRkaegIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 NNI----RYGRVTAGdseiqaaaqaagihdAILSfpEGYETQVGERGLK---------------LSGGEKQRVAIARTIL 742
Cdd:PRK11288 350 DNInisaRRHHLRAG---------------CLIN--NRWEAENADRFIRslniktpsreqlimnLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 743 KAPDIILLDEATSALDTSNERAIQA---SLAKvcTNRTTIVVAHRLSTVVN-ADQILVIKDGCII-ERGRHEA 810
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNviyELAA--QGVAVLFVSSDLPEVLGvADRIVVMREGRIAgELAREQA 483
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
601-759 |
5.10e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS------HIGVVPQDTV 674
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 675 LFNDTIANNIRyGRVTAGDseiqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIARTILKAPDII 748
Cdd:PRK13538 92 LENLRFYQRLH-GPGDDEA-----------LWEAL--------AQVGLAGFEdvpvrqLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|.
gi 18034785 749 LLDEATSALDT 759
Cdd:PRK13538 152 ILDEPFTAIDK 162
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
606-811 |
1.38e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRllfrfyDISSgciRIDGQDISQVTQISLRSHIG--VVPQDT--VLFNDTia 681
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLK------TIAS---NTDGFHIGVEGVITYDGITPeeIKKHYRgdVVYNAE-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 682 NNIRYGRVTAGD------------------SEIQAAAQAAGIHDAILSFPEGYETQVGE---RGLklSGGEKQRVAIART 740
Cdd:TIGR00956 146 TDVHFPHLTVGEtldfaarcktpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 741 ILKAPDIILLDEATSALDTSNE----RAIQASLakVCTNRTTIVVAHRLSTvvNA----DQILVIKDGCIIERG-RHEAL 811
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATAlefiRALKTSA--NILDTTPLVAIYQCSQ--DAyelfDKVIVLYEGYQIYFGpADKAK 299
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
265-555 |
1.71e-06 |
|
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: 50.46 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 265 VLLCMGLMGLDRALNVLVPIFYRDIVN--LLTSKAPWSSLAWTVTTYVFLKFLQgggtgstgFVSN-LRTFLWIRVQQFT 341
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLS--------FLLQyLQTYLLQKLGQRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 342 SRGVELRLFSHLHELSLRWHLGRRTGevlRIVDRGTS---SVTGLLSYLVFNIIptlADI--IIGIIYFSMFFNAWFGLI 416
Cdd:cd18544 73 IYDLRRDLFSHIQRLPLSFFDRTPVG---RLVTRVTNdteALNELFTSGLVTLI---GDLllLIGILIAMFLLNWRLALI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 417 VFLCMSLYLILTIMVTEW-RAKFRR------DMNT--QENatraravdsLLNFETVKYYNAEGYELER-------YREAI 480
Cdd:cd18544 147 SLLVLPLLLLATYLFRKKsRKAYREvreklsRLNAflQES---------ISGMSVIQLFNREKREFEEfdeinqeYRKAN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 481 LK--------FQGLEWKSTASLVLlnqtqnmVIGFGllagsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYR 552
Cdd:cd18544 218 LKsiklfalfRPLVELLSSLALAL-------VLWYG--------GGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFN 282
|
...
gi 18034785 553 MIQ 555
Cdd:cd18544 283 ILQ 285
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
329-544 |
2.74e-06 |
|
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: 49.80 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 329 LRTFLWIRVqqfTSR-GVEL--RLFSHLHELSLRWHLGRRTGEVL-RIvdRGTSSVTgllSYLVFNIIPTLADIIIGIIY 404
Cdd:cd18588 61 LRTYLFSHT---TNRiDAELgaRLFRHLLRLPLSYFESRQVGDTVaRV--RELESIR---QFLTGSALTLVLDLVFSVVF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 405 FS-MFFNAWF-GLIVFLCMSLYLILTIMVTewrAKFRRDMNTQ-ENATRARA--VDSLLNFETVKYYNAEGYELERYREA 479
Cdd:cd18588 133 LAvMFYYSPTlTLIVLASLPLYALLSLLVT---PILRRRLEEKfQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEEL 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 480 ILKFQglewKSTASLVLLNQTQNMVIGF--GLLAGSLLC--AYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18588 210 LARYV----KASFKTANLSNLASQIVQLiqKLTTLAILWfgAYLVMDGELTIGQLIAFNMLAGQVSQPV 274
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
590-789 |
3.06e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILR--LLFRFYDISSGCI------RIDGQDISqVTQIS 661
Cdd:PLN03073 178 IHMENFSISVG-GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQilhveqEVVGDDTT-ALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 662 LRSHI---------------------------GVVPQDTVLFNDTIANNIR--YGRVTAGDSEIQAAAQAAGIhdAILSF 712
Cdd:PLN03073 256 LNTDIertqlleeeaqlvaqqrelefetetgkGKGANKDGVDKDAVSQRLEeiYKRLELIDAYTAEARAASIL--AGLSF 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 713 PEgyETQVgERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKvcTNRTTIVVAHR---LSTVV 789
Cdd:PLN03073 334 TP--EMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK--WPKTFIVVSHArefLNTVV 408
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
725-800 |
7.95e-06 |
|
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: 47.18 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 725 LKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNE----RAIQASLAKvcTNRTTIVVAHRLSTVVNADQILVIKDG 800
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEE--GKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
597-834 |
9.30e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 597 FSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfydiSSGCIRIDGQDISQVTQISLRShigvVPQDTVLF 676
Cdd:PRK10938 11 FRLSDTK-TLQLPSLTLNAGDSWAFVGANGSGKSALARAL------AGELPLLSGERQSQFSHITRLS----FEQLQKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 677 NDTIANNIR---------YGRVTAgdsEIQAAaqaaGIHDAILSfpEGYETQVG-----ERGLK-LSGGEKQRVAIARTI 741
Cdd:PRK10938 80 SDEWQRNNTdmlspgeddTGRTTA---EIIQD----EVKDPARC--EQLAQQFGitallDRRFKyLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 742 LKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIV-VAHRLSTVVN-ADQILVIKDGCIIERGRHEALLSRgGVYA 819
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ-ALVA 229
|
250
....*....|....*
gi 18034785 820 EMWQLQQQGQETVPE 834
Cdd:PRK10938 230 QLAHSEQLEGVQLPE 244
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
340-544 |
1.00e-05 |
|
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: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 340 FTSRGVELRLFS----HLHELSLRWHLGRRTGEVL-RIVDRGTssvtgLLSYLVFNIIPTLADIIIGIIYFSMFF--NAW 412
Cdd:cd18568 68 YFANRIDLSLLSdfykHLLSLPLSFFASRKVGDIItRFQENQK-----IRRFLTRSALTTILDLLMVFIYLGLMFyyNLQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 413 FGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEgYEL-----ERYREAILK-FQGL 486
Cdd:cd18568 143 LTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAE-RPIrwrweNKFAKALNTrFRGQ 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 487 EWKSTASLV--LLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18568 222 KLSIVLQLIssLINHLGTIAV---LWYG----AYLVISGQLTIGQLVAFNMLFGSVINPL 274
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
589-761 |
1.38e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 589 RVEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRL--------------LFrfydissGCIRIDGQDI 654
Cdd:PRK10938 260 RIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltLF-------GRRRGSGETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 655 SQVTQislrsHIGVVPQDTVL---FNDTIANNIrygrvtagdseiqaaaqAAGIHDAIlsfpeGYETQVGER-------- 723
Cdd:PRK10938 332 WDIKK-----HIGYVSSSLHLdyrVSTSVRNVI-----------------LSGFFDSI-----GIYQAVSDRqqklaqqw 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18034785 724 ----GL----------KLSGGEKQRVAIARTILKAPDIILLDEATSALDTSN 761
Cdd:PRK10938 385 ldilGIdkrtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
366-544 |
1.71e-05 |
|
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: 47.63 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 366 TGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQ 445
Cdd:cd18556 100 SGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLFVINNTIFTKKIVSLRNDLMDA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 446 ENATRARAVDSLLNFETVKYYNAEGYELERYREAILK---FQGLEWKSTASLVLLNQTQNmVIGFGLLAGSLLcaYFVSE 522
Cdd:cd18556 180 GRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNdrnSQKRYWKLTFKMLILNSLLN-VILFGLSFFYSL--YGVVN 256
|
170 180
....*....|....*....|..
gi 18034785 523 RRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18556 257 GQVSIGHFVLITSYILLLSTPI 278
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
600-800 |
2.17e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 600 ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYD---ISSGCIRIDGQDIsqvtQISLRSHIGVVPQ-DTVL 675
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPL----DSSFQRSIGYVQQqDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 676 FNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAI--LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIIL-LDE 752
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIklLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18034785 753 ATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVNA--DQILVIKDG 800
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
606-795 |
2.31e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTIL---------RLLFRFYDISSGCIRIDG-QDISQVTQISlRSHIGVVPQD--- 672
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGlEHIDKVIVID-QSPIGRTPRSnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 --TVLFnDTI-------ANNIRYGRVT-----AGDSeiqaaaqaagIHDAI-LSFPEGYE-------------------- 717
Cdd:cd03271 90 tyTGVF-DEIrelfcevCKGKRYNRETlevryKGKS----------IADVLdMTVEEALEffenipkiarklqtlcdvgl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 718 --TQVGERGLKLSGGEKQRVAIARTILKA---PDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVA-HRLSTVVNA 791
Cdd:cd03271 159 gyIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCA 238
|
....
gi 18034785 792 DQIL 795
Cdd:cd03271 239 DWII 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
597-758 |
2.91e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 597 FSYAdgrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFR-------------------------------FYDISSG 645
Cdd:PRK11147 13 FSDA---PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqqdpprnvegtVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 646 CIRIDGQDISQVTQISLRshIGVVPQDTVLfndtianNiRYGRVTAG---------DSEIQAAAQAAGIH-DAILSfpeg 715
Cdd:PRK11147 90 GIEEQAEYLKRYHDISHL--VETDPSEKNL-------N-ELAKLQEQldhhnlwqlENRINEVLAQLGLDpDAALS---- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18034785 716 yetqvgerglKLSGGEKQRVAIARTILKAPDIILLDEATSALD 758
Cdd:PRK11147 156 ----------SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
606-798 |
3.12e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLrSHIGvvPQDTVLFNDTIANNIR 685
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 686 YGrvtagdSEIQAAAQAagIHDAILSFPegYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNeRAI 765
Cdd:PRK13541 93 FW------SEIYNSAET--LYAAIHYFK--LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN-RDL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 18034785 766 QASLAKVCTNRTTIVV--AHRLSTVVNAdQILVIK 798
Cdd:PRK13541 162 LNNLIVMKANSGGIVLlsSHLESSIKSA-QILQLD 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
593-769 |
6.47e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 593 ENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfydisSGCIRIDGQDISQVTQISLrshiGVVPQD 672
Cdd:PRK10636 316 EKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------AGELAPVSGEIGLAKGIKL----GYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 673 TVLFNDTIANNIRY-GRVTAGDSEiqaaaqaAGIHDAILSFpeGYE-TQVGERGLKLSGGEKQRVAIARTILKAPDIILL 750
Cdd:PRK10636 384 QLEFLRADESPLQHlARLAPQELE-------QKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170
....*....|....*....
gi 18034785 751 DEATSALDTSNERAIQASL 769
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEAL 473
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
348-526 |
2.24e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 44.19 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLYLIL 427
Cdd:cd18561 74 RLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALL-GPLLILIYLFFLDPLVALILLVFALLIPLS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 428 TIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQglewKSTASLVLLNQTQNMVIGF 507
Cdd:cd18561 153 PALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLR----QATMKVLAVSLLSSGIMGL 228
|
170
....*....|....*....
gi 18034785 508 GLLAGSLLCAYFVSERRLQ 526
Cdd:cd18561 229 ATALGTALALGVGALRVLG 247
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
601-659 |
2.54e-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: 43.16 E-value: 2.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 601 DGRETLQDVsftvMPGQTVALVGPSGAGKSTILRLLFrfydissGCIRIDGQDISQVTQ 659
Cdd:cd01854 74 EGLDELREL----LKGKTSVLVGQSGVGKSTLLNALL-------PELVLATGEISEKLG 121
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
606-795 |
2.99e-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: 42.31 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRfydiSSGCIRIdgqdisqvtqISLRShigVVPQDTVLFNDTIANNIR 685
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARL----------ISFLP---KFSRNKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 686 YGRvtagdseiqaaaqaagihdailsfpeGYETqVGERGLKLSGGEKQRVAIARTILKAPD--IILLDEATSALDTSNER 763
Cdd:cd03238 74 VGL--------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|...
gi 18034785 764 AIQASLAK-VCTNRTTIVVAHRLSTVVNADQIL 795
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWII 159
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
615-650 |
3.26e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.77 E-value: 3.26e-04
10 20 30
....*....|....*....|....*....|....*.
gi 18034785 615 PGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRID 650
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVRED 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
595-813 |
3.85e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 595 VHFSYADGRETLQD-VSFTVMPGQTVALVGPSGAGKSTILRLL--------------FRFYDISSGCI------RIDGQD 653
Cdd:PRK15093 11 IEFKTSDGWVKAVDrVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDDIDLLRLsprerrKLVGHN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 654 ISQVTQislrshigvVPQDTVLFNDTIANNIR------------YGRVTAGDSEIQAAAQAAGI--HDAIL-SFPegYEt 718
Cdd:PRK15093 91 VSMIFQ---------EPQSCLDPSERVGRQLMqnipgwtykgrwWQRFGWRKRRAIELLHRVGIkdHKDAMrSFP--YE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 719 qvgerglkLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVC-TNRTTI-VVAHRLSTVVN-ADQIL 795
Cdd:PRK15093 159 --------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTIlLISHDLQMLSQwADKIN 230
|
250
....*....|....*...
gi 18034785 796 VIKDGCIIERGRHEALLS 813
Cdd:PRK15093 231 VLYCGQTVETAPSKELVT 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
590-656 |
4.20e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 4.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18034785 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 656
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD 67
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
325-539 |
5.00e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 42.83 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 325 FVSNLRTFLWIRV-----QQFTSRgvelrLFSHLHELSLRWHLGRRTGEVL-RIvdrgtSSVTGLLSYLVFNIIPTLADI 398
Cdd:cd18567 57 LLSALRSWLVLYLstslnLQWTSN-----LFRHLLRLPLSYFEKRHLGDIVsRF-----GSLDEIQQTLTTGFVEALLDG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 399 IIGIIYFSM--FFNAWFGLIVFLCMSLYLILTImvtewrAKFRRDMNTQENATRARA------VDSLLNFETVKYYNAEG 470
Cdd:cd18567 127 LMAILTLVMmfLYSPKLALIVLAAVALYALLRL------ALYPPLRRATEEQIVASAkeqshfLETIRGIQTIKLFGREA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 471 YELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQ 539
Cdd:cd18567 201 EREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQ 269
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
350-533 |
5.69e-04 |
|
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: 42.62 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 350 FSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGL-LSYLVFNiIPTLADIIIgIIYFSMFFNAWFGLIVFLCMSLYLILT 428
Cdd:cd18562 76 FEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLwLGFFREH-LAALVSLIV-LLPVALWMNWRLALLLVVLAAVYAALN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 429 IMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYN---AEGYELERYREAILKFQG--LEWKSTAS-LVLLNQTQN 502
Cdd:cd18562 154 RLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTrlaAETSALRGITRRLLAAQYpvLNWWALASvLTRAASTLT 233
|
170 180 190
....*....|....*....|....*....|.
gi 18034785 503 MVIGFgllagsLLCAYFVSERRLQVGDFVLF 533
Cdd:cd18562 234 MVAIF------ALGAWLVQRGELTVGEIVSF 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
727-795 |
1.25e-03 |
|
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: 42.74 E-value: 1.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18034785 727 LSGGEKQRVAIAR--TILK---APdIILLDEATSALDTSN-ERAiqASLAKVCTNRTT-IVVAHRLSTVVNADQIL 795
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIFKvkpAP-FCILDEVDAPLDDANvERF--ANLLKEFSKNTQfIVITHNKGTMEVADQLY 1162
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
727-795 |
1.41e-03 |
|
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: 40.53 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18034785 727 LSGGEKQRVAIAR--TILK---APdIILLDEATSALDTSN-ERAIQAsLAKVCTNRTTIVVAHRLSTVVNADQIL 795
Cdd:cd03278 114 LSGGEKALTALALlfAIFRvrpSP-FCVLDEVDAALDDANvERFARL-LKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
601-636 |
2.54e-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: 39.45 E-value: 2.54e-03
10 20 30
....*....|....*....|....*....|....*.
gi 18034785 601 DGRETLQDVsftvMPGQTVALVGPSGAGKSTILRLL 636
Cdd:pfam03193 95 EGIEALKEL----LKGKTTVLAGQSGVGKSTLLNAL 126
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
727-795 |
3.31e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18034785 727 LSGGEKQRVAIARTIL---KAPDIILLDEATSALDTSNERA-IQASLAKVCTNRTTIVVAHRLSTVVNADQIL 795
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
715-795 |
3.50e-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: 41.15 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 715 GYeTQVGERGLKLSGGEKQRVAIARTILK---APDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVV-AHRLSTVVN 790
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKT 897
|
....*
gi 18034785 791 ADQIL 795
Cdd:TIGR00630 898 ADYII 902
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
366-480 |
3.56e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 40.51 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18034785 366 TGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYfsMFFNAW-FGLIVFLCMSLYLILTIMVTEWRAKF-RRDMN 443
Cdd:cd18578 110 TGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLII--AFVYGWkLALVGLATVPLLLLAGYLRMRLLSGFeEKNKK 187
|
90 100 110
....*....|....*....|....*....|....*..
gi 18034785 444 TQENATRaRAVDSLLNFETVKYYNAEGYELERYREAI 480
Cdd:cd18578 188 AYEESSK-IASEAVSNIRTVASLTLEDYFLEKYEEAL 223
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
603-636 |
3.79e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 3.79e-03
10 20 30
....*....|....*....|....*....|....
gi 18034785 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL 636
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALL 47
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
606-664 |
6.72e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 6.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18034785 606 LQDVSFTVMPGQTVaLVGPSGAGKSTILRLLFRFYDISSGcIRIDGQDISQVTQISLRS 664
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSS-RKFDEEDFYLGDDPDLPE 70
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
614-642 |
6.88e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 38.25 E-value: 6.88e-03
10 20 30
....*....|....*....|....*....|....
gi 18034785 614 MPGQTVALVGPSGAGKSTILRLL-----FRFYDI 642
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLakrlgYDFIDT 35
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
621-641 |
8.81e-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: 8.81e-03
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
619-660 |
9.28e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.47 E-value: 9.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 18034785 619 VALVGPSGAGKSTILRLLFRFYD---ISSGCIRID--GQDISQVTQI 660
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAKKLGlpyLDTGGIRTEevGKLASEVAAI 48
|
|
| |
