|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
232-752 |
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: 640.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 232 STDPRSTWRDLGRKLRLLSGYLWPRGSPSLQLTVLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLA--WTVTTY 309
Cdd:COG5265 5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVpvGLLLAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 310 VFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVF 389
Cdd:COG5265 85 GLLRLL------SVLF-GELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 390 NIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAE 469
Cdd:COG5265 158 NILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 470 GYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGT 549
Cdd:COG5265 238 AREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 550 YYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGK 629
Cdd:COG5265 318 VYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 630 STILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAI 709
Cdd:COG5265 398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958800879 710 LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG5265 478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
|
| 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: 531.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSK---APWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18581 1 CLLLLAAGRVVNVLVPILYKKIVDSLTPDsadSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 345 VELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 424
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 425 LILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMV 504
Cdd:cd18581 161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 505 IGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18581 241 ITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
232-752 |
2.65e-144 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 435.36 E-value: 2.65e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 232 STDPRSTWRDLgrkLRLLSGYLWPrgspslqltVLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVF 311
Cdd:COG1132 2 SKSPRKLLRRL---LRYLRPYRGL---------LILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 312 LKFLQGggtgstgFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNI 391
Cdd:COG1132 70 LALLRA-------LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 392 IPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGY 471
Cdd:COG1132 143 VRSVV-TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREER 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 472 ELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYY 551
Cdd:COG1132 222 ELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 552 RMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKST 631
Cdd:COG1132 302 NQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKST 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 632 ILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILS 711
Cdd:COG1132 382 LVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEA 461
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1958800879 712 FPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1132 462 LPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDE 502
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
268-564 |
7.27e-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: 374.64 E-value: 7.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSkAPWSSLAWTVTTYVFLKFLQGggtgSTGFVSNLRTFLWIRVQQFTSRGVEL 347
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTL-AKVKDLESAVTLILLYALLRF----SSKLLKELRSLLYRRVQQNAYRELSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLIL 427
Cdd:cd18560 76 KTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 428 TIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGF 507
Cdd:cd18560 156 TIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 508 GLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18560 236 GLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
268-564 |
2.53e-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: 329.10 E-value: 2.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 268 CMGLMGLDRALNVLVPIFYRDIVNLLT---SKAPWSSlawtVTTYVFLKFLQGGGtgstgFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLSggsGKSPWKE----IGLYVLLRFLQSGG-----GLGLLRSWLWIPVEQYSYRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 345 VELRLFSHLHELSLRWHLGRRTGEVLRIVDRGtSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLY 424
Cdd:cd18583 72 LSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQG-SSINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 425 LILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMV 504
Cdd:cd18583 151 VWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 505 IGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18583 231 LTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
590-752 |
2.15e-104 |
|
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: 319.56 E-value: 2.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
...
gi 1958800879 750 LDE 752
Cdd:cd03253 161 LDE 163
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
268-564 |
2.65e-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: 315.98 E-value: 2.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLA--WTVTTYVFLKFLqgggtgSTGFvSNLRTFLWIRVQQFTSRGV 345
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVplLLLLAYGLARIL------SSLF-NELRDALFARVSQRAVRRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 346 ELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYL 425
Cdd:cd18582 74 ALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 426 ILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVI 505
Cdd:cd18582 154 AFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALII 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 506 GFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:cd18582 234 SLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
231-752 |
3.18e-97 |
|
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: 316.78 E-value: 3.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 231 RSTDPRSTWRDLGRKLRLLSGYLWprgspslqlTVLLCMGLMGLdraLNVLVPIFYRDIVNLLTSKAPWSSLaWTVTtyv 310
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLL---------QVLLASLLINL---LALATPLFTQVVIDRVLPNQDLSTL-WVLA--- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 311 flkFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RIvdRGTSSVTGLLSYLVF 389
Cdd:COG2274 200 ---IGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAsRF--RDVESIREFLTGSLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 390 NiipTLADIIIGIIYFSM--FFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYN 467
Cdd:COG2274 275 T---ALLDLLFVLIFLIVlfFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 468 AEGYELERYREAILKFQGLEWKS---TASLVLLNQTQNMVIGFGLLAgslLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:COG2274 352 AESRFRRRWENLLAKYLNARFKLrrlSNLLSTLSGLLQQLATVALLW---LGAYLVIDGQLTLGQLIAFNILSGRFLAPV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 545 NWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYA-DGRETLQDVSFTVMPGQTVALVG 623
Cdd:COG2274 429 AQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 624 PSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAA 703
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLA 588
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1958800879 704 GIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG2274 589 GLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDE 637
|
|
| MTABC_N |
pfam16185 |
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ... |
6-255 |
1.04e-95 |
|
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: 297.27 E-value: 1.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 6 NYCEAEGPAGPAWTQNGLSPCFFYTLVPSTLMTLGVLALVLVLPCRRRevpAGTEeLSWAAGPRVAPYALQLSLAILQMA 85
Cdd:pfam16185 1 SYCEPNVSLTPVWVDHGLSPCFYDTLVPSVLLGFLLLFGTIQLIMYRK---YGTP-MEPKFIPRSRLYVLQLFLALLLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 86 LPLASLAGRVGTARGVRLPGYLLLASVLESLASACGLWLLVVERSQARQSLAMgvwmkFRHSLGLLLLWTVTFAAENLVL 165
Cdd:pfam16185 77 LALARFILRAALIGGGRLYGYMVLYACLSLLAWPFSLALLRLERRYALPSLPT-----RGHGLVLLLFWTLAFVAENLAF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 166 VSWNSPQWWWSRADLGQQVQFGLWVLRYMTSGGLFILGLWAPGLRPQSYTLHVNEEDQDGGRNQ---GRSTDPRSTWRDL 242
Cdd:pfam16185 152 VSWNSPDWWWGLETLSDQVEFGLFVVRYVCTLLLFVLGLKAPGLPRKPYMLLINEDERDVESSQpllGDSEENGSTWRNF 231
|
250
....*....|...
gi 1958800879 243 GRKLRLLSGYLWP 255
Cdd:pfam16185 232 GKKLRLLWPYLWP 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
350-752 |
1.06e-79 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 266.44 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 350 FSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLlsYLVF--NIIPTLADIIIgIIYFSMFFNAWFGLIVFLCMSLYLIL 427
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALFGL--WLEFmrEHLATLVALVV-LLPLALFMNWRLSLVLVVLGIVYTLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 428 TIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYN---AEGYELERYREAILKFQG--LEWKSTAS-LVLLNQTQ 501
Cdd:PRK13657 173 TTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIADNLLAAQMpvLSWWALASvLNRAASTI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 502 NMVIGFgllagsLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAG 581
Cdd:PRK13657 253 TMLAIL------VLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 582 PLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS 661
Cdd:PRK13657 327 DLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTI 741
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
410
....*....|.
gi 1958800879 742 LKAPDIILLDE 752
Cdd:PRK13657 487 LKDPPILILDE 497
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
253-752 |
6.15e-76 |
|
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: 256.18 E-value: 6.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 253 LWPRGSPSLQLTVLLCMGlMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgSTGFVSnlrTF 332
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVA-MILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRG----ICSFVS---TY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 333 LWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNiipTLadIIIGIIYFSMF 408
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLsRItfdSEQVASAATDAFIVLVRE---TL--TVIGLFIVLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 409 FNAWFGLIVFLcmsLYLILTIMVTEWRAKFRR-DMNTQE-NATRARAVDSLL-NFETVKYYNAEGYELERYREAILKFQG 485
Cdd:TIGR02203 152 YSWQLTLIVVV---MLPVLSILMRRVSKRLRRiSKEIQNsMGQVTTVAEETLqGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 486 LEWKSTASLVLLNQTQNMVIGFGLlAGSLLCAYFVSER-RLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENM 564
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLAL-AVVLFIALFQAQAgSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 565 FDLLKEETEVKDvpGAGPLRFHKGRVEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS 643
Cdd:TIGR02203 308 FTLLDSPPEKDT--GTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 644 SGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRV-TAGDSEIQAAAQAAGIHDAILSFPEGYETQVGE 722
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510
....*....|....*....|....*....|
gi 1958800879 723 RGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDE 495
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
590-752 |
7.50e-74 |
|
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: 239.44 E-value: 7.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
....
gi 1958800879 749 LLDE 752
Cdd:cd03251 161 ILDE 164
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
588-752 |
1.76e-72 |
|
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: 235.58 E-value: 1.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
....*
gi 1958800879 748 ILLDE 752
Cdd:cd03254 161 LILDE 165
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
590-752 |
1.28e-69 |
|
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: 228.19 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYAD--GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
....*
gi 1958800879 748 ILLDE 752
Cdd:cd03249 161 LLLDE 165
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
348-752 |
1.66e-69 |
|
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: 238.50 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGtssVTGLLSYLVfNIIP--TLADIIIGIIYFSMFFNAWF-GLIVFLCMSLy 424
Cdd:COG4988 96 RLLEKLLALGPAWLRGKSTGELATLLTEG---VEALDGYFA-RYLPqlFLAALVPLLILVAVFPLDWLsGLILLVTAPL- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 425 LILTIMVTEWRAKfrrDMNTQENATRARA----VDSLLNFETVKYYNAEGYEL-------ERYREA---ILKFQ-----G 485
Cdd:COG4988 171 IPLFMILVGKGAA---KASRRQWRALARLsghfLDRLRGLTTLKLFGRAKAEAeriaeasEDFRKRtmkVLRVAflssaV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 486 LEWKSTAS--LVLLnqtqnmVIGFGLLAGSLLcayfvserrLQVGDFVLFgtyitqL----YMPLNWFGTYY--RMIQTN 557
Cdd:COG4988 248 LEFFASLSiaLVAV------YIGFRLLGGSLT---------LFAALFVLL------LapefFLPLRDLGSFYhaRANGIA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 558 FidMENMFDLLkEETEVKDVPGAGPLRFHKG-RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL 636
Cdd:COG4988 307 A--AEKIFALL-DAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 637 FRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGY 716
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGL 463
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958800879 717 ETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
324-752 |
2.53e-67 |
|
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: 233.05 E-value: 2.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 324 GFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEvlrIVDRGTSSVTGLLSYLVFNIIPTLADIIIGII 403
Cdd:TIGR02204 72 ALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGE---VVSRLTTDTTLLQSVIGSSLSMALRNALMCIG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 404 YFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQEN--ATRARAVDSLLNFETVKYYNAEGYELERYREAIL 481
Cdd:TIGR02204 149 GLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRiaDAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 482 KFQGLEWKSTASLVLLNqTQNMVIGFGLLAGSL-LCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFID 560
Cdd:TIGR02204 229 KAYEAARQRIRTRALLT-AIVIVLVFGAIVGVLwVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 561 MENMFDLLKEETEVK--DVPGAGPLRFhKGRVEFENVHFSYADGRET--LQDVSFTVMPGQTVALVGPSGAGKSTILRLL 636
Cdd:TIGR02204 308 AERLIELLQAEPDIKapAHPKTLPVPL-RGEIEFEQVNFAYPARPDQpaLDGLNLTVRPGETVALVGPSGAGKSTLFQLL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 637 FRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGY 716
Cdd:TIGR02204 387 LRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGY 466
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958800879 717 ETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR02204 467 DTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDE 502
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
347-752 |
3.46e-67 |
|
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: 232.35 E-value: 3.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 347 LRLFSHLHELSLRWHLGRRTGEVL-RIVdrgtSSVTGLLSYLVFNIIPTLADI--IIGIIYFSMFFNAWFGLIVFLCMSL 423
Cdd:COG4987 92 VRLYRRLEPLAPAGLARLRSGDLLnRLV----ADVDALDNLYLRVLLPLLVALlvILAAVAFLAFFSPALALVLALGLLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 424 YLILTIMVTEWRAKFR-RDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQN 502
Cdd:COG4987 168 AGLLLPLLAARLGRRAgRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 503 MVIGFGLLAGSLLCAYFVSERRLQVGDFVLFgtyitqLYMPLNWF-------GTYYRMIQTnfID-MENMFDLLKEETEV 574
Cdd:COG4987 248 LAAGLAVVAVLWLAAPLVAAGALSGPLLALL------VLAALALFealaplpAAAQHLGRV--RAaARRLNELLDAPPAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 575 KDvPGAGPLRFHKGRVEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD 653
Cdd:COG4987 320 TE-PAEPAPAPGGPSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 654 ISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQ 733
Cdd:COG4987 399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:COG4987 479 RLALARALLRDAPILLLDE 497
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
350-752 |
1.01e-59 |
|
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: 212.44 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 350 FSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGL-LSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLcmslylILT 428
Cdd:TIGR01192 96 FGRIISMPLSWHQQRGTSNALHTLLRATETLFGLwLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLG------ILY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 429 IMVTEWRAKFRRD----MNTQENATRARAVDSLLNFETVKYYN---AEGYELERYREAILKFQG--LEWKSTASLvlLNQ 499
Cdd:TIGR01192 170 ILIAKLVMQRTKNgqaaVEHHYHNVFKHVSDSISNVSVVHSYNrieAETSALKQFTNNLLSAQYpvLDWWALASG--LNR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 500 TQNMVigfGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPG 579
Cdd:TIGR01192 248 MASTI---SMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPAD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 580 AGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ 659
Cdd:TIGR01192 325 APELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTR 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 660 ISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIAR 739
Cdd:TIGR01192 405 ESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484
|
410
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:TIGR01192 485 AILKNAPILVLDE 497
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
100-752 |
2.71e-56 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 204.96 E-value: 2.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 100 GVRLPGYLLLA----SVLESLASACGLWLLVVERSQARQSLAMGVWMKFRhslgLLLLWTVTFAAENLVLVSWNSPQWWW 175
Cdd:TIGR00958 40 VLWLEGTLRLGvlwlGALGILLNKAGGLLAAVKPLVAALCLATPSLSSLR----ALAFWEALDPAVRVALGLWSWFVWSY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 176 SRADLGQqvqfGLWVlrymtsgglFILGLWAPGLrpqsytlhvneEDQDGGRNQGrstdprstwrDLGRKLRLLSGYLWP 255
Cdd:TIGR00958 116 GAALPAA----ALWA---------VLSSAGASEK-----------EAEQGQSETA----------DLLFRLLGLSGRDWP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 256 RGSPSLQLTVLLCMGLMgldralnvLVPIFYRDIVNLLTSKAPWSSLAWTVTtyvFLKFLQGGGTGSTGFVSNLRTFLWI 335
Cdd:TIGR00958 162 WLISAFVFLTLSSLGEM--------FIPFYTGRVIDTLGGDKGPPALASAIF---FMCLLSIASSVSAGLRGGSFNYTMA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 336 RVQqftsRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVfNIIPTLADIIIGIIYFSMFFNAWFGL 415
Cdd:TIGR00958 231 RIN----LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNV-NVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 416 IVFLCMSLYLILTIMVTEWRAKFRRDmnTQENATRARAV--DSLLNFETVKYYNAEGYELERYREAILKFQGLEWKStAS 493
Cdd:TIGR00958 306 VTLINLPLVFLAEKVFGKRYQLLSEE--LQEAVAKANQVaeEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRK-AL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 494 LVLLNQTQNMVIGFGLLAGSLLC-AYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEET 572
Cdd:TIGR00958 383 AYAGYLWTTSVLGMLIQVLVLYYgGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 573 EVKDVPGAGPLRFhKGRVEFENVHFSYAD--GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRID 650
Cdd:TIGR00958 463 NIPLTGTLAPLNL-EGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 651 GQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGG 730
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
|
650 660
....*....|....*....|..
gi 1958800879 731 EKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDE 643
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
289-752 |
5.77e-56 |
|
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: 200.59 E-value: 5.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 289 IVNLLTSKAPWSSLAWTVTTY---VFLKFLQGGGTGSTGFVSNLRtflwIRVQqftsrgVELRLFSHLHELSLRWHLGRR 365
Cdd:TIGR02857 30 VDGLISAGEPLAELLPALGALalvLLLRALLGWLQERAAARAAAA----VKSQ------LRERLLEAVAALGPRWLQGRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 366 TGEVLRIVDRGTSSVTGLLS-YLVFNIiptLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNT 444
Cdd:TIGR02857 100 SGELATLALEGVEALDGYFArYLPQLV---LAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 445 QENATRARAV-DSLLNFETVKYYNAEGYEL-------ERYRE--------AILKFQGLEWKSTASLVLLNqtqnMVIGFG 508
Cdd:TIGR02857 177 AALSRLSGHFlDRLRGLPTLKLFGRAKAQAaairrssEEYRErtmrvlriAFLSSAVLELFATLSVALVA----VYIGFR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 509 LLAGSLLcayfvserrLQVGDFVLFgtYITQLYMPLNWFGTYY--RMIQTNFIdmENMFDLLKEET----EVKDVPGAGP 582
Cdd:TIGR02857 253 LLAGDLD---------LATGLFVLL--LAPEFYLPLRQLGAQYhaRADGVAAA--EALFAVLDAAPrplaGKAPVTAAPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 583 LRfhkgrVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL 662
Cdd:TIGR02857 320 SS-----LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTIL 742
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
490
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:TIGR02857 475 RDAPLLLLDE 484
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
590-752 |
4.41e-55 |
|
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: 186.82 E-value: 4.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFNDTIANNIrygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
....
gi 1958800879 749 LLDE 752
Cdd:cd03228 119 ILDE 122
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
588-752 |
8.81e-53 |
|
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: 182.40 E-value: 8.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03245 1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:cd03245 161 ILLLDE 166
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
587-752 |
5.07e-49 |
|
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: 172.27 E-value: 5.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 587 KGRVEFENVHFSYAD--GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS 664
Cdd:cd03248 9 KGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 665 HIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:cd03248 169 PQVLILDE 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
296-752 |
1.38e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 180.99 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 296 KAPWSSLAWTVTTYVFLKFLQGggtgSTGFVSNLrTFLWI--RVQQFTSRgvelRLFSHLHELSLRWHLGRRTGEVLRIV 373
Cdd:PRK11176 58 KADRSVLKWMPLVVIGLMILRG----ITSFISSY-CISWVsgKVVMTMRR----RLFGHMMGMPVSFFDKQSTGTLLSRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 374 DRGTSSVTGLLSYLVFNIIPTLADIIIgiIYFSMFFNAW-FGLIVFLCMSLYLILTIMVTEwraKFR---RDMNTQENAT 449
Cdd:PRK11176 129 TYDSEQVASSSSGALITVVREGASIIG--LFIMMFYYSWqLSLILIVIAPIVSIAIRVVSK---RFRnisKNMQNTMGQV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 450 RARAVDSLLNFETVKYYNAEGYELERYREAI--LKFQGLEWKSTASLvlLNQTQNMVIGFGLlAGSLLCAYFVSERR-LQ 526
Cdd:PRK11176 204 TTSAEQMLKGHKEVLIFGGQEVETKRFDKVSnrMRQQGMKMVSASSI--SDPIIQLIASLAL-AFVLYAASFPSVMDtLT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 527 VGDF-VLFGTYITqLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEvKDVpGAGPLRFHKGRVEFENVHFSYaDGRET 605
Cdd:PRK11176 281 AGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE-KDE-GKRVIERAKGDIEFRNVTFTY-PGKEV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 --LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANN 683
Cdd:PRK11176 357 paLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANN 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 684 IRYGRV-TAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11176 437 IAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
590-752 |
1.60e-48 |
|
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: 171.13 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
....
gi 1958800879 749 LLDE 752
Cdd:cd03252 161 IFDE 164
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
587-752 |
1.73e-46 |
|
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: 174.55 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 587 KGRVEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSH 665
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 IGVVPQDTVLFNDTIANNI-RYGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIaRFGDAD--PEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:COG4618 486 PRLVVLDE 493
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
348-752 |
1.36e-44 |
|
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: 168.31 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 348 RLFSHLHELSLRWHLGRRTGEVLRIVdrgTSSVTGLLSYLVFNIIPTLADIIIGIIY--FSMFFNAWFGLIVFLCMSLYL 425
Cdd:TIGR02868 91 RVYERLARQALAGRRRLRRGDLLGRL---GADVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILAAGLLLAG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 426 ILTIMVTEWRAKFRRDMNTQENATRARAVDSLL-NFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMV 504
Cdd:TIGR02868 168 FVAPLVSLRAARAAEQALARLRGELAAQLTDALdGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 505 IGFGLLAGSLLCAYFVSERRLQ---VGDFVLFGTYITQLYMPL-NWFGTYYRMIQTnfidMENMFDLLKEETEVKDV--P 578
Cdd:TIGR02868 248 AGLAVLGALWAGGPAVADGRLApvtLAVLVLLPLAAFEAFAALpAAAQQLTRVRAA----AERIVEVLDAAGPVAEGsaP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 579 GAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT 658
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 659 QISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIA 738
Cdd:TIGR02868 404 QDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALA 483
|
410
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:TIGR02868 484 RALLADAPILLLDE 497
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
588-752 |
4.90e-44 |
|
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: 158.04 E-value: 4.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGEYS--DEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:cd03244 159 KILVLDE 165
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
567-752 |
7.53e-44 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 166.81 E-value: 7.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 567 LLKEETEVKDvpGAGPLRFHKGRVEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSG 645
Cdd:PRK10789 293 MLAEAPVVKD--GSEPVPEGRGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 646 CIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGL 725
Cdd:PRK10789 371 DIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGV 450
|
170 180
....*....|....*....|....*..
gi 1958800879 726 KLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK10789 451 MLSGGQKQRISIARALLLNAEILILDD 477
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
326-752 |
1.66e-42 |
|
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: 164.91 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 326 VSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEvlrIVDRGTSsVTGLLSYLVFNIIPTLAD--IIIGII 403
Cdd:TIGR01193 212 LSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGE---IVSRFTD-ASSIIDALASTILSLFLDmwILVIVG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 404 YFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMnTQENATRARAV-DSLLNFETVKYYNAEG-------YELER 475
Cdd:TIGR01193 288 LFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDA-MQANAVLNSSIiEDLNGIETIKSLTSEAeryskidSEFGD 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 476 YREAILKFQGLEWKSTASLVLLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:TIGR01193 367 YLNKSFKYQKADQGQQAIKAVTKLILNVVI---LWTG----AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 556 TNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRL 635
Cdd:TIGR01193 440 AARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 636 LFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYG-RVTAGDSEIQAAAQAAGIHDAILSFPE 714
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPL 599
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958800879 715 GYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
606-752 |
3.01e-39 |
|
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: 142.02 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFND-TIANNI 684
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 685 RYGRVTAGDSEIQAAAQaagIHDAI--LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR---AEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
590-752 |
1.33e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT--QIS-LRSHI 666
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrrEIPyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFND-TIANNIRYG-RVT-AGDSEIQAAAQAA----GIHDAILSFPEgyetqvgerglKLSGGEKQRVAIAR 739
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPlRVTgKSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVAIAR 150
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:COG2884 151 ALVNRPELLLADE 163
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
591-752 |
3.39e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.41 E-value: 3.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:COG4619 2 ELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLFNDTIANNI----RYGRVTAGDSEIQAAAQAAGIHDAILsfpegyETQVGErglkLSGGEKQRVAIARTILKAPD 746
Cdd:COG4619 81 QEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPD 150
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:COG4619 151 VLLLDE 156
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
588-752 |
5.78e-37 |
|
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: 137.54 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYA-DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03369 5 GEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFNDTIANNI-RYGRVTagDSEIQaaaqaagihdAILSFPEGyetqvgerGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDEYS--DEEIY----------GALRVSEG--------GLNLSQGQRQLLCLARALLKRP 144
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:cd03369 145 RVLVLDE 151
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
578-752 |
1.83e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 142.27 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 578 PGAGPLRFHKGRVEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 656
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 657 VTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIhDAILSFPEGYETQVGERGLKLSGGEKQRVA 736
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLG 485
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:PRK11160 486 IARALLHDAPLLLLDE 501
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
509-752 |
5.65e-34 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 137.93 E-value: 5.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 509 LLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLkeetevkDVPGAG------P 582
Cdd:PRK10790 263 ILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM-------DGPRQQygnddrP 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 583 LRfhKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL 662
Cdd:PRK10790 336 LQ--SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVVPQDTVLFNDTIANNIRYGRvTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTIL 742
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
250
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:PRK10790 493 QTPQILILDE 502
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
591-752 |
7.34e-34 |
|
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: 127.72 E-value: 7.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03246 2 EVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFNDTIANNIrygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
...
gi 1958800879 750 LDE 752
Cdd:cd03246 120 LDE 122
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
589-752 |
1.41e-33 |
|
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: 129.39 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVL-FNDTIANNIRYGR---------VTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEK 732
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREA--------VEEAL--------ERTGLEHLAdrpvdeLSGGER 143
|
170 180
....*....|....*....|
gi 1958800879 733 QRVAIARTILKAPDIILLDE 752
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDE 163
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
590-752 |
2.03e-33 |
|
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: 128.22 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQ--DTVLFNDTIANNIRYGRVTAG--DSEIQAAaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIAR 739
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGPENLGlpREEIRER-----VEEAL--------ELVGLEHLAdrppheLSGGQKQRVAIAG 147
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:COG1122 148 VLAMEPEVLVLDE 160
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
591-752 |
3.28e-33 |
|
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: 127.20 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIARTI 741
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLGLPEEEIEER---VEEAL--------ELVGLEGLRdrspftLSGGQKQRVAIAGVL 149
|
170
....*....|.
gi 1958800879 742 LKAPDIILLDE 752
Cdd:cd03225 150 AMDPDILLLDE 160
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
590-752 |
5.87e-32 |
|
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: 124.22 E-value: 5.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDI-----SSGCIRIDGQDI--SQVTQISL 662
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVVPQDTVLFNDTIANNIRYG-------RVTAGDSEIQAAAQAAGIHDailsfpegyetQVGER--GLKLSGGEKQ 733
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD-----------EVKDRlhALGLSGGQQQ 148
|
170
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:cd03260 149 RLCLARALANEPEVLLLDE 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
389-752 |
1.69e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 132.46 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 389 FNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEwRAKFRRDMNT-QENATRARAVDSLLNFETVKYYN 467
Cdd:PTZ00265 175 FITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNK-KVKINKKTSLlYNNNTMSIIEEALVGIRTVVSYC 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 468 AEGYELER-------YREAILKFQGLEwksTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQvGDF-------VLF 533
Cdd:PTZ00265 254 GEKTILKKfnlseklYSKYILKANFME---SLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPN-NDFhggsvisILL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 534 GTYITQ--LYMPLNWFGTYYRMIQ-TNfidmeNMFDLLKEETEVKDVPGAGPLRFHKgRVEFENVHFSYaDGR---ETLQ 607
Cdd:PTZ00265 330 GVLISMfmLTIILPNITEYMKSLEaTN-----SLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHY-DTRkdvEIYK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 608 DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRY 686
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKY 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 687 GRV---------------------------------------------------------TAGDSEIQAAAQAAGIHDAI 709
Cdd:PTZ00265 483 SLYslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFV 562
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958800879 710 LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PTZ00265 563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
590-754 |
2.09e-31 |
|
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: 122.20 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHI 666
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFN-DTIANNIRYGRVTAG--DSEIQAAaqaagIHDAILSFpegyetqvgerGLK---------LSGGEKQR 734
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGvpKAEARER-----AEELLELV-----------GLSgfenayphqLSGGMRQR 139
|
170 180
....*....|....*....|
gi 1958800879 735 VAIARTILKAPDIILLDELF 754
Cdd:cd03293 140 VALARALAVDPDVLLLDEPF 159
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
265-562 |
3.90e-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: 123.81 E-value: 3.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRA-------LLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 345 VELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLY 424
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVL-TLIGALVILFYLNWKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 425 LILTIMVTEW-RAKFRRDMNTQENATrARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNM 503
Cdd:cd07346 153 VLILRYFRRRiRKASREVRESLAELS-AFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 504 VIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDME 562
Cdd:cd07346 232 LTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
590-752 |
6.26e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 121.70 E-value: 6.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHI 666
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQD-------TVLfndtiaNNI---RYGRVtagdseiqaaaqaaGIHDAILSF--PEGYET------QVG------E 722
Cdd:COG3638 83 GMIFQQfnlvprlSVL------TNVlagRLGRT--------------STWRSLLGLfpPEDRERalealeRVGladkayQ 142
|
170 180 190
....*....|....*....|....*....|
gi 1958800879 723 RGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADE 172
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
591-752 |
1.69e-30 |
|
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: 120.35 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRSHIGVVP 670
Cdd:COG4555 3 EVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLF-NDTIANNIRYgrvTAGDSEIQAAAQAAGIHDAI--LSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:COG4555 81 DERGLYdRLTVRENIRY---FAELYGLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
....*
gi 1958800879 748 ILLDE 752
Cdd:COG4555 154 LLLDE 158
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
591-754 |
2.42e-30 |
|
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: 116.96 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QdtvlfndtiannirygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDIILL 750
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
....
gi 1958800879 751 DELF 754
Cdd:cd00267 105 DEPT 108
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
590-752 |
2.54e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.40 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHIGVV 669
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFND-TIANNIRYgrvTAGDSEIQAAAQAAGIHDAI--LSFPEGYETQVGerglKLSGGEKQRVAIARTILKAPD 746
Cdd:COG1131 79 PQEPALYPDlTVRENLRF---FARLYGLPRKEARERIDELLelFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPE 151
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:COG1131 152 LLILDE 157
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
277-544 |
2.95e-30 |
|
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: 120.44 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 277 ALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLkflqgGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHEL 356
Cdd:pfam00664 13 AISPAFPLVLGRILDVLLPDGDPETQALNVYSLALL-----LLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 357 SLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIyFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRA 436
Cdd:pfam00664 88 PMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGII-VMFYYGWKLTLVLLAVLPLYILVSAVFAKILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 437 KFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLC 516
Cdd:pfam00664 167 KLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFG 246
|
250 260
....*....|....*....|....*...
gi 1958800879 517 AYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:pfam00664 247 AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
589-754 |
3.90e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 3.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvtqisLRSH 665
Cdd:COG1116 7 ALELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 IGVVPQDTVLFN-DTIANNIRYGRVTAGDSeiqaaaqaagihdailsfpegyETQVGER--------GLK---------L 727
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVP----------------------KAERRERarellelvGLAgfedayphqL 139
|
170 180
....*....|....*....|....*..
gi 1958800879 728 SGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPF 166
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
590-752 |
3.96e-30 |
|
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: 117.03 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRSHIGV 668
Cdd:cd03247 1 LSINNVSFSYPEQEQQvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFNDTIANNIrygrvtagdseiqaaaqaagihdailsfpegyetqvgerGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
....
gi 1958800879 749 LLDE 752
Cdd:cd03247 121 LLDE 124
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
590-752 |
4.56e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.61 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---- 662
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVVPQD-------TVLFNdtIANNIRYGRVTAGDSE--IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQ 733
Cdd:COG1136 85 RRHIGFVFQFfnllpelTALEN--VALPLLLAGVSRKERRerARELLERVGLGDRLDHRPS-----------QLSGGQQQ 151
|
170
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:COG1136 152 RVAIARALVNRPKLILADE 170
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
590-752 |
5.09e-30 |
|
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: 119.14 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSY---ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQD---------TVlfNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILS-FPEgyetqvgerglKLSGGEKQRVA 736
Cdd:COG1124 82 QMVFQDpyaslhprhTV--DRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDrYPH-----------QLSGGQRQRVA 148
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:COG1124 149 IARALILEPELLLLDE 164
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
525-752 |
7.78e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 125.34 E-value: 7.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 525 LQVGDFVLFgtYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLkeETEVKDVPGAGPLRFHKGRVEFENVH---FSYaD 601
Cdd:PRK11174 287 LFAGFFVLI--LAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFL--ETPLAHPQQGEKELASNDPVTIEAEDleiLSP-D 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRF--YdisSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDT 679
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800879 680 IANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
590-754 |
8.37e-30 |
|
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: 117.24 E-value: 8.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIslRSHIGVV 669
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNIRYGRVTAGDSE------IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTIL 742
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLRGVPKaeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALA 146
|
170
....*....|..
gi 1958800879 743 KAPDIILLDELF 754
Cdd:cd03259 147 REPSLLLLDEPL 158
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
590-752 |
1.55e-29 |
|
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: 117.39 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT---QISLRSHI 666
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFND-TIANNI-----RYGRVTagDSEIQAAAQAA----GIHDAILSFPegyetqvGErglkLSGGEKQRVA 736
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLS--EAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRKRVA 151
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:COG1127 152 LARALALDPEILLYDE 167
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
590-754 |
1.64e-29 |
|
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: 117.40 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNI-------RYGRVTAgDSEIQAAAQAAGIHDAilSFPEGYETQvgerglkLSGGEKQRVAIARTI 741
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkllKWPKEKI-RERADELLALVGLDPA--EFADRYPHE-------LSGGQQQRVGVARAL 150
|
170
....*....|...
gi 1958800879 742 LKAPDIILLDELF 754
Cdd:cd03295 151 AADPPLLLMDEPF 163
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
590-752 |
2.55e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.82 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRsHIGVV 669
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-PEKR-NVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNIRYG----RVTAgdSEIQAAaqaagIHDAIlsfpegyeTQVGERGL------KLSGGEKQRVAIA 738
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGlrmrGVPK--AEIRAR-----VAELL--------ELVGLEGLadryphQLSGGQQQRVALA 147
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:COG3842 148 RALAPEPRVLLLDE 161
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
590-752 |
3.18e-29 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 116.05 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---- 662
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVVPQDTVLFND-TIANNIRYGRVTAGDSEIQAAAQAA------GIHDAILSFPEgyetqvgerglKLSGGEKQRV 735
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEellervGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:cd03255 150 AIARALANDPKIILADE 166
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
591-752 |
1.03e-28 |
|
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: 114.97 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHIG 667
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFND-TIANNIRYGRVtagdseiqaaaqaaGIHDAILSFPEGYE-----------TQVG------ERGLKLSG 729
Cdd:cd03256 82 MIFQQFNLIERlSVLENVLSGRL--------------GRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQLSG 147
|
170 180
....*....|....*....|...
gi 1958800879 730 GEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADE 170
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
590-752 |
1.09e-28 |
|
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: 114.16 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ--ISLRSHIG 667
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLF-NDTIANNIRYGRVTA-GDSEIQAAAQAA------GIHDAILSFPegyetqvgergLKLSGGEKQRVAIAR 739
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVkGMSKAEAEERALellekvGLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:cd03262 149 ALAMNPKVMLFDE 161
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
514-752 |
2.95e-28 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 122.36 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 514 LLCAYF--VSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVK-DVPGAGPLRF--HKG 588
Cdd:TIGR00957 1204 LFAALFavISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGwpPRG 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLDpFSQYS--DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:TIGR00957 1442 ILVLDE 1447
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
590-752 |
3.27e-28 |
|
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: 119.62 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET----LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---L 662
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVVPQDTVL-FNDtiannirygRVTAGDSeiqaaaqaagIHDAILSFPEGYETQVGER--------GLK------- 726
Cdd:COG1123 341 RRRVQMVFQDPYSsLNP---------RMTVGDI----------IAEPLRLHGLLSRAERRERvaellervGLPpdladry 401
|
170 180
....*....|....*....|....*....
gi 1958800879 727 ---LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1123 402 pheLSGGQRQRVAIARALALEPKLLILDE 430
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
590-752 |
3.39e-28 |
|
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: 111.51 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS--LRSHIG 667
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLF-NDTIANNIRYGrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPD 746
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:cd03229 121 VLLLDE 126
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
590-752 |
8.94e-28 |
|
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: 111.73 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV--TQIS-LRSHI 666
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgRAIPyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFND-TIANNIRYGRVTAGDS------EIQAAAQAAGIHDAILSFPEGyetqvgerglkLSGGEKQRVAIAR 739
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEVTGVPpreirkRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:cd03292 150 AIVNSPTILIADE 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
455-752 |
1.08e-27 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 120.52 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 455 DSLLNFETVKYYNAEGYELERYREAI-LKFQGLEWKSTASLVL--LNQTQNMVI-GFGLLAGSLLcayfVSERRLQVGDF 530
Cdd:PTZ00265 1027 EAFYNMNTVIIYGLEDYFCNLIEKAIdYSNKGQKRKTLVNSMLwgFSQSAQLFInSFAYWFGSFL----IRRGTILVDDF 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 531 V--LF-----GTYITQLyMPLNWFGTYYRMiqtnfiDMENMFDLLKEETEVkDVPGAGPLRFH-----KGRVEFENVHFS 598
Cdd:PTZ00265 1103 MksLFtflftGSYAGKL-MSLKGDSENAKL------SFEKYYPLIIRKSNI-DVRDNGGIRIKnkndiKGKIEIMDVNFR 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 599 YADGRET--LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDI---------------------------------- 642
Cdd:PTZ00265 1175 YISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 643 --------------------SSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQA 702
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKF 1334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958800879 703 AGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PTZ00265 1335 AAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDE 1384
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
590-754 |
1.11e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.10 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHIGVV 669
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQD---------TVLfnDTIANNiRYG------RVTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LS 728
Cdd:COG1121 81 PQRaevdwdfpiTVR--DVVLMG-RYGrrglfrRPSRADREA--------VDEAL--------ERVGLEDLAdrpigeLS 141
|
170 180
....*....|....*....|....*.
gi 1958800879 729 GGEKQRVAIARTILKAPDIILLDELF 754
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPF 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
591-752 |
1.45e-27 |
|
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: 109.83 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QdtVLfndtiannirygrvtagdseiqaaaQAAGIHDaiLSfpegyetqvgERGL-KLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03214 80 Q--AL-------------------------ELLGLAH--LA----------DRPFnELSGGERQRVLLARALAQEPPILL 120
|
...
gi 1958800879 750 LDE 752
Cdd:cd03214 121 LDE 123
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
590-752 |
1.45e-27 |
|
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: 111.44 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---R 663
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVVPQD---------TVLfnDTIANNIRYGRVTAGDSEIQAAAQAA----GIHDAIL-SFPegYEtqvgerglkLSG 729
Cdd:cd03257 82 KEIQMVFQDpmsslnprmTIG--EQIAEPLRIHGKLSKKEARKEAVLLLlvgvGLPEEVLnRYP--HE---------LSG 148
|
170 180
....*....|....*....|...
gi 1958800879 730 GEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADE 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
590-752 |
1.71e-27 |
|
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: 109.41 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHIGVV 669
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFNDtiannirygrvtagdseiqaaaqaagihdaiLSfpeGYETqvgergLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03230 79 PEEPSLYEN-------------------------------LT---VREN------LKLSGGMKQRLALAQALLHDPELLI 118
|
...
gi 1958800879 750 LDE 752
Cdd:cd03230 119 LDE 121
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
590-752 |
1.96e-27 |
|
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: 111.05 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRSHI 666
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFND-TIANNIRYG---RVTAGDSEIQAAAQAA----GIHDAILSFPegyetqvGErglkLSGGEKQRVAIA 738
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEKleavGLRGAEDLYP-------AE----LSGGMKKRVALA 148
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:cd03261 149 RALALDPELLLYDE 162
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
590-752 |
3.31e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 110.85 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQISLRSHIG 667
Cdd:COG1126 2 IEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFND-TIANNIRYG---------------------RVtagdseiqaaaqaaGIHDAILSFPEgyetqvgergl 725
Cdd:COG1126 81 MVFQQFNLFPHlTVLENVTLApikvkkmskaeaeeramelleRV--------------GLADKADAYPA----------- 135
|
170 180
....*....|....*....|....*..
gi 1958800879 726 KLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDE 162
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
590-754 |
5.49e-27 |
|
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: 109.10 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRE----TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGciridgqdisqvtQISLRSH 665
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------------SVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 IGVVPQDTVLFNDTIANNI---------RYGRVtagdseiqaaaqaagIHDAILS-----FPEGYETQVGERGLKLSGGE 731
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgkpfdeeRYEKV---------------IKACALEpdleiLPDGDLTEIGEKGINLSGGQ 132
|
170 180
....*....|....*....|...
gi 1958800879 732 KQRVAIARTILKAPDIILLDELF 754
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPL 155
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
593-752 |
8.81e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 108.50 E-value: 8.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqisLRSHIGVVPQD 672
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 T--VLFNDTIANNIRYG--RVTAGDSEIQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03226 80 VdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
....
gi 1958800879 749 LLDE 752
Cdd:cd03226 149 IFDE 152
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
580-752 |
1.27e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.74 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 580 AGPLRFHKGRVEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDI 654
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 655 --SQVTQISLRSHIGVVPQDTVLFNDTIANNIRYG-RVtagdseiqaaaqaAGIH-----DAILsfpEGYETQVG----- 721
Cdd:COG1117 81 ydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlRL-------------HGIKskselDEIV---EESLRKAAlwdev 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958800879 722 -----ERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1117 145 kdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDE 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
591-755 |
3.22e-26 |
|
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: 107.13 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----- 665
Cdd:cd03224 2 EVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-----GLPPHerara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 -IGVVPQDTVLFND-TIANNIRYGRVTAGDSEIQAAAqaagihDAILS-FPEGYETQvGERGLKLSGGEKQRVAIARTIL 742
Cdd:cd03224 76 gIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARL------ERVYElFPRLKERR-KQLAGTLSGGEQQMLAIARALM 148
|
170
....*....|...
gi 1958800879 743 KAPDIILLDELFL 755
Cdd:cd03224 149 SRPKLLLLDEPSE 161
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
588-752 |
1.16e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.01 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRsHIG 667
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL-PPKDR-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLF-NDTIANNIRYG----RVTAgdSEIqaaaqaagihdailsfpegyETQVGE-------------RGLKLSG 729
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrKVPK--AEI--------------------DRRVREaaellgledlldrKPKQLSG 136
|
170 180
....*....|....*....|...
gi 1958800879 730 GEKQRVAIARTILKAPDIILLDE 752
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDE 159
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
591-752 |
3.62e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 104.68 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----- 665
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-----GLPPHriarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 -IGVVPQDTVLFND-TIANNIRYGRVTAGDSEiqaaaQAAGIHDAILS-FPEgyetqVGER----GLKLSGGEKQRVAIA 738
Cdd:COG0410 79 gIGYVPEGRRIFPSlTVEENLLLGAYARRDRA-----EVRADLERVYElFPR-----LKERrrqrAGTLSGGEQQMLAIG 148
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:COG0410 149 RALMSRPKLLLLDE 162
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
591-754 |
4.08e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 103.77 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHIGVVP 670
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 Q----DT---VLFNDTIANNiRYG------RVTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGE 731
Cdd:cd03235 75 QrrsiDRdfpISVRDVVLMG-LYGhkglfrRLSKADKAK--------VDEAL--------ERVGLSELAdrqigeLSGGQ 137
|
170 180
....*....|....*....|...
gi 1958800879 732 KQRVAIARTILKAPDIILLDELF 754
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPF 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
590-752 |
5.87e-25 |
|
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: 104.20 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---R 663
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVVPQDTVLFND-TIANNIRYGRVTAG------DSEIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVA 736
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGvpkaeiEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVG 150
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:cd03258 151 IARALANNPKVLLCDE 166
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
590-752 |
2.02e-24 |
|
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: 107.68 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGR-ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS---SGCIRIDGQDISQVTQISLRSH 665
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 IGVVPQD--TVLFNDTIANNIRYGRVTAGDS------EIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAI 737
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALENLGLSraearaRVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170
....*....|....*
gi 1958800879 738 ARTILKAPDIILLDE 752
Cdd:COG1123 154 AMALALDPDLLIADE 168
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
590-752 |
1.66e-23 |
|
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: 99.62 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP--PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFND-TIANNIRYGRVTAGDSEiqaAAQAAGIHDAI-LSFPEGYEtqvGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGLRLKKLPK---AEIKERVAEALdLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKV 151
|
....*
gi 1958800879 748 ILLDE 752
Cdd:cd03300 152 LLLDE 156
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
606-754 |
1.96e-23 |
|
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: 99.72 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIslRSHIGVVPQDTVLF-NDTIANNI 684
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 685 RYG-------RVTAgDSEIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:cd03299 93 AYGlkkrkvdKKEI-ERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
590-752 |
5.12e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.29 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQ--DTVLFNDTIANNIRYG----RVTAGDseiqaaaqaagIHDAILSfpegYETQVG-ERGLK-----LSGGEKQRVA 736
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkKVPPKK-----------MKDIIDD----LAKKVGmEDYLDkepqnLSGGQKQRVA 152
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:PRK13632 153 IASVLALNPEIIIFDE 168
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
590-752 |
1.14e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.55 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK13635 6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAIlsfpegyeTQVG------ERGLKLSGGEKQRVAIART 740
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGLENIG---VPREEMVERVDQAL--------RQVGmedflnREPHRLSGGQKQRVAIAGV 154
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:PRK13635 155 LALQPDIIILDE 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
590-752 |
2.33e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.10 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---LRSHI 666
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFND-TIANNIRYGRVTAGDSE------IQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQRVAIAR 739
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLIIAGASGddirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK10908 151 AVVNKPAVLLADE 163
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
591-754 |
2.34e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.36 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYadGRETLQdVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRShIGVVP 670
Cdd:COG3840 3 RLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLFND-TIANNIRYG-----RVTAGDSEiqaaaqaaGIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIA 738
Cdd:COG3840 78 QENNLFPHlTVAQNIGLGlrpglKLTAEQRA--------QVEQAL--------ERVGLAGLLdrlpgqLSGGQRQRVALA 141
|
170
....*....|....*.
gi 1958800879 739 RTILKAPDIILLDELF 754
Cdd:COG3840 142 RCLVRKRPILLLDEPF 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
590-752 |
2.43e-22 |
|
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: 95.72 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTvALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQiSLRSHIGVV 669
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQD-------TVL-FNDTIA--NNIRYGRVtagDSEIQAAAQAAGIHDAilsfpegYETQVGerglKLSGGEKQRVAIAR 739
Cdd:cd03264 78 PQEfgvypnfTVReFLDYIAwlKGIPSKEV---KARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQ 143
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:cd03264 144 ALVGDPSILIVDE 156
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
588-752 |
3.33e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 102.68 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYA-DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQISLRSHI 666
Cdd:TIGR01271 1216 GQMDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLDpYEQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:TIGR01271 1373 KILLLDE 1379
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
593-752 |
4.13e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:PRK13548 6 RNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 TVL-FNDTIANNIRYGRVTAGDSEiqaaaqaagIHDAILsfPEGYETQVGERGLK------LSGGEKQRVAIAR--TILK 743
Cdd:PRK13548 85 SSLsFPFTVEEVVAMGRAPHGLSR---------AEDDAL--VAAALAQVDLAHLAgrdypqLSGGEQQRVQLARvlAQLW 153
|
170
....*....|...
gi 1958800879 744 APD----IILLDE 752
Cdd:PRK13548 154 EPDgpprWLLLDE 166
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
606-754 |
4.56e-22 |
|
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: 96.56 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRSH-IGVVPQDTVLF-NDTI 680
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelRELRRKkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958800879 681 ANNIRYGRVTAG-DSEIQAAAQAAGIHDAILsfpEGYETQ-VGErglkLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:cd03294 120 LENVAFGLEVQGvPRAEREERAAEALELVGL---EGWEHKyPDE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
563-752 |
4.65e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 102.36 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 563 NMFDLLKEETEV--KDVPGAG-PLRfhkGRVEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFR 638
Cdd:PLN03232 1208 NYIDLPSEATAIieNNRPVSGwPSR---GSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 639 FYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRyGRVTAGDSEIQAAAQAAGIHDAILSFPEGYET 718
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDA 1363
|
170 180 190
....*....|....*....|....*....|....
gi 1958800879 719 QVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PLN03232 1364 EVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
590-752 |
6.48e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.84 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILR---LLFRFydiSSGCIRIDGQDISQVTQISL- 662
Cdd:COG1135 2 IELENLSKTFPTKGGPvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLERP---TSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 --RSHIGVVPQDtvlFN----DTIANNIRYGRVTAG--DSEIqaaaqaagihdailsfpegyETQVGER----GLK---- 726
Cdd:COG1135 79 aaRRKIGMIFQH---FNllssRTVAENVALPLEIAGvpKAEI--------------------RKRVAELlelvGLSdkad 135
|
170 180 190
....*....|....*....|....*....|.
gi 1958800879 727 -----LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1135 136 aypsqLSGGQKQRVGIARALANNPKVLLCDE 166
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
590-752 |
6.71e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.34 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQ--DTVLFNDTIANNIRYGRVTAGDSEiqaaaqaagihDAILSFPEGYETQVGERGLK------LSGGEKQRVAIARTI 741
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGPVNMGLDK-----------DEVERRVEEALKAVRMWDFRdkppyhLSYGQKKRVAIAGVL 153
|
170
....*....|.
gi 1958800879 742 LKAPDIILLDE 752
Cdd:PRK13647 154 AMDPDVIVLDE 164
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
590-754 |
6.75e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.91 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvTQISLR-SHIGV 668
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPPReRRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLF-NDTIANNIRYG-RV-TAGDSEIqaaaqaagihdailsfpegyETQVGE-------RGLK------LSGGEK 732
Cdd:COG1118 80 VFQHYALFpHMTVAENIAFGlRVrPPSKAEI--------------------RARVEEllelvqlEGLAdrypsqLSGGQR 139
|
170 180
....*....|....*....|..
gi 1958800879 733 QRVAIARTILKAPDIILLDELF 754
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPF 161
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
593-752 |
8.11e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.57 E-value: 8.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:COG4559 5 ENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 TVL-FNDTIANNIRYGR-----VTAGDSEIqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIART 740
Cdd:COG4559 84 SSLaFPFTVEEVVALGRaphgsSAAQDRQI--------VREAL--------ALVGLAHLAgrsyqtLSGGEQQRVQLARV 147
|
170
....*....|....*....
gi 1958800879 741 I--LKAPD-----IILLDE 752
Cdd:COG4559 148 LaqLWEPVdggprWLFLDE 166
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
590-752 |
1.99e-21 |
|
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: 94.80 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQIslRSH 665
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEI--RKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 IGVVPQD--------TVlfNDTIA---NNIRYGRvtagdSEIQAAaqaagIHDAIlsfpegyeTQVGERGLK------LS 728
Cdd:TIGR04520 79 VGMVFQNpdnqfvgaTV--EDDVAfglENLGVPR-----EEMRKR-----VDEAL--------KLVGMEDFRdrephlLS 138
|
170 180
....*....|....*....|....
gi 1958800879 729 GGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR04520 139 GGQKQRVAIAGVLAMRPDIIILDE 162
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
572-752 |
2.12e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 100.24 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 572 TEVKDVPGAGPLRFHKGRVEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRID 650
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVN 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 651 GQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRyGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGG 730
Cdd:PTZ00243 1371 GREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVG 1449
|
170 180
....*....|....*....|...
gi 1958800879 731 EKQRVAIARTILK-APDIILLDE 752
Cdd:PTZ00243 1450 QRQLMCMARALLKkGSGFILMDE 1472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
588-752 |
2.81e-21 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 94.54 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYAD-GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISsGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03289 1 GQMTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFNDTIANNIR-YGRVTagDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:cd03289 158 KILLLDE 164
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
590-752 |
5.81e-21 |
|
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: 91.93 E-value: 5.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRShIGVV 669
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRD-IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNIRYG--RVTAGDSEIqaaaqAAGIHDA--ILsfpeGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlkLRKVPKDEI-----DERVREVaeLL----QIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:cd03301 149 PKVFLMDE 156
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
599-752 |
6.17e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 599 YADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQISLRSHIGVVPQ 671
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 DTVLFNDTIANNIRYGRVTAG--DSEIQAAAQAAGIHDAilSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGikDKQVLDEAVEKSLKGA--SIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
...
gi 1958800879 750 LDE 752
Cdd:PRK14239 172 LDE 174
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
606-752 |
7.57e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.41 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHIGVVPQDTvlfndtian 682
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 683 nirYG----RVTAGDseiqaaaqaagihdaILSFP-----EGYETQVGER--------GLK----------LSGGEKQRV 735
Cdd:COG4608 105 ---YAslnpRMTVGD---------------IIAEPlrihgLASKAERRERvaellelvGLRpehadrypheFSGGQRQRI 166
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:COG4608 167 GIARALALNPKLIVCDE 183
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
589-752 |
1.51e-20 |
|
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: 90.62 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQiSLRSHIGV 668
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFND-TIANNIR-----YGRVTAGDSeiqaaaqaagIHDAILSF-PEGYE-TQVGerglKLSGGEKQRVAIART 740
Cdd:COG4133 80 LGHADGLKPElTVRENLRfwaalYGLRADREA----------IDEALEAVgLAGLAdLPVR----QLSAGQKRRVALARL 145
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:COG4133 146 LLSPAPLWLLDE 157
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
590-752 |
1.67e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.24 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--AENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNIRYG----RVTAgdSEIQAAaqaagIHDAI----LsfpegyETQVGERGLKLSGGEKQRVAIART 740
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqKTPA--AEITPR-----VMEALrmvqL------EEFAQRKPHQLSGGQQQRVAIARA 158
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:PRK09452 159 VVNKPKVLLLDE 170
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
590-752 |
2.74e-20 |
|
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: 90.57 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLR 663
Cdd:COG4181 9 IELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 S-HIGVVPQD-------TVLFNdtiannirygrVT-----AGDSEiqaaaqAAGIHDAILsfpegyeTQVG--ERgLK-- 726
Cdd:COG4181 89 ArHVGFVFQSfqllptlTALEN-----------VMlplelAGRRD------ARARARALL-------ERVGlgHR-LDhy 143
|
170 180
....*....|....*....|....*....
gi 1958800879 727 ---LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG4181 144 paqLSGGEQQRVALARAFATEPAILFADE 172
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
590-752 |
2.94e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 90.91 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGC-IRIDGQDISQVTQISLRSHIGV 668
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 V---------PQDTVL------FNDTIAnniRYGRVTAGDSEIQaaaqaagihDAILsfpegyeTQVGERGLK------L 727
Cdd:COG1119 83 VspalqlrfpRDETVLdvvlsgFFDSIG---LYREPTDEQRERA---------RELL-------ELLGLAHLAdrpfgtL 143
|
170 180
....*....|....*....|....*
gi 1958800879 728 SGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDE 168
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
590-752 |
3.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.29 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQISLRSHIG 667
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQ--DTVLFNDTIANNIRYGRVTAGDSEiqaAAQAAGIHDAILSFP-EGYETQVGERglkLSGGEKQRVAIARTILKA 744
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGPLNLGLSK---EEVEKRVKEALKAVGmEGFENKPPHH---LSGGQKKRVAIAGILAMK 155
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:PRK13639 156 PEIIVLDE 163
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
593-754 |
3.34e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.47 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTIlrllfrFYDI------SSGCIRIDGQDISQVTqISLRSH- 665
Cdd:COG1137 7 ENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIvglvkpDSGRIFLDGEDITHLP-MHKRARl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 -IGVVPQDTVLFND-TIANNIRygrvtagdseiqaaaqaagihdAILSF----PEGYETQVGE-------------RGLK 726
Cdd:COG1137 79 gIGYLPQEASIFRKlTVEDNIL----------------------AVLELrklsKKEREERLEElleefgithlrksKAYS 136
|
170 180
....*....|....*....|....*...
gi 1958800879 727 LSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPF 164
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
606-752 |
3.67e-20 |
|
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: 90.19 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtQISLRSHIGVVP--QDTVLFND-TIAN 682
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGRtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 683 NIRYGRVTAGDSEIQAAAQAAGIHDA------ILSF---PEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAreraeeLLERvglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
589-752 |
4.87e-20 |
|
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: 88.76 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENV-----HFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL--FRFYDISSGCIRIDGQDISqvtQIS 661
Cdd:cd03213 3 TLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQDTVLF-NDTIANNIRYGrvtagdseiqaaaqaagihdAILsfpegyetqvgeRGlkLSGGEKQRVAIART 740
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMFA--------------------AKL------------RG--LSGGERKRVSIALE 125
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:cd03213 126 LVSNPSLLFLDE 137
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
608-752 |
4.98e-20 |
|
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: 92.47 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 608 DVSFTVMPGQTVALVGPSGAGKSTILRL---LFRFydiSSGCIRIDG---QDISQvtQISLRSH---IGVVPQDTVLFND 678
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGevlQDSAR--GIFLPPHrrrIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 679 -TIANNIRYG--RVTAGDSEIqaaaqaagihdailSFPE-----GYETQVGERGLKLSGGEKQRVAIARTILKAPDIILL 750
Cdd:COG4148 92 lSVRGNLLYGrkRAPRAERRI--------------SFDEvvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
..
gi 1958800879 751 DE 752
Cdd:COG4148 158 DE 159
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
588-752 |
5.60e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 95.58 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:PLN03130 1236 GSIKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFNDTIANNIR-YGRvtAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDpFNE--HNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:PLN03130 1394 KILVLDE 1400
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
591-752 |
8.49e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.12 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----- 665
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT-----KLPPHerara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 -IGVVPQDTVLFND-TIANNIRYGRVTAGDSEiqaaaqaAGIHDAILS-FPEGYETQvGERGLKLSGGEKQRVAIARTIL 742
Cdd:TIGR03410 76 gIAYVPQGREIFPRlTVEENLLTGLAALPRRS-------RKIPDEIYElFPVLKEML-GRRGGDLSGGQQQQLAIARALV 147
|
170
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:TIGR03410 148 TRPKLLLLDE 157
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
590-754 |
1.15e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.30 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqiSLRS-HIGV 668
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFND-TIANNIRYG-----RVTAGDSEIQAAAQAAGIHDAILS-FPEGYETQvgerglkLSGGEKQRVAIARTI 741
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlpRRERPNAAAIKAKVTQLLEMVQLAhLADRYPAQ-------LSGGQKQRVALARAL 151
|
170
....*....|...
gi 1958800879 742 LKAPDIILLDELF 754
Cdd:PRK10851 152 AVEPQILLLDEPF 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
608-754 |
1.15e-19 |
|
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: 88.12 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 608 DVSFTVmPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdISQVTQISL-----RSHIGVVPQDTVLF-NDTIA 681
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGLVFQQYALFpHLNVR 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800879 682 NNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpegyeTQVGERG-LKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGL--------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
590-752 |
1.38e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.44 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNIRYG----RVTAGDSEIQAAAQAAGIHdaILSFPEGYETQvgerglkLSGGEKQRVAIARTILKA 744
Cdd:PRK11607 97 FQSYALFpHMTVEQNIAFGlkqdKLPKAEIASRVNEMLGLVH--MQEFAKRKPHQ-------LSGGQRQRVALARSLAKR 167
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:PRK11607 168 PKLLLLDE 175
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
606-752 |
1.45e-19 |
|
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: 88.26 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ----DISQVTQ---ISLRSH-IGVVPQdtvlFN 677
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPreiLALRRRtIGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 678 DTIAnnirygRVTAGDseiqaaaqaagihdaILSFP---EGYETQVG-ERGLKL------------------SGGEKQRV 735
Cdd:COG4778 103 RVIP------RVSALD---------------VVAEPlleRGVDREEArARARELlarlnlperlwdlppatfSGGEQQRV 161
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:COG4778 162 NIARGFIADPPLLLLDE 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
590-752 |
1.47e-19 |
|
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: 90.50 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQ---DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYD---ISSGCIRIDGQDISQVTQISLR 663
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 ----SHIGVVPQD---------TVLfnDTIANNIRygrvtagdseiqaaaqaagIHDaILSFPEGYE------TQVG--- 721
Cdd:COG0444 82 kirgREIQMIFQDpmtslnpvmTVG--DQIAEPLR-------------------IHG-GLSKAEAREraiellERVGlpd 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958800879 722 -ERGLK-----LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG0444 140 pERRLDrypheLSGGMRQRVMIARALALEPKLLIADE 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
592-752 |
1.62e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 592 FENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqisLRshIGVVPQ 671
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 D-------TVL-----------------------FNDTIANNIRYGRVT---------AGDSEIqaaaqaagihDAILS- 711
Cdd:COG0488 69 EppldddlTVLdtvldgdaelraleaeleeleakLAEPDEDLERLAELQeefealggwEAEARA----------EEILSg 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958800879 712 --FPEG-YETQVGErglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG0488 139 lgFPEEdLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDE 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
590-752 |
1.92e-19 |
|
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: 87.81 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQ---DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHI 666
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFND-TIANNIRY-GRV--TAGDSeiqaaaqaagIHDAI--LSFPEGYETQVGERGLKLSGGEKQRVAIART 740
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfAGLygLKGDE----------LTARLeeLADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:cd03266 151 LVHDPPVLLLDE 162
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
591-753 |
2.30e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.46 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVP 670
Cdd:PRK10247 9 QLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLFNDTIANNIRYG---RVTAGDSE-IQAAAQAAGIHDAILsfpegyETQVGErglkLSGGEKQRVAIARTILKAPD 746
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPwqiRNQQPDPAiFLDDLERFALPDTIL------TKNIAE----LSGGEKQRISLIRNLQFMPK 157
|
....*..
gi 1958800879 747 IILLDEL 753
Cdd:PRK10247 158 VLLLDEI 164
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
570-752 |
2.31e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 570 EETEVKDVPGAGPLRFHKGR------VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS 643
Cdd:COG0488 290 EREEPPRRDKTVEIRFPPPErlgkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 644 SGCIRIdGQDIsqvtqislrsHIGVVPQDTVLF--NDTIANNIRYGRVTAGDSEIQaaaqaagihdAIL-SF---PEGYE 717
Cdd:COG0488 369 SGTVKL-GETV----------KIGYFDQHQEELdpDKTVLDELRDGAPGGTEQEVR----------GYLgRFlfsGDDAF 427
|
170 180 190
....*....|....*....|....*....|....*
gi 1958800879 718 TQVGerglKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG0488 428 KPVG----VLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
590-752 |
2.37e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDG------QDISQVTQISLR 663
Cdd:COG4161 3 IQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVV-------PQDTVLFNdTIANNIRYGRVT--AGDSEIQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQR 734
Cdd:COG4161 82 QKVGMVfqqynlwPHLTVMEN-LIEAPCKVLGLSkeQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQQR 149
|
170
....*....|....*...
gi 1958800879 735 VAIARTILKAPDIILLDE 752
Cdd:COG4161 150 VAIARALMMEPQVLLFDE 167
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
590-754 |
2.49e-19 |
|
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: 87.16 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYAdgrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqVTQISLRShIGVV 669
Cdd:cd03298 1 VRLDKIRFSYG---EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-AAPPADRP-VSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFND-TIANNIRYGRV-----TAGDSE-IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTIL 742
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLSpglklTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170
....*....|..
gi 1958800879 743 KAPDIILLDELF 754
Cdd:cd03298 145 RDKPVLLLDEPF 156
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
593-754 |
2.96e-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: 87.60 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRSHIGV--VP 670
Cdd:cd03218 4 ENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-MHKRARLGIgyLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLFND-TIANNIRYGRVTAGDSEiqaaaqaAGIHDAILSFPE--GYETQVGERGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03218 82 QEASIFRKlTVEENILAVLEIRGLSK-------KEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
....*..
gi 1958800879 748 ILLDELF 754
Cdd:cd03218 155 LLLDEPF 161
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
590-752 |
3.84e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCiRIDGQDI--------SQVTQIS 661
Cdd:PRK14243 11 LRTENLNVYYGSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQDTVLFNDTIANNIRYGRVTAG-----DSEIQAAAQAAGIHDAIlsfpegyETQVGERGLKLSGGEKQRVA 736
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGARINGykgdmDELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLC 161
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:PRK14243 162 IARAIAVQPEVILMDE 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
590-754 |
4.25e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 87.01 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSHIGVV 669
Cdd:cd03296 3 IEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFND-TIANNIRYG-RVTAGDSEIQAAAQAAGIHDAI----LS-FPEGYETQvgerglkLSGGEKQRVAIARTIL 742
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqLDwLADRYPAQ-------LSGGQRQRVALARALA 152
|
170
....*....|..
gi 1958800879 743 KAPDIILLDELF 754
Cdd:cd03296 153 VEPKVLLLDEPF 164
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
590-752 |
4.96e-19 |
|
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: 86.40 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqVTQI-SLRSHIG 667
Cdd:cd03263 1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRkAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFND-TIANNIR-YGRV-----TAGDSEIQAAAQAAGIHDAIlsfpegyETQVGErglkLSGGEKQRVAIART 740
Cdd:cd03263 79 YCPQFDALFDElTVREHLRfYARLkglpkSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIA 147
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:cd03263 148 LIGGPSVLLLDE 159
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
590-752 |
7.26e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDtvlfndtiaNNI-------------RY----GRVTAGDSEIqaaaqaagIHDAILSFP-EGYEtqvgERGLK-LSGG 730
Cdd:COG4604 81 RQE---------NHInsrltvrelvafgRFpyskGRLTAEDREI--------IDEAIAYLDlEDLA----DRYLDeLSGG 139
|
170 180
....*....|....*....|..
gi 1958800879 731 EKQRVAIARTILKAPDIILLDE 752
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDE 161
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
590-752 |
1.25e-18 |
|
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: 83.63 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI-SLRSHIGV 668
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQdtvlfndtiannirygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDII 748
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
....
gi 1958800879 749 LLDE 752
Cdd:cd03216 105 ILDE 108
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
590-752 |
1.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.64 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS--QVTQISLR 663
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVVPQ--DTVLFNDTIANNIRYGRVTAG--DSEIQAAaqaagIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIAR 739
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGlsEEEIENR-----VKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK13637 158 VVAMEPKILILDE 170
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
606-752 |
1.71e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QISLRSHIGVVPQDTVLFND-TIANN 683
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 684 IRYGRvtagdseiqaAAQAAGIHD------------AILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLD 751
Cdd:COG1129 100 IFLGR----------EPRRGGLIDwramrrrarellARLGLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
.
gi 1958800879 752 E 752
Cdd:COG1129 166 E 166
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
590-752 |
2.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.94 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRE--TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAiLSFpegyetqVGERGLK------LSGGEKQRVAIAR 739
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENKG---IPHEEMKERVNEA-LEL-------VGMQDFKereparLSGGQKQRVAIAG 153
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK13650 154 AVAMRPKIIILDE 166
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
601-754 |
2.90e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL-------FRFydisSGCIRIDGQDISQVtQISLRsHIGVVPQDT 673
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFSA----SGEVLLNGRRLTAL-PAEQR-RIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 674 VLF-NDTIANNIRYG---RVTAGD--SEIQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKAPDI 747
Cdd:COG4136 86 LLFpHLSVGENLAFAlppTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRA 154
|
....*..
gi 1958800879 748 ILLDELF 754
Cdd:COG4136 155 LLLDEPF 161
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
588-752 |
3.70e-18 |
|
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: 84.96 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYADG-RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHI 666
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFNDTIANNIRYGRvTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:cd03288 177 ILIMDE 182
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
602-752 |
5.07e-18 |
|
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: 83.04 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqVTQISLRSHIGVVPQDTVLF-NDTI 680
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFYpNLTA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800879 681 ANNIRYGRVTAG--DSEIQAAAQAAGIHDAilsfpegyetqVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03268 90 RENLRLLARLLGirKKRIDEVLDVVGLKDS-----------AKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
606-752 |
1.02e-17 |
|
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: 83.55 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-----QVTQISL-RS--HIGVVPQDTVLFN 677
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpphRIARLGIaRTfqNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 678 DTIANNIRYGRvtagdseiqaaaqaaGIHDAILSFPEGY--ETQVGER--------GLK---------LSGGEKQRVAIA 738
Cdd:COG0411 100 VLVAAHARLGR---------------GLLAALLRLPRARreEREARERaeellervGLAdradepagnLSYGQQRRLEIA 164
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:COG0411 165 RALATEPKLLLLDE 178
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
590-752 |
1.34e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISlRSHIGVV 669
Cdd:PRK13536 42 IDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQ-DTVLFNDTIANNI----RYGRVTAGDSEiqaaaqaaGIHDAILSFPEgYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMSTREIE--------AVIPSLLEFAR-LESKADARVSDLSGGMKRRLTLARALIND 190
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:PRK13536 191 PQLLILDE 198
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
590-752 |
1.73e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.45 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI--SQVTQISLRSHIG 667
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFNDTIA-NNIRYG-RVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:PRK09493 81 MVFQQFYLFPHLTAlENVMFGpLRVRGASKEEAEKQARELLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:PRK09493 156 KLMLFDE 162
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
590-752 |
2.08e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.88 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSY-ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQ--DTVLFNDTIANNIRYG-RVTAGDSEIQAAAQAAGIHDAILSFPEGYETQvgerglKLSGGEKQRVAIARTILKAP 745
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGlENHAVPYDEMHRRVSEALKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALNP 161
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:PRK13648 162 SVIILDE 168
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
590-752 |
2.38e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGR---ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS-- 664
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 665 -HIGVVPQDtvlFN----DTIANNIRYGRVTAGDS--EIQAAAQ----AAGIHDAILSFPEgyetqvgerglKLSGGEKQ 733
Cdd:PRK11153 82 rQIGMIFQH---FNllssRTVFDNVALPLELAGTPkaEIKARVTelleLVGLSDKADRYPA-----------QLSGGQKQ 147
|
170
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:PRK11153 148 RVAIARALASNPKVLLCDE 166
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
608-752 |
2.52e-17 |
|
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: 84.39 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 608 DVSFTVmPGQTV-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDG---QDISQVTQISL-RSHIGVVPQDTVLFND-TIA 681
Cdd:TIGR02142 15 DADFTL-PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPPeKRRIGYVFQEARLFPHlSVR 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800879 682 NNIRYG--RVTAGDSEIQAaaqaagihDAILSFpEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR02142 94 GNLRYGmkRARPSERRISF--------ERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
606-752 |
5.14e-17 |
|
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: 84.74 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQ---ISLRSHIGVVPQDTvlfnd 678
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRralRPLRRRMQVVFQDP----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 679 tiannirYG----RVTAGD--SEiqaaaqaaG--IHDAILSfPEGYETQVG----ERGLK----------LSGGEKQRVA 736
Cdd:COG4172 372 -------FGslspRMTVGQiiAE--------GlrVHGPGLS-AAERRARVAealeEVGLDpaarhrypheFSGGQRQRIA 435
|
170
....*....|....*..
gi 1958800879 737 IART-ILKaPDIILLDE 752
Cdd:COG4172 436 IARAlILE-PKLLVLDE 451
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
590-752 |
7.43e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:PRK09536 4 IDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVL-FNDTIANNIRYGRV-------TAGDSEiqaaaqAAGIHDAIlsfPEGYETQVGERGL-KLSGGEKQRVAIART 740
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGRTphrsrfdTWTETD------RAAVERAM---ERTGVAQFADRPVtSLSGGERQRVLLARA 153
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:PRK09536 154 LAQATPVLLLDE 165
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
590-752 |
8.90e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.38 E-value: 8.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRL---LFRFYDISSGCIRIDGQDISQVTQISLRSH 665
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 IGVVPQ--DTVLFNDTIANNIRYGRVTAGDSE------IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAI 737
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLENRAVPRpemikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170
....*....|....*
gi 1958800879 738 ARTILKAPDIILLDE 752
Cdd:PRK13640 155 AGILAVEPKIIILDE 169
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
590-754 |
9.06e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 79.63 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsqvtQISLRSHIGVV 669
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFND-TIANNIRYGRVTAGdseiqaaaqaAGIHDA---ILSFPEGYEtqVGERGLK----LSGGEKQRVAIARTI 741
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYLAQLKG----------LKKEEArrrIDEWLERLE--LSEYANKrveeLSKGNQQKVQFIAAV 143
|
170
....*....|...
gi 1958800879 742 LKAPDIILLDELF 754
Cdd:cd03269 144 IHDPELLILDEPF 156
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
591-754 |
1.01e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.68 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVTQISLRShiG 667
Cdd:COG4525 5 TVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLF-----NDTIANNIRYGRVTAGDSEiqaaaqaaGIHDAILSfpegyetQVGERGL------KLSGGEKQRVA 736
Cdd:COG4525 80 VVFQKDALLpwlnvLDNVAFGLRLRGVPKAERR--------ARAEELLA-------LVGLADFarrriwQLSGGMRQRVG 144
|
170
....*....|....*...
gi 1958800879 737 IARTILKAPDIILLDELF 754
Cdd:COG4525 145 IARALAADPRFLLMDEPF 162
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
590-752 |
1.35e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET--LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAILSFPE-GYETQVGERglkLSGGEKQRVAIARTILKA 744
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQG---IPREEMIKRVDEALLAVNMlDFKTREPAR---LSGGQKQRVAVAGIIALR 158
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:PRK13642 159 PEIIILDE 166
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
602-752 |
1.38e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.18 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIR-----ID-----GQDISQVTQisLRSHIGVVPQ 671
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditIDtarslSQQKGLIRQ--LRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 DTVLF-NDTIANNIRYGRV----------TAGDSEIQAAAQAAGIHDAilsFPEgyetqvgerglKLSGGEKQRVAIART 740
Cdd:PRK11264 93 NFNLFpHRTVLENIIEGPVivkgepkeeaTARARELLAKVGLAGKETS---YPR-----------RLSGGQQQRVAIARA 158
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:PRK11264 159 LAMRPEVILFDE 170
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
590-752 |
1.45e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISlRSHIGVV 669
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFND-TIANNIR-YGRVTAGDSEIQAAAQAAGIHDAILSfpEGYETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK13537 86 PQFDNLDPDfTVRENLLvFGRYFGLSAAAARALVPPLLEFAKLE--NKADAKVGE----LSGGMKRRLTLARALVNDPDV 159
|
....*
gi 1958800879 748 ILLDE 752
Cdd:PRK13537 160 LVLDE 164
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
590-752 |
1.45e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETlQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQiSLRShIGVV 669
Cdd:PRK11000 4 VTLRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP-AERG-VGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNIRYGRVTAG--DSEIQAAAQAAGihdAILsfpegyetQVG---ERGLK-LSGGEKQRVAIARTIL 742
Cdd:PRK11000 81 FQSYALYpHLSVAENMSFGLKLAGakKEEINQRVNQVA---EVL--------QLAhllDRKPKaLSGGQRQRVAIGRTLV 149
|
170
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:PRK11000 150 AEPSVFLLDE 159
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
265-555 |
1.84e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 80.63 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 265 VLLCMGLMGLDRALNVLVPIFYR----DIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQF 340
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKilidDVLIQLGPGGNTSLLLLLVLGLAGAYVLSA-------LLGILRGRLLARLGER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 341 TSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLS----YLVFNIIpTLadIIIGIIYFSMffNAWFGLI 416
Cdd:cd18563 74 ITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSdglpDFLTNIL-MI--IGIGVVLFSL--NWKLALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 417 VFLCMSLYLILTIMV-----TEWRAKFRR--DMNTQENatraravDSLLNFETVKYYNAEGYELERYREAILKFQglewK 489
Cdd:cd18563 149 VLIPVPLVVWGSYFFwkkirRLFHRQWRRwsRLNSVLN-------DTLPGIRVVKAFGQEKREIKRFDEANQELL----D 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 490 STASLVLLNQTQNMVIGFGLLAGSLLCAYF----VSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:cd18563 218 ANIRAEKLWATFFPLLTFLTSLGTLIVWYFggrqVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWIT 287
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
590-752 |
3.04e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQI----SLR 663
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVV-------PQDTVLFNDTIANNirygRVTAGDSEIQAAAQaagihDAILS----------FPegyetqvgergLK 726
Cdd:PRK11124 82 RNVGMVfqqynlwPHLTVQQNLIEAPC----RVLGLSKDQALARA-----EKLLErlrlkpyadrFP-----------LH 141
|
170 180
....*....|....*....|....*.
gi 1958800879 727 LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDE 167
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
590-752 |
3.53e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.46 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVV 669
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQ--DTVLFNDTIANNIRYGRVTAG-DSEIQAAAQAAGIHDAILsfpEGYETQVGERglkLSGGEKQRVAIARTILKAPD 746
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGlDEETVAHRVSSALHMLGL---EELRDRVPHH---LSGGEKKRVAIAGVIAMEPQ 157
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:PRK13652 158 VLVLDE 163
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
590-752 |
3.72e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQISLRSHIG 667
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQ--DTVLFNDTIANNIRYGRVTAGDSEiqaaaqaagihDAILSFPEGYETQVGERGLK------LSGGEKQRVAIAR 739
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGAVNLKLPE-----------DEVRKRVDNALKRTGIEHLKdkpthcLSFGQKKRVAIAG 154
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK13636 155 VLVMEPKVLVLDE 167
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
610-754 |
4.18e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.09 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 610 SFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRShIGVVPQDTVLFND-TIANNIRYG- 687
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRP-VSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800879 688 ----RVTAGDSE-IQAAAQAAGIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:PRK10771 97 npglKLNAAQREkLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPF 157
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
593-754 |
5.12e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLrshIGVVPQD 672
Cdd:PRK15056 10 NDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 T-------VLFNDTIANNiRYG------RVTAGDSEIQAAAQaagihdAILSFPEGYETQVGErglkLSGGEKQRVAIAR 739
Cdd:PRK15056 87 EevdwsfpVLVEDVVMMG-RYGhmgwlrRAKKRDRQIVTAAL------ARVDMVEFRHRQIGE----LSGGQKKRVFLAR 155
|
170
....*....|....*
gi 1958800879 740 TILKAPDIILLDELF 754
Cdd:PRK15056 156 AIAQQGQVILLDEPF 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
593-752 |
1.01e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:PRK11231 6 ENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 TVLFND-TIANNIRYGRvtagdSEIQAAAQAAGIHDAILSFPEGYETQVGE----RGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK11231 85 HLTPEGiTVRELVAYGR-----SPWLSLWGRLSAEDNARVNQAMEQTRINHladrRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
....*
gi 1958800879 748 ILLDE 752
Cdd:PRK11231 160 VLLDE 164
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
265-548 |
1.08e-15 |
|
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: 78.24 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRG-------VFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 345 VELRLFSHLHELSLRWHLGRRTGEvlrIVDRGTSSVTGL---LSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLIVFLCM 421
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDKARTGD---LMSRCTSDVDTIrrfLAFGLVELVRAVL-LFIGALIIMFSINWKLTLISLAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 422 SLYLILTI-MVTEWRAKFRR------DMNT--QENATRARavdsllnfeTVKYYNAEGYELER-------YREAILKFQG 485
Cdd:cd18542 150 PFIALFSYvFFKKVRPAFEEireqegELNTvlQENLTGVR---------VVKAFAREDYEIEKfdkeneeYRDLNIKLAK 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800879 486 LEWKSTASLVLLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFG 548
Cdd:cd18542 221 LLAKYWPLMDFLSGLQIVLV---LWVG----GYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
590-752 |
1.77e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.48 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQI-S 661
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAA------GIHDAILSfpegyetqvgERGLKLSGGEKQ 733
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAReklalvGISESLFE----------KNPFELSGGQMR 152
|
170
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDE 171
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
590-752 |
1.95e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----IS 661
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERG-LKLSGGEKQRVAIA 738
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV-----GLSEDLISKSpFELSGGQMRRVAIA 157
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:PRK13641 158 GVMAYEPEILCLDE 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
590-752 |
2.06e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.35 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDisqVTQISLRSH-IGV 668
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV---VNELEPADRdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLF-NDTIANNIRYGRVTAGDS--EIQAAaqaagIHDA--ILSFpegyETQVGERGLKLSGGEKQRVAIARTILK 743
Cdd:PRK11650 81 VFQNYALYpHMSVRENMAYGLKIRGMPkaEIEER-----VAEAarILEL----EPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
....*....
gi 1958800879 744 APDIILLDE 752
Cdd:PRK11650 152 EPAVFLFDE 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
591-752 |
2.95e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYADGRET---LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL----R 663
Cdd:PRK10535 6 ELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVVPQDTVLFND-TIANNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERGLKLSGGEKQRVAIARTIL 742
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:PRK10535 161 NGGQVILADE 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
590-754 |
3.94e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 75.06 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCI----RIDGQDISQVTQISLRSH 665
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 666 IGVVPQDTVLFNDTIANNI---------RYGRVTAGDSeiqaaaqaagIHDAILSFPEGYETQVGERGLKLSGGEKQRVA 736
Cdd:cd03290 81 VAYAAQKPWLLNATVEENItfgspfnkqRYKAVTDACS----------LQPDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170
....*....|....*...
gi 1958800879 737 IARTILKAPDIILLDELF 754
Cdd:cd03290 151 VARALYQNTNIVFLDDPF 168
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
590-752 |
5.60e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 79.60 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRE-TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDissgciRIDGQdisqvtqISLRSHIGV 668
Cdd:TIGR00957 637 ITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILsFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
....
gi 1958800879 749 LLDE 752
Cdd:TIGR00957 783 LFDD 786
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
599-752 |
5.64e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.85 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 599 YADGR---ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT---QISLRSH-IGVVPQ 671
Cdd:PRK11629 15 YQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 DTVLFND-TIANNIRYGRVTAGDSEIQAAAQAAGIHDAIlsfpeGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILL 750
Cdd:PRK11629 95 FHHLLPDfTALENVAMPLLIGKKKPAEINSRALEMLAAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
..
gi 1958800879 751 DE 752
Cdd:PRK11629 170 DE 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
590-754 |
7.98e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqislRSHIGVV 669
Cdd:COG4152 2 LELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLF-NDTIANNIRY-GR---VTAGDseiqaaaqaagIHDAILSFPEGYEtqVGERGLK----LSGGEKQRVAIART 740
Cdd:COG4152 77 PEERGLYpKMKVGEQLVYlARlkgLSKAE-----------AKRRADEWLERLG--LGDRANKkveeLSKGNQQKVQLIAA 143
|
170
....*....|....
gi 1958800879 741 ILKAPDIILLDELF 754
Cdd:COG4152 144 LLHDPELLILDEPF 157
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
590-752 |
9.57e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.30 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGReTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDisqVTQISLRSH-IGV 668
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLF-NDTIANNIRYGRVTAGDS--EIQAAaqaagIHDAI-LSFPEGYEtqvgERGL-KLSGGEKQRVAIARTILK 743
Cdd:PRK11432 83 VFQSYALFpHMSLGENVGYGLKMLGVPkeERKQR-----VKEALeLVDLAGFE----DRYVdQISGGQQQRVALARALIL 153
|
....*....
gi 1958800879 744 APDIILLDE 752
Cdd:PRK11432 154 KPKVLLFDE 162
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
605-752 |
1.12e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 605 TLQDVSFTV---MPGQTV-ALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ-ISL---RSHIGVVPQDTVLF 676
Cdd:PRK11144 9 QLGDLCLTVnltLPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgICLppeKRRIGYVFQDARLF 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 677 -NDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPegyetqvgergLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11144 89 pHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
606-754 |
1.17e-14 |
|
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: 74.89 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqislrshIGVVPQDTVLFNDTIANNIR 685
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 686 YGrVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:cd03291 120 FG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
593-754 |
1.32e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QISLRSHIGVVPQ 671
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 DTVLFND-TIANNIrygrvtAGDSEIQAAAQAAGIHDAILSFPEGYETQ--VGERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:PRK10895 86 EASIFRRlSVYDNL------MAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
....*.
gi 1958800879 749 LLDELF 754
Cdd:PRK10895 160 LLDEPF 165
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
590-752 |
1.40e-14 |
|
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: 73.56 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqISLRSHIGVV 669
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFNDTIA--NNIRYGRVTAGDSEIQAAAQaagihDAILSFPEGYEtqVGERGLK-LSGGEKQRVAIARTILKAPD 746
Cdd:cd03265 79 FQDLSVDDELTGweNLYIHARLYGVPGAERRERI-----DELLDFVGLLE--AADRLVKtYSGGMRRRLEIARSLVHRPE 151
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:cd03265 152 VLFLDE 157
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
606-752 |
1.54e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.39 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDI---SQVTQISLRSHIGVVPQDTvlfndtian 682
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 683 nirYG----RVTAGdseiqaaaqaagihdAILSFPEGYETQVG--ER-----------GLK----------LSGGEKQRV 735
Cdd:PRK11308 102 ---YGslnpRKKVG---------------QILEEPLLINTSLSaaERrekalammakvGLRpehydryphmFSGGQRQRI 163
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:PRK11308 164 AIARALMLDPDVVVADE 180
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
591-752 |
1.62e-14 |
|
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: 73.83 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDISQVtQISLRSHIGV 668
Cdd:TIGR01978 2 KIKDLHVSVED-KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLEL-EPDERARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 ---------VPQDTVL-FNDTIANNIRYGRvtaGDSEIQAAAQAAGIHD--AILSFPEGYEtqvgERGLK--LSGGEKQR 734
Cdd:TIGR01978 80 flafqypeeIPGVSNLeFLRSALNARRSAR---GEEPLDLLDFEKLLKEklALLDMDEEFL----NRSVNegFSGGEKKR 152
|
170
....*....|....*...
gi 1958800879 735 VAIARTILKAPDIILLDE 752
Cdd:TIGR01978 153 NEILQMALLEPKLAILDE 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
591-752 |
1.74e-14 |
|
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: 72.56 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTqISLRSHIGV 668
Cdd:cd03217 2 EIKDLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 vpqdTVLFND-------TIANNIRYgrvtagdseiqaaaqaagihdailsfpegyetqVGErglKLSGGEKQRVAIARTI 741
Cdd:cd03217 80 ----FLAFQYppeipgvKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLL 119
|
170
....*....|.
gi 1958800879 742 LKAPDIILLDE 752
Cdd:cd03217 120 LLEPDLAILDE 130
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
606-752 |
1.89e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 73.46 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQDISQVTqisLRSHIGVVPQ-DTVLFNDTIA 681
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKPDQ---FQKCVAYVRQdDILLPGLTVR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 682 NNIRY-----GRVTAGDSEIQAAAQAAGIHDAILsfpegyeTQVGERGLK-LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03234 100 ETLTYtailrLPRKSSDAIRKKRVEDVLLRDLAL-------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDE 169
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
606-752 |
2.17e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.60 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisQVT----QISLRSHIGVVPQDTVLFND-TI 680
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRirspRDAIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 681 ANNIRYGRVTAGdseiQAAAQAAGIHDAILSFPEGYetqvgerGLK---------LSGGEKQRVAIARTILKAPDIILLD 751
Cdd:COG3845 98 AENIVLGLEPTK----GGRLDRKAARARIRELSERY-------GLDvdpdakvedLSVGEQQRVEILKALYRGARILILD 166
|
.
gi 1958800879 752 E 752
Cdd:COG3845 167 E 167
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
590-752 |
2.75e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS-----GCIRIDGQDI--SQVTQISL 662
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVVPQDTVLFNDTIANNIRYGRVTAG-------DSEIQAAAQAAGIHDAIlsfpegyETQVGERGLKLSGGEKQRV 735
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:PRK14258 160 CIARALAVKPKVLLMDE 176
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
590-752 |
2.96e-14 |
|
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: 70.56 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQDISqvtqislrshIGVV 669
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQdtvlfndtiannirygrvtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDIIL 749
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
...
gi 1958800879 750 LDE 752
Cdd:cd03221 94 LDE 96
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
590-752 |
3.65e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS--QVTQIsLRSHIG 667
Cdd:PRK11614 6 LSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKI-MREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFND-TIANNIRYGRVTAGDSEIQAAaqaagIHDAILSFPEGYETQVgERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQER-----IKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPR 157
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:PRK11614 158 LLLLDE 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
591-752 |
4.58e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 75.49 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYADGRETLQ---DVSFTVMPGQTVALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVTQISLR 663
Cdd:COG4172 8 SVEDLSVAFGQGGGTVEavkGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 ----SHIGVVPQD--TVLfND--TIANNI-----RYGRVTAGD--SEIQAAAQAAGIHDA---ILSFPEgyetqvgergl 725
Cdd:COG4172 88 rirgNRIAMIFQEpmTSL-NPlhTIGKQIaevlrLHRGLSGAAarARALELLERVGIPDPerrLDAYPH----------- 155
|
170 180
....*....|....*....|....*..
gi 1958800879 726 KLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADE 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
597-752 |
6.01e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.39 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 597 FSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRID------GQDISQVTQISLRSHIGVVP 670
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLF-NDTIANNIRYGRVTAGdseIQAAAQAAGIHDAILSfPEGYETQVGER----GLKLSGGEKQRVAIARTILKAP 745
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHG---IKEKREIKKIVEECLR-KVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKP 172
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:PRK14246 173 KVLLMDE 179
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
606-752 |
7.82e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRS-HIGVVPQDTVLFNDTIA 681
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAkHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958800879 682 -NNIRYGRVTAGDSEIQAAAQAAgihdAILSfpegyETQVGER----GLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK10584 106 lENVELPALLRGESSRQSRNGAK----ALLE-----QLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
590-755 |
8.33e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---RSHI 666
Cdd:PRK11831 8 VDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQDTVLFND-TIANNIRYG--RVTAGDSEIqaaaqaagIHDAILSFPEGyetqVGERGL------KLSGGEKQRVAI 737
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPlrEHTQLPAPL--------LHSTVMMKLEA----VGLRGAaklmpsELSGGMARRAAL 154
|
170
....*....|....*...
gi 1958800879 738 ARTILKAPDIILLDELFL 755
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFV 172
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
585-752 |
1.18e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.66 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 585 FHKGRVEfENVhfsyadgreTLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS 664
Cdd:COG1101 11 FNPGTVN-EKR---------ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 665 HIGVVPQDTVL---FNDTIANNI--------RYG---RVTAGDSEIqaaaqaagIHDAILSFPEGYETQVGER-GLkLSG 729
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENLalayrrgkRRGlrrGLTKKRREL--------FRELLATLGLGLENRLDTKvGL-LSG 151
|
170 180
....*....|....*....|...
gi 1958800879 730 GEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDE 174
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
606-754 |
1.50e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.14 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS----HIGVVPQDTVLF-NDTI 680
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800879 681 ANNIRYGRVTAGdseIQAAAQAAGIHDAILSFpeGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:PRK10070 124 LDNTAFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
589-752 |
2.80e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYADGrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDISQVTQISLR 663
Cdd:PRK14247 3 KIEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVV-----PQDTVLFNDTIANNIRYGRVTAGDSEIqAAAQAAGIHDAILSfpEGYETQVGERGLKLSGGEKQRVAIA 738
Cdd:PRK14247 82 RRVQMVfqipnPIPNLSIFENVALGLKLNRLVKSKKEL-QERVRWALEKAQLW--DEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:PRK14247 159 RALAFQPEVLLADE 172
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
606-754 |
2.82e-13 |
|
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: 69.80 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV--TQISLRSHIGVVPQDTVLFNDTIA-N 682
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRMVVFQNYSLLPWLTVRENIALAvD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800879 683 NIRYGRVTAGDSEIQAAaqaagiHDAILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEE------HIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
457-754 |
3.16e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.86 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 457 LLNFETVKYYNAE-GYElerYREAILKFQGLEWKSTASLV------LLNQTQNMV--IGFG---LLAGSLLCAY-FVSER 523
Cdd:PLN03232 486 LASMDTVKCYAWEkSFE---SRIQGIRNEELSWFRKAQLLsafnsfILNSIPVVVtlVSFGvfvLLGGDLTPARaFTSLS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 524 RLQVgdfvlfgtyitqLYMPLNWFGTYYRMIQTNFIDMENMFDL-LKEETEVKDVPgagPLRFHKGRVEFENVHFSYADG 602
Cdd:PLN03232 563 LFAV------------LRSPLNMLPNLLSQVVNANVSLQRIEELlLSEERILAQNP---PLQPGAPAISIKNGYFSWDSK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RE--TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRfyDISSgciridgqdiSQVTQISLRSHIGVVPQDTVLFNDTI 680
Cdd:PLN03232 628 TSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--ELSH----------AETSSVVIRGSVAYVPQVSWIFNATV 695
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800879 681 ANNIRYGRVTAGDSEIQAAAQAAGIHDAILsFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
602-752 |
3.17e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQiSLRSHIGVVPQD----TVL 675
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRD-AIRAGIAYVPEDrkgeGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 676 FNDTIANNI---RYGRVTAGdseiqaaaqaaGI--HDAILSFPEGY-----------ETQVGErglkLSGGEKQRVAIAR 739
Cdd:COG1129 343 LDLSIRENItlaSLDRLSRG-----------GLldRRRERALAEEYikrlriktpspEQPVGN----LSGGNQQKVVLAK 407
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:COG1129 408 WLATDPKVLILDE 420
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
591-754 |
3.25e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqislrSHIGVVP 670
Cdd:PRK11248 3 QISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLFN-DTIANNIRYGRVTAGDSEIQAAAQAAGIhdAILSFPEGYETQvgeRGLKLSGGEKQRVAIARTILKAPDIIL 749
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGLQLAGVEKMQRLEIAHQM--LKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLL 151
|
....*
gi 1958800879 750 LDELF 754
Cdd:PRK11248 152 LDEPF 156
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
320-554 |
3.36e-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: 71.00 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 320 TGSTGFVSNLRTFLWIRV-QQFTSRgVELRLFSHLHELSLRWHLGRRTGEVLRivdRGTSSVTGLLSYLVFNIIPTLADI 398
Cdd:cd18564 64 ALLRGLASYAGTYLTALVgQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLS---RLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 399 IIGIIYFS-MFFNAW-FGLIVFLCMSLYLILTimvtewrAKFRRDMNTQENATR-------ARAVDSLLNFETVKYYNAE 469
Cdd:cd18564 140 LTLVGMLGvMFWLDWqLALIALAVAPLLLLAA-------RRFSRRIKEASREQRrregalaSVAQESLSAIRVVQAFGRE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 470 GYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGT 549
Cdd:cd18564 213 EHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAK 292
|
....*
gi 1958800879 550 YYRMI 554
Cdd:cd18564 293 LTGRI 297
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
590-752 |
3.86e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqisLRshIGVV 669
Cdd:PRK09544 5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLfNDTIANNI-RYGRVTAGDSEIQAAAQAAGIHDA-ILSFPEGyetqvgerglKLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK09544 73 PQKLYL-DTTLPLTVnRFLRLRPGTKKEDILPALKRVQAGhLIDAPMQ----------KLSGGETQRVLLARALLNRPQL 141
|
....*
gi 1958800879 748 ILLDE 752
Cdd:PRK09544 142 LVLDE 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
603-752 |
3.96e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.27 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDgqdisqvtqislRShIGVVPQDTVLFNDTIAN 682
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 683 NIRYGrvtagDSEiqaaaQAAGIHDAI---------LSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PTZ00243 740 NILFF-----DEE-----DAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
602-752 |
4.41e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGvvPQDTVLFNDTIA 681
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 682 NNIRYGRVTAGDSEiqaaaqaAGIHDAILSF--------PEGYetqvgerglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK13539 92 ENLEFWAAFLGGEE-------LDIAAALEAVglaplahlPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
606-752 |
4.64e-13 |
|
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: 68.23 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-VTQISLRSHIGVVPQD---TVLFND-TI 680
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIAYVPEDrkrEGLVLDlSV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800879 681 ANNIrygrvtagdseiqaaaqaagihdAILSFpegyetqvgerglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03215 96 AENI-----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDE 130
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
589-752 |
9.23e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGV 668
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFNDTIAnniryGRVTAGDSEIQAAAQaagihdAILSFPEGYETQVGE-RGLKLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK10522 402 VFTDFHLFDQLLG-----PEGKPANPALVEKWL------ERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470
|
....*
gi 1958800879 748 ILLDE 752
Cdd:PRK10522 471 LLLDE 475
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
590-752 |
1.21e-12 |
|
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: 66.41 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIridgqdisqvtQISLRSHIGVV 669
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFNDTIANNIRY--GRVtagdseiqaaaqaagihdailsfpegyetqvgerglkLSGGEKQRVAIARTILKAPDI 747
Cdd:cd03223 70 PQRPYLPLGTLREQLIYpwDDV-------------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
....*
gi 1958800879 748 ILLDE 752
Cdd:cd03223 113 VFLDE 117
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
603-752 |
1.30e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGciridgqdisqvTQISLRSHIGVVPQDTVLFNDTIAN 682
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD------------ASVVIRGTVAYVPQVSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 683 NIRYG------------RVTAGDseiqaaaqaagiHDAILsFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILL 750
Cdd:PLN03130 698 NILFGspfdperyeraiDVTALQ------------HDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
..
gi 1958800879 751 DE 752
Cdd:PLN03130 765 DD 766
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
588-752 |
1.42e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISqvtqislrshi 666
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 gVVPQDTVLFNDTIANNIRYGRVTA--GDSEIQAAAQAAGIHDAILSFpegyeTQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:COG4178 430 -FLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHK 503
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:COG4178 504 PDWLFLDE 511
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
606-752 |
1.54e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKST----ILRLLfrfydISSGCIRIDGQDISQVTQ---ISLRSHIGVVPQD------ 672
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRrqlLPVRHRIQVVFQDpnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 ---TVLfnDTIANNIRygrvtagdseiqaaaqaagIHDAILSfPEGYETQV----GERGL----------KLSGGEKQRV 735
Cdd:PRK15134 377 prlNVL--QIIEEGLR-------------------VHQPTLS-AAQREQQViavmEEVGLdpetrhrypaEFSGGQRQRI 434
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:PRK15134 435 AIARALILKPSLIILDE 451
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
329-533 |
1.98e-12 |
|
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: 68.63 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 329 LRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RIVDrgTSSVTGLLSYLVFN-IIPTLADIIIGIIYFs 406
Cdd:cd18570 61 IRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIIsRFND--ANKIREAISSTTISlFLDLLMVIISGIILF- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 407 mFFNAWFGLIVFLCMSLYLILTIMVTE-WRAKFRRDMntQENA-TRARAVDSLLNFETVKYYNAEGYELERYREAILKFQ 484
Cdd:cd18570 138 -FYNWKLFLITLLIIPLYILIILLFNKpFKKKNREVM--ESNAeLNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLL 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958800879 485 glewKSTASLVLLNQTQNMVIGFGLLAGSLL----CAYFVSERRLQVGDFVLF 533
Cdd:cd18570 215 ----KKSFKLGKLSNLQSSIKGLISLIGSLLilwiGSYLVIKGQLSLGQLIAF 263
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
590-752 |
2.66e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.12 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----IS 661
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEiqaaaqaagiHDAILSFPE-----GYETQVGERG-LKLSGGEKQ 733
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE----------EDAKQKAREmielvGLPEELLARSpFELSGGQMR 152
|
170
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDE 171
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
606-754 |
3.36e-12 |
|
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: 70.32 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQdisqvtqislrshIGVVPQDTVLFNDTIANNIR 685
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 686 YGrVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:TIGR01271 509 FG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
277-556 |
4.22e-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: 67.56 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 277 ALNVLVPIFYRDIVNLLT-SKAPWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNlrtflwiRVQQFTSRGVELRLFSHLHE 355
Cdd:cd18778 13 LLGLVPPWLIRELVDLVTiGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNH-------VAEQKVVADLRSDLYDKLQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 356 LSLRWHLGRRTGEVL-RIVDrGTSSVTGLLSYLVFNIIPT-LADIIIGIIYFSMffNAWFGLIVFLCMSLYLILTIMVTE 433
Cdd:cd18778 86 LSLRYFDDRQTGDLMsRVIN-DVANVERLIADGIPQGITNvLTLVGVAIILFSI--NPKLALLTLIPIPFLALGAWLYSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 434 W-RAKFRR------DMNtqenatrARAVDSLLNFETVKYYNAEGYELER-------YREAILK--------FQGLEWKST 491
Cdd:cd18778 163 KvRPRYRKvrealgELN-------ALLQDNLSGIREIQAFGREEEEAKRfealsrrYRKAQLRamklwaifHPLMEFLTS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958800879 492 ASLVLlnqtqnmVIGFGllagsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQT 556
Cdd:cd18778 236 LGTVL-------VLGFG--------GRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQR 285
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
590-752 |
5.03e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-----SGCIRIDGQDI--SQVTQISL 662
Cdd:PRK14267 5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 RSHIGVV-----PQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAaGIHDAILSfpEGYETQVGERGLKLSGGEKQRVAI 737
Cdd:PRK14267 84 RREVGMVfqypnPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEW-ALKKAALW--DEVKDRLNDYPSNLSGGQRQRLVI 160
|
170
....*....|....*
gi 1958800879 738 ARTILKAPDIILLDE 752
Cdd:PRK14267 161 ARALAMKPKILLMDE 175
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
597-752 |
1.01e-11 |
|
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: 65.98 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 597 FSYADGRET-LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---LRSHIGVVPQD 672
Cdd:TIGR02769 17 LFGAKQRAPvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 TV-LFN------DTIANNIR-YGRVTAGDSE--IQAAAQAAGIHDAILSfpegyetqvgERGLKLSGGEKQRVAIARTIL 742
Cdd:TIGR02769 97 SPsAVNprmtvrQIIGEPLRhLTSLDESEQKarIAELLDMVGLRSEDAD----------KLPRQLSGGQLQRINIARALA 166
|
170
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:TIGR02769 167 VKPKLIVLDE 176
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
263-561 |
1.07e-11 |
|
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: 66.32 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 263 LTVLLCMGLMGldrALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQgggTGSTGFVSNLRTFLWIRVQQFTS 342
Cdd:cd18549 5 FLDLFCAVLIA---ALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILR---TLLNYFVTYWGHVMGARIETDMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 343 RgvelRLFSHLHELSLRWHLGRRTGEVL-RIVDrGTSSVTGLLSY----LVFNIIptladIIIGIIYFSMFFNAWFGLIV 417
Cdd:cd18549 79 R----DLFEHLQKLSFSFFDNNKTGQLMsRITN-DLFDISELAHHgpedLFISII-----TIIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 418 FLCMSLYLILTImvtewraKFRRDMNTQENATR-------ARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKS 490
Cdd:cd18549 149 FALLPLMIIFTI-------YFNKKMKKAFRRVRekigeinAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958800879 491 -------TASLVLLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNwfgtyyRMIqtNFIDM 561
Cdd:cd18549 222 ykamayfFSGMNFFTNLLNLVV---LVAG----GYFIIKGEITLGDLVAFLLYVNVFIKPIR------RLV--NFTEQ 284
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
590-752 |
1.87e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-QISLRSHIGV 668
Cdd:PRK09700 6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLFND-TIANNIRYGRVTA----GDSEIQAAAQAagIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILK 743
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGRHLTkkvcGVNIIDWREMR--VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
....*....
gi 1958800879 744 APDIILLDE 752
Cdd:PRK09700 163 DAKVIIMDE 171
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
601-754 |
2.25e-11 |
|
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: 63.67 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTI 680
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 681 ANNIRYGRVTAGDSeiqaaaqaaGIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:cd03231 91 LENLRFWHADHSDE---------QVEEAL--------ARVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
598-752 |
2.45e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 598 SYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQISLRSHIGVVPQDTVL-F 676
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KDFNGEARPQPGIKVGYLPQEPQLdP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 677 NDTIANNI------------RYGRVTAG----DSEIQAAAQAAG-IHDAI------------------LSFPEGyETQVG 721
Cdd:TIGR03719 82 TKTVRENVeegvaeikdaldRFNEISAKyaepDADFDKLAAEQAeLQEIIdaadawdldsqleiamdaLRCPPW-DADVT 160
|
170 180 190
....*....|....*....|....*....|.
gi 1958800879 722 erglKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR03719 161 ----KLSGGERRRVALCRLLLSKPDMLLLDE 187
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
266-555 |
2.54e-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: 65.14 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 266 LLCMGLMGldrALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTgstgFVSNlrtFLWIRVQQFTSRGV 345
Cdd:cd18552 5 ILGMILVA---ATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLAS----YLQT---YLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 346 ELRLFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNIIptladIIIGIIYFSMFFNAWFGLIVFLCM 421
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDRNSSGDLIsRItndVNQVQNALTSALTVLVRDPL-----TVIGLLGVLFYLDWKLTLIALVVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 422 SLYLILTIMVTEwraKFRRDM-NTQENATR--ARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLN 498
Cdd:cd18552 150 PLAALPIRRIGK---RLRKISrRSQESMGDltSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 499 QTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:cd18552 227 PLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQ 283
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
603-752 |
2.71e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFY--DISSGCIRIDGQDISQVTQISlrshigvvpqDTVLFNDTI 680
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLI----------DAIGRKGDF 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958800879 681 ANNIRY-GRVtagdseiqaaaqaaGIHDAIL---SFPEgyetqvgerglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG2401 113 KDAVELlNAV--------------GLSDAVLwlrRFKE------------LSTGQKFRFRLALLLAERPKLLVIDE 162
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
268-555 |
4.47e-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: 64.43 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 268 CMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRGVEL 347
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQA-------VFSFFRIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 348 RLFSHLHELSLRWHLGRRTGEVL-RIvdrgTSSVTGLLSYLVFNI---IPTLADIIIGIIYfsMFFNAW-FGLIVFLCMS 422
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTsRL----SNDVTQIQDTLTTTLaefLRQILTLIGGVVL--LFFISWkLTLLMLATVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 423 LYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQtqn 502
Cdd:cd18576 148 VVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSS--- 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 503 mVIGFGLLAGSLLCAYF----VSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQ 555
Cdd:cd18576 225 -FIIFLLFGAIVAVLWYggrlVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQ 280
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
583-752 |
5.05e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 583 LRFHKGRVEFENVhfsyadgrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQIS 661
Cdd:PRK11288 5 LSFDGIGKTFPGV--------KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQDTVLFND-TIANNI-------RYGRVTAGD--SEIQAAAQAAGIH-DAilsfpegyETQVGErglkLSGG 730
Cdd:PRK11288 77 LAAGVAIIYQELHLVPEmTVAENLylgqlphKGGIVNRRLlnYEAREQLEHLGVDiDP--------DTPLKY----LSIG 144
|
170 180
....*....|....*....|..
gi 1958800879 731 EKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDE 166
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
277-545 |
5.78e-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: 64.35 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 277 ALNVLVPIFYRDIVNLLTSKAP------WSSLAWTVTTYVFLKFLqgggtgstGFVSN-LRTFLWIRVQQFTSRgvELR- 348
Cdd:cd18547 13 LLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLLGLYLL--------SALFSyLQNRLMARVSQRTVY--DLRk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 349 -LFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNIIptladIIIGIIYFsMFF-NAWFGLIVFLCMS 422
Cdd:cd18547 83 dLFEKLQRLPLSYFDTHSHGDIMsRVtndVDNISQALSQSLTQLISSIL-----TIVGTLIM-MLYiSPLLTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 423 LYLILTIMVTEW-RAKFRR------DMN--TQENATraravdsllNFETVKYYNAEGYELERYREAILKFQGLEWKSTAS 493
Cdd:cd18547 157 LSLLVTKFIAKRsQKYFRKqqkalgELNgyIEEMIS---------GQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958800879 494 LVLLNQTQNMV--IGFGLLAgsLLCAYFVSERRLQVGDFVLFGTYITQLYMPLN 545
Cdd:cd18547 228 SGLLMPIMNFInnLGYVLVA--VVGGLLVINGALTVGVIQAFLQYSRQFSQPIN 279
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
590-752 |
8.19e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.60 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYAD----GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQIS---- 661
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYEtqvgERGLKLSGGEKQRVAIAR 739
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWE----KSPFELSGGQMRRVAIAG 157
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK13643 158 ILAMEPEVLVLDE 170
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
277-544 |
9.30e-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: 63.58 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 277 ALNVLVPIFYRDIVNLLTSK-APWSSLAWTVTTYVFLKFLQGGGTgstgfvsnlrtFLWiRVQQF-TSRGVE--LR--LF 350
Cdd:cd18541 13 LLQLLIPRIIGRAIDALTAGtLTASQLLRYALLILLLALLIGIFR-----------FLW-RYLIFgASRRIEydLRndLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 351 SHLHELSLRWHLGRRTGEvlrIVDRGTSSVTGLLSYLVFNIIpTLADII---IGIIYFSMFFNAWFGLIVFLCMSLYLIL 427
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGD---LMARATNDLNAVRMALGPGIL-YLVDALflgVLVLVMMFTISPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 428 TIMVTEW-RAKFRR------DMN--TQENATRARavdsllnfeTVKYYNAEGYELERYREAILKFQglewKSTASLV--- 495
Cdd:cd18541 157 VYRLGKKiHKRFRKvqeafsDLSdrVQESFSGIR---------VIKAFVQEEAEIERFDKLNEEYV----EKNLRLArvd 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958800879 496 -LLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18541 224 aLFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPM 273
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
590-752 |
1.01e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.26 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADG----RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ----IS 661
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGdseIQAAAQAAGIHDAILSFpeGYETQVGERG-LKLSGGEKQRVAIA 738
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFK---MNLDEVKNYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:PRK13646 158 SILAMNPDIIVLDE 171
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
606-651 |
1.03e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 1.03e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDG 651
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
591-752 |
1.04e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.97 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfydissgciridgqdISQVTQISLRSHIG--- 667
Cdd:PRK11147 321 EMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM-----------------LGQLQADSGRIHCGtkl 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 -----------VVPQDTVLFNdtiannirygrVTAGDSEIqaaaQAAGIHDAILSF-------PEGYETQVGerglKLSG 729
Cdd:PRK11147 383 evayfdqhraeLDPEKTVMDN-----------LAEGKQEV----MVNGRPRHVLGYlqdflfhPKRAMTPVK----ALSG 443
|
170 180
....*....|....*....|...
gi 1958800879 730 GEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDE 466
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
593-752 |
1.21e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVtqislRSHIGVVPQD 672
Cdd:PRK11247 16 NAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 TVLFN-DTIANNIRYG-----RVTAgdseiqaaaqaagiHDAILSFpeGYETQVGERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGlkgqwRDAA--------------LQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:PRK11247 154 LLLLDE 159
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
601-752 |
1.49e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 61.10 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGqdisqvtqislRSHIGVVPQDTVL---FN 677
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 678 DTIANNIRYG---------RVTAGD-SEIQAAAQAAGIHDaiLSfpegyETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:NF040873 72 LTVRDLVAMGrwarrglwrRLTRDDrAAVDDALERVGLAD--LA-----GRQLGE----LSGGQRQRALLAQGLAQEADL 140
|
....*
gi 1958800879 748 ILLDE 752
Cdd:NF040873 141 LLLDE 145
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
269-551 |
1.61e-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: 62.56 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 269 MGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLqgggtgsTGFVSNLRTFLWIRVQQFTSRGVELR 348
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVL-------SGLFSGLRGGCFSYAGTRLVRRLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 349 LFSHLHELSLRWHLGRRTGEvlrIVDRGTS---SVTGLLSYLVFNIIPTLADIIIGIIYfsMFFNAWF-GLIVFLCMsly 424
Cdd:cd18572 75 LFRSLLRQDIAFFDATKTGE---LTSRLTSdcqKVSDPLSTNLNVFLRNLVQLVGGLAF--MFSLSWRlTLLAFITV--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 425 lILTIMVTEWRAKFRRDMNTQENATRAR----AVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKStASLVLLNQT 500
Cdd:cd18572 147 -PVIALITKVYGRYYRKLSKEIQDALAEanqvAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQ-ALAYAGYVA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958800879 501 QNMVIGFGLLAGSLL-CAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYY 551
Cdd:cd18572 225 VNTLLQNGTQVLVLFyGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVF 276
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
606-752 |
2.19e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVT-----------QISLRSHIGVV-PQDT 673
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdiQMVFQDSISAVnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 674 VlfNDTIANNIRYgrVTAGDSE-----IQAAAQAAGIHDAILSfpegyetqvgERGLKLSGGEKQRVAIARTILKAPDII 748
Cdd:PRK10419 108 V--REIIREPLRH--LLSLDKAerlarASEMLRAVDLDDSVLD----------KRPPQLSGGQLQRVCLARALAVEPKLL 173
|
....
gi 1958800879 749 LLDE 752
Cdd:PRK10419 174 ILDE 177
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
577-752 |
3.30e-10 |
|
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: 63.61 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 577 VPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD--- 653
Cdd:TIGR00954 439 VPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklf 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 654 -ISQVTQISLRSHigvvpQDTVLFNDTIANNIRYGrvtAGDSEIQAAAQAAGIHDaILSFPEGYETqVGERGLKLSGGEK 732
Cdd:TIGR00954 519 yVPQRPYMTLGTL-----RDQIIYPDSSEDMKRRG---LSDKDLEQILDNVQLTH-ILEREGGWSA-VQDWMDVLSGGEK 588
|
170 180
....*....|....*....|
gi 1958800879 733 QRVAIARTILKAPDIILLDE 752
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDE 608
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
263-558 |
3.62e-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: 61.71 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 263 LTVLLCMGLMGldrALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQgggtgstgFVSNlrtFLWIRVQQFTS 342
Cdd:cd18545 3 LLALLLMLLST---AASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVN--------WVAS---RLRIYLMAKVG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 343 RGV--ELR--LFSHLHELSLRWHLGRRTGEVL-RIV-DrgTSSVTGLLSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLI 416
Cdd:cd18545 69 QRIlyDLRqdLFSHLQKLSFSFFDSRPVGKILsRVInD--VNSLSDLLSNGLINLIPDLL-TLVGIVIIMFSLNVRLALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 417 VFLCMSLyLILTIMVTEWRAK--FRR------DMNT--QENATRARavdsllnfeTVKYYNAEGYELERYREAILKFQGl 486
Cdd:cd18545 146 TLAVLPL-LVLVVFLLRRRARkaWQRvrkkisNLNAylHESISGIR---------VIQSFAREDENEEIFDELNRENRK- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800879 487 EWKSTASLV-LLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNF 558
Cdd:cd18545 215 ANMRAVRLNaLFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAM 287
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
590-752 |
3.66e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.64 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRET-----LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI-SLR 663
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 664 SHIGVVPQ--DTVLFNDTIANNIRYGRVTAG--DSEIQAAAqaagihDAILSFPEGYETQVGERGLkLSGGEKQRVAIAR 739
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGPENLGipPEEIRERV------DESLKKVGMYEYRRHAPHL-LSGGQKQRVAIAG 157
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK13633 158 ILAMRPECIIFDE 170
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
606-752 |
3.79e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI---SLRSHIGVVPQDTVLFNDTian 682
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQDPYASLDP--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 683 nirygRVTAGDSeIQAAAQAAGIHDAilsfpEGYETQVG---ER-GLK----------LSGGEKQRVAIARTILKAPDII 748
Cdd:PRK10261 417 -----RQTVGDS-IMEPLRVHGLLPG-----KAAAARVAwllERvGLLpehawrypheFSGGQRQRICIARALALNPKVI 485
|
....
gi 1958800879 749 LLDE 752
Cdd:PRK10261 486 IADE 489
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
604-752 |
4.48e-10 |
|
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: 60.42 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQvTQISLRSHIGVV------------PQ 671
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgqktqlwwdlpVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 DTVLFNDTIAnNIRYGRVTAGDSEIQaaaqaagihdAILSFPEGYETQVgeRglKLSGGEKQRVAIARTILKAPDIILLD 751
Cdd:cd03267 114 DSFYLLAAIY-DLPPARFKKRLDELS----------ELLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLD 178
|
.
gi 1958800879 752 E 752
Cdd:cd03267 179 E 179
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
593-752 |
6.25e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.57 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 593 ENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQ- 671
Cdd:PRK10575 15 RNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 ----DTVLFNDTIANNiRY------GRVTAGDSEiqaaaqaaGIHDAIlsfpegyeTQVGERGL------KLSGGEKQRV 735
Cdd:PRK10575 94 lpaaEGMTVRELVAIG-RYpwhgalGRFGAADRE--------KVEEAI--------SLVGLKPLahrlvdSLSGGERQRA 156
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDE 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
606-752 |
6.67e-10 |
|
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: 59.85 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSHIGVVPQDTVLfndtiaNNIR 685
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-----LLGLGGGFNPELTGR------ENIY 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958800879 686 -----YGRVTAGDSEIQaaaqaagihDAILSFPE-G--YETQVGErglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03220 107 lngrlLGLSRKEIDEKI---------DEIIEFSElGdfIDLPVKT----YSSGMKARLAFAIATALEPDILLIDE 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
590-752 |
6.87e-10 |
|
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: 62.26 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRI-DGQDISQVTQislrSHIGV 668
Cdd:TIGR03719 323 IEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ----SRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQDTVLfnDTIANNIRYGRVtaGDSEIQAAaqaagihdAILS---FpEGYETQ--VGErglkLSGGEKQRVAIARTILK 743
Cdd:TIGR03719 398 DPNKTVW--EEISGGLDIIKL--GKREIPSR--------AYVGrfnF-KGSDQQkkVGQ----LSGGERNRVHLAKTLKS 460
|
....*....
gi 1958800879 744 APDIILLDE 752
Cdd:TIGR03719 461 GGNVLLLDE 469
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
603-752 |
7.38e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKS----TILRLLFR---FYdiSSGCIRIDGQDISQVTQISLR----SHIGVVPQ 671
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY--PSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 D-TVLFN--DTIANNI-------RYGRVTAGDSEIQAAAQAAGIHDA---ILSFPEgyetqvgerglKLSGGEKQRVAIA 738
Cdd:PRK15134 100 EpMVSLNplHTLEKQLyevlslhRGMRREAARGEILNCLDRVGIRQAakrLTDYPH-----------QLSGGERQRVMIA 168
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:PRK15134 169 MALLTRPELLIADE 182
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
604-752 |
1.06e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFY--DISSGC-IRIDGQDISQVTQISL-----RSHIGVVPQDTVL 675
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREGRLARdirksRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 676 FND-TIANNIRYGRV--TAGDSEIQAAAQAAGIHDAILSFpegyeTQVG------ERGLKLSGGEKQRVAIARTILKAPD 746
Cdd:PRK09984 98 VNRlSVLENVLIGALgsTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:PRK09984 173 VILADE 178
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
601-752 |
1.58e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.08 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRetLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDiSSGCIRIDGQDISQVTQISLRSHIGVVPQDTV------ 674
Cdd:COG4138 9 AGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 675 ------LFNDTIANnirygrVTAGDSEIQAAAQAAGIHDAilsfpegYETQVGerglKLSGGEKQRVAIARTILKA-PDI 747
Cdd:COG4138 86 vfqylaLHQPAGAS------SEAVEQLLAQLAEALGLEDK-------LSRPLT----QLSGGEWQRVRLAAVLLQVwPTI 148
|
170
....*....|.
gi 1958800879 748 ------ILLDE 752
Cdd:COG4138 149 npegqlLLLDE 159
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
277-548 |
1.61e-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: 59.80 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 277 ALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTGstgfvsnLRTFLWIRVQQFTSRGVELRLFSHLHEL 356
Cdd:cd18543 13 LAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSF-------LRRYLAGRLSLGVEHDLRTDLFAHLQRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 357 SLRWHLGRRTGEVLrivDRGTS---SVTGLLSYLVFNIIPTLADIIIGIIYFSMffNAWFGLIVFLCMSLYLILTimvte 433
Cdd:cd18543 86 DGAFHDRWQSGQLL---SRATSdlsLVQRFLAFGPFLLGNLLTLVVGLVVMLVL--SPPLALVALASLPPLVLVA----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 434 wrAKFRRDMNT------QENATRARAVD-SLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIG 506
Cdd:cd18543 156 --RRFRRRYFPasrraqDQAGDLATVVEeSVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958800879 507 FGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFG 548
Cdd:cd18543 234 LGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
604-752 |
1.83e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.21 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQV------------TQI-SLRSHIGVVP 670
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadkNQLrLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 671 QDTVLFND-TIANNIRYGRVtagdsEIQAAAQAAGIHDAILsfpegYETQVG--ERG-----LKLSGGEKQRVAIARTIL 742
Cdd:PRK10619 99 QHFNLWSHmTVLENVMEAPI-----QVLGLSKQEARERAVK-----YLAKVGidERAqgkypVHLSGGQQQRVSIARALA 168
|
170
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:PRK10619 169 MEPEVLLFDE 178
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
589-752 |
2.33e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYadGRETL-QDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIG 667
Cdd:PRK10253 7 RLRGEQLTLGY--GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFND-TIANNIRYGRV----------TAGDSEIQAAAQAAGIHDAILsfpEGYETqvgerglkLSGGEKQRVA 736
Cdd:PRK10253 85 LLAQNATTPGDiTVQELVARGRYphqplftrwrKEDEEAVTKAMQATGITHLAD---QSVDT--------LSGGQRQRAW 153
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:PRK10253 154 IAMVLAQETAIMLLDE 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
588-752 |
2.37e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYADGR----ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSG-------CIRIDGQDISQ 656
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 657 VTQisLRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDaILSFPEGYetqVGERGLKLSGGEKQR 734
Cdd:PRK13645 85 VKR--LRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLK-LVQLPEDY---VKRSPFELSGGQKRR 158
|
170
....*....|....*...
gi 1958800879 735 VAIARTILKAPDIILLDE 752
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDE 176
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
595-752 |
3.42e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 595 VHFSYADGR-------ETLQ---DVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS 664
Cdd:PRK15079 16 VHFDIKDGKqwfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 665 higvVPQD-TVLFNDTIAN-NiryGRVTAGDSeiqaaaqaagIHDAILSF-PEGYETQVGER--------GL-------- 725
Cdd:PRK15079 96 ----VRSDiQMIFQDPLASlN---PRMTIGEI----------IAEPLRTYhPKLSRQEVKDRvkammlkvGLlpnlinry 158
|
170 180
....*....|....*....|....*....
gi 1958800879 726 --KLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK15079 159 phEFSGGQCQRIGIARALILEPKLIICDE 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
589-749 |
4.43e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ--VTQIsLRSHI 666
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsPRER-RRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 667 GVVPQD-----TVLfNDTIANNI---RYGRvtagdseiqAAAQAAGIHD--AILSF-----------PEGYETQVGergl 725
Cdd:COG3845 336 AYIPEDrlgrgLVP-DMSVAENLilgRYRR---------PPFSRGGFLDrkAIRAFaeelieefdvrTPGPDTPAR---- 401
|
170 180
....*....|....*....|....
gi 1958800879 726 KLSGGEKQRVAIARTILKAPDIIL 749
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLI 425
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
265-545 |
5.49e-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: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGgtgstgfVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASAL-------LGVVQTYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 345 VELRLFSHLHELSLRWHLGRRTGEVL-RI---VDRGTSSVTGLLSYLVFNIIPTLADIIIgiiyfsMFFNAW-FGLIVFL 419
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQsRLnndVGGAQSVVTGTLTSVVSNVVTLVATLVA------MLALDWrLALLSLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 420 CMSLYLILTIMVTEWRAKFRRDmnTQE-NATRARAVDSLLN---FETVKYYNAEGYELERYREAILKFQGLEWKStaslV 495
Cdd:cd18550 148 LLPLFVLPTRRVGRRRRKLTRE--QQEkLAELNSIMQETLSvsgALLVKLFGREDDEAARFARRSRELRDLGVRQ----A 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958800879 496 LLNQTQNMVIGFGLLAGS----LLCAYFVSERRLQVGDFVLFGTYITQLYMPLN 545
Cdd:cd18550 222 LAGRWFFAALGLFTAIGPalvyWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLT 275
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
609-752 |
5.58e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 609 VSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISqvtqiSLRSH----IGVVP--QDTVLFND-TIA 681
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-----GLPGHqiarMGVVRtfQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 682 NNI---RYGRVTAgdseiqaaaqaaGIHDAILSFPeGY---ETQVGER--------GLK---------LSGGEKQRVAIA 738
Cdd:PRK11300 99 ENLlvaQHQQLKT------------GLFSGLLKTP-AFrraESEALDRaatwlervGLLehanrqagnLAYGQQRRLEIA 165
|
170
....*....|....
gi 1958800879 739 RTILKAPDIILLDE 752
Cdd:PRK11300 166 RCMVTQPEILMLDE 179
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
599-752 |
7.38e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 599 YADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRllfrfydISSGcirIDgQDISQVTQISLRSHIGVVPQD------ 672
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD-KEFEGEARPAPGIKVGYLPQEpqldpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 -TVLFN------DTIANNIRYGRVTAG------------------------------DSEIQAAAqaagihDAiLSFPEG 715
Cdd:PRK11819 85 kTVRENveegvaEVKAALDRFNEIYAAyaepdadfdalaaeqgelqeiidaadawdlDSQLEIAM------DA-LRCPPW 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958800879 716 yETQVGerglKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11819 158 -DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDE 189
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
606-752 |
8.08e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.94 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILR-----LLFRFYDISSGCIRIdGQDISQVTQIS------------LRSHIGV 668
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYI-GDKKNNHELITnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQ------AAGIHDAILsfpegyetqvgERG-LKLSGGEKQRVAIAR 739
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLakfylnKMGLDDSYL-----------ERSpFGLSGGQKRRVAIAG 189
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK13631 190 ILAIQPEILIFDE 202
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
263-556 |
1.36e-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: 56.67 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 263 LTVLLCMGLMGldRALNVLVPIFYRDIVNLLTSKAP-WSSLAWTVTTYVFLKFLQGGGT---GSTG--FVSNLRTflwir 336
Cdd:cd18551 1 LILALLLSLLG--TAASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSyllGRTGerVVLDLRR----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 337 vqqftsrgvelRLFSHLHELSLRWHLGRRTGEVL-RIVdrgtsSVTGLLSYLVFNIIPTLAD---IIIGIIYFSMFFNAW 412
Cdd:cd18551 74 -----------RLWRRLLRLPVSFFDRRRSGDLVsRVT-----NDTTLLRELITSGLPQLVTgvlTVVGAVVLMFLLDWV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 413 FGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTA 492
Cdd:cd18551 138 LTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAK 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800879 493 SLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQT 556
Cdd:cd18551 218 IEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQK 281
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
597-752 |
1.61e-08 |
|
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: 56.26 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 597 FSYADGRETLQDVSFTVMPG-----QTVALVGPSGAGKSTILRLLfrfydisSGCIRIDGQDISqvtqislrshigvvpq 671
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIE---------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 dtvLFNDTIANNIRY------GRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAP 745
Cdd:cd03237 58 ---IELDTVSYKPQYikadyeGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDA 134
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:cd03237 135 DIYLLDE 141
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
590-687 |
2.08e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTqiSLRSH---I 666
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHqlgI 88
|
90 100
....*....|....*....|..
gi 1958800879 667 GVVPQDTVLF-NDTIANNIRYG 687
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFG 110
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
602-752 |
2.22e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.70 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISL---------RSHIGVV--- 669
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVhqh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFNDTIANNI----------RYGRV--TAGD----SEIQAAAqaagIHDAILSFpegyetqvgerglklSGGEKQ 733
Cdd:PRK11701 98 PRDGLRMQVSAGGNIgerlmavgarHYGDIraTAGDwlerVEIDAAR----IDDLPTTF---------------SGGMQQ 158
|
170
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDE 177
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
584-752 |
2.57e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 584 RFHKGRVEFE----------NVHFSYADGRETLQDVSFTVMPGQ-----TVALVGPSGAGKSTILRLLfrfydisSGCIR 648
Cdd:PRK13409 318 RIRPEPIEFEerpprdeserETLVEYPDLTKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLL-------AGVLK 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 649 IDGQDISQVTQISLR-SHIGVVPQDTV-LFNDTIANNIrygrvtaGDS----EIQAAaqaagihdaiLSFPEGYETQVGE 722
Cdd:PRK13409 391 PDEGEVDPELKISYKpQYIKPDYDGTVeDLLRSITDDL-------GSSyyksEIIKP----------LQLERLLDKNVKD 453
|
170 180 190
....*....|....*....|....*....|
gi 1958800879 723 rglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK13409 454 ----LSGGELQRVAIAACLSRDADLYLLDE 479
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
606-669 |
2.60e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 2.60e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfYDI---SSGCIRIDGQDISQvTQISLRSHIGVV 669
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKML---TGIlvpTSGEVRVLGYVPFK-RRKEFARRIGVV 100
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
603-752 |
2.65e-08 |
|
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: 54.56 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS--SGCIRIDGQDIsqvtQISLRSHIGVVPQdtvlfNDti 680
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQRSTGYVEQ-----QD-- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800879 681 annirygrvtagdseiqaaaqaagIHDAILSFPEGYETQVGERGLKLSggEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03232 89 ------------------------VHSPNLTVREALRFSALLRGLSVE--QRKRLTIGVELAAKPSILFLDE 134
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
602-752 |
2.70e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQISLRSHIGVVPQDTVLF-NDT 679
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIpQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 680 IANNIRYGRvtagdsEIqaaAQAAGIHD------------AILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDI 747
Cdd:PRK10762 96 IAENIFLGR------EF---VNRFGRIDwkkmyaeadkllARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
....*
gi 1958800879 748 ILLDE 752
Cdd:PRK10762 163 IIMDE 167
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
594-752 |
2.76e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 594 NVHFSYAdGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGC-----IRIDGQDISQVTQI-SLRSHIG 667
Cdd:PRK14271 26 NLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVLFNDTIANNIRYGrVTAgdSEIQAAAQAAGIHDAILS---FPEGYETQVGERGLKLSGGEKQRVAIARTILKA 744
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAG-VRA--HKLVPRKEFRGVAQARLTevgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:PRK14271 182 PEVLLLDE 189
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
277-538 |
2.85e-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: 56.03 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 277 ALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTSRGVELRLFSHLHEL 356
Cdd:cd18557 10 AAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQS-------VFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 357 SLRWHLGRRTGEvlrIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYF-SMFFNAW-FGLIVFLCMSLYLILTIMVTEW 434
Cdd:cd18557 83 EIAFFDKHKTGE---LTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLiILFILSWkLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 435 RAKFRRDMntQENATRARAV--DSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAG 512
Cdd:cd18557 160 IRKLSKEV--QDALAKAGQVaeESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260
....*....|....*....|....*....
gi 1958800879 513 SLLCAYFVSERRLQVGD---FVLFGTYIT 538
Cdd:cd18557 238 LWYGGYLVLSGQLTVGEltsFILYTIMVA 266
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
605-752 |
3.45e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 605 TLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-------------VTQisLRSHIGVVPQ 671
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTE--ERRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 672 DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLD 751
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLD 416
|
.
gi 1958800879 752 E 752
Cdd:PRK10982 417 E 417
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
590-753 |
4.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.99 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQI-SLRSHIGV 668
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLqGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 669 VPQ--DTVLFNDTIANNIRYG--RVTAGDSEIQAAAqaagihDAILSfpegyETQVGE---RGLK-LSGGEKQRVAIART 740
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRV------DRALA-----EIGLEKyrhRSPKtLSGGQGQCVALAGI 150
|
170
....*....|...
gi 1958800879 741 ILKAPDIILLDEL 753
Cdd:PRK13644 151 LTMEPECLIFDEV 163
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
348-544 |
6.39e-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: 54.73 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIiptLADIIIGIIYFS-MFFnawfgLIVFLCMSLYLI 426
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNI---WLDMITIIIAICiMLV-----LNPKLTFVSLVI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 427 LTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFE------TVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQT 500
Cdd:cd18554 156 FPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHEriqgmsVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSA 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958800879 501 QNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18554 236 VNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPL 279
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
602-752 |
6.65e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIsQVTQISLRSHIGVVPQDTVLFND-TI 680
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTV 1020
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958800879 681 ANNIRYGRVTAGDS------EIQAAAQAAGIHDailsfpegyetQVGERGLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR01257 1021 AEHILFYAQLKGRSweeaqlEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
590-752 |
6.78e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIdGQ--DISQVTQislrSHIG 667
Cdd:PRK11819 325 IEAENLSKSFGD-RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVDQ----SRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPQDTVlF------NDTIannirygrvTAGDSEIQAAaqaagihdAILS---FpEGYETQ--VGErglkLSGGEKQRVA 736
Cdd:PRK11819 399 LDPNKTV-WeeisggLDII---------KVGNREIPSR--------AYVGrfnF-KGGDQQkkVGV----LSGGERNRLH 455
|
170
....*....|....*.
gi 1958800879 737 IARTILKAPDIILLDE 752
Cdd:PRK11819 456 LAKTLKQGGNVLLLDE 471
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
398-544 |
7.03e-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: 54.71 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 398 IIIGIIYFSMFFNAWFGLIVFLCMSLyLILTIMVTEWRA--KFRR------DMN--TQENATRARavdsllnfeTVKYYN 467
Cdd:cd18548 126 MLIGAIIMAFRINPKLALILLVAIPI-LALVVFLIMKKAipLFKKvqkkldRLNrvVRENLTGIR---------VIRAFN 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 468 AEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18548 196 REDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
590-752 |
7.28e-08 |
|
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: 55.58 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL--FRFYDISSG-----------CIRIDGQdiSQ 656
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekCGYVERP--SK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 657 VTQISLRSHIGVVPQDTVLFN--DTIANNIR------YGRVTA--GDSEIqaaaqaagIHDAILSFPE-GYE-------- 717
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWNlsDKLRRRIRkriaimLQRTFAlyGDDTV--------LDNVLEALEEiGYEgkeavgra 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958800879 718 ------TQVGER----GLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR03269 150 vdliemVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADE 194
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
295-548 |
8.25e-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: 54.49 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 295 SKAPWSSLAWTVTT----YVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL 370
Cdd:cd18565 35 SFLPLVPASLGPADprgqLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 371 RIVDRGTSSVTGLLSYLVFNIIPTLADII-IGIIYFSMffNAWFGLIVFLCMSLYLILTIMVTEW-RAKFRR------DM 442
Cdd:cd18565 115 SVLNNDVNQLERFLDDGANSIIRVVVTVLgIGAILFYL--NWQLALVALLPVPLIIAGTYWFQRRiEPRYRAvreavgDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 443 NtqenatrARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSE 522
Cdd:cd18565 193 N-------ARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLD 265
|
250 260 270
....*....|....*....|....*....|..
gi 1958800879 523 RR------LQVGDFVLFGTYITQLYMPLNWFG 548
Cdd:cd18565 266 GPplftgtLTVGTLVTFLFYTQRLLWPLTRLG 297
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
604-752 |
8.74e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 604 ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDG-------------------QDISqvTQISLRS 664
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqrirmifQDPS--TSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 665 HIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAaaqaagIHDAILSFPEgyetqvgerglKLSGGEKQRVAIARTILKA 744
Cdd:PRK15112 105 RISQILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPDHASYYPH-----------MLAPGQKQRLGLARALILR 167
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:PRK15112 168 PKVIIADE 175
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
606-752 |
9.03e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.32 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQD--------------------------ISQVTQ 659
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvleklviqktrfkkIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 660 IslRSHIGVVPQ--DTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDaILSFPEGYetqVGERGLKLSGGEKQRVAI 737
Cdd:PRK13651 103 I--RRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIE-LVGLDESY---LQRSPFELSGGQKRRVAL 176
|
170
....*....|....*
gi 1958800879 738 ARTILKAPDIILLDE 752
Cdd:PRK13651 177 AGILAMEPDFLVFDE 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
601-752 |
1.06e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDIsQVTQI--SLRSHIGVVPQDTVLF 676
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEEL-QASNIrdTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 677 ND-TIANNIRYGRvtagdsEIQaaaqaagiHDAILSFPEGY----------------ETQVGErglkLSGGEKQRVAIAR 739
Cdd:PRK13549 95 KElSVLENIFLGN------EIT--------PGGIMDYDAMYlraqkllaqlkldinpATPVGN----LGLGQQQLVEIAK 156
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:PRK13549 157 ALNKQARLLILDE 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
615-754 |
1.16e-07 |
|
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: 51.61 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 615 PGQTVALVGPSGAGKSTILRLLFRFYDISS-GCIRIDGQDISQVTQISLRshigvvpqdtvlfndtiannirygrvtagd 693
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958800879 694 seiqaaaqaagihdailsfpegyETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDELF 754
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEIT 88
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
265-544 |
1.20e-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: 54.03 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 265 VLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLkflqgggTGSTGFVSNLRTFLWIRVQQFTSRG 344
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAV-------VLAGWVAQRAQTRLTGRTGERLLYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 345 VELRLFSHLHELSLRWHLGRRTGevlRIVDRGTS---SVTGLLSY-LVFNIIPTLADIIIGIIYFSMffNAWFGLIVFLC 420
Cdd:cd18546 74 LRLRVFAHLQRLSLDFHERETSG---RIMTRMTSdidALSELLQTgLVQLVVSLLTLVGIAVVLLVL--DPRLALVALAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 421 mslyLILTIMVTEWrakFRRDMNTQENATRARAVDSLLNF-ET------VKYYNAEGYELER-------YREAILK---- 482
Cdd:cd18546 149 ----LPPLALATRW---FRRRSSRAYRRARERIAAVNADLqETlagirvVQAFRRERRNAERfaelsddYRDARLRaqrl 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958800879 483 ----FQGLEWKSTASLVLlnqtqnmVIGFGllagsllcAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18546 222 vaiyFPGVELLGNLATAA-------VLLVG--------AWRVAAGTLTVGVLVAFLLYLRRFFAPI 272
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
582-752 |
1.53e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 582 PLRFHK---GRVEFENVHFSYADGRETLQDVSFTVMPGQ-----TVALVGPSGAGKSTILRLLfrfydisSGCIRIDGQD 653
Cdd:COG1245 324 PIEFEVhapRREKEEETLVEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 654 ISQVTQISLRshigvvPQ----DtvlFNDTIANNIRYGRVTAGDSeiqaaaqaagihdailSFpegYETQVGER-GLK-- 726
Cdd:COG1245 397 VDEDLKISYK------PQyispD---YDGTVEEFLRSANTDDFGS----------------SY---YKTEIIKPlGLEkl 448
|
170 180 190
....*....|....*....|....*....|...
gi 1958800879 727 -------LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:COG1245 449 ldknvkdLSGGELQRVAIAACLSRDADLYLLDE 481
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
324-556 |
2.17e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 53.28 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 324 GFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RIvdrgtSSVTGLLSYLVFNIIPTLADIIIGI 402
Cdd:cd18555 56 GLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLfRA-----NSNVYIRQILSNQVISLIIDLLLLV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 403 IYFSM--FFNAWFGLIVFLCMSLYLILTIMVTewraKFRRDMNTQENATRARA----VDSLLNFETVKYYNAEGYE---- 472
Cdd:cd18555 131 IYLIYmlYYSPLLTLIVLLLGLLIVLLLLLTR----KKIKKLNQEEIVAQTKVqsylTETLYGIETIKSLGSEKNIykkw 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 473 LERYREAILKFQGLEwKSTASLVLLNQTQNMVIGFGLLagsLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYR 552
Cdd:cd18555 207 ENLFKKQLKAFKKKE-RLSNILNSISSSIQFIAPLLIL---WIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYN 282
|
....
gi 1958800879 553 MIQT 556
Cdd:cd18555 283 QFIL 286
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
324-539 |
3.16e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.59 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 324 GFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVL-RIVDRGTssvtgLLSYLVFNIIPTLADIIIGI 402
Cdd:cd18782 56 AVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELStRISELDT-----IRGFLTGTALTTLLDVLFSV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 403 IYFS-MFFNAWF-GLIVFLCMSLYLILTIMVT-----EWRAKFRRDMNTQenatrARAVDSLLNFETVKYYNAEGYELER 475
Cdd:cd18782 131 IYIAvLFSYSPLlTLVVLATVPLQLLLTFLFGpilrrQIRRRAEASAKTQ-----SYLVESLTGIQTVKAQNAELKARWR 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 476 YREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLF---GTYITQ 539
Cdd:cd18782 206 WQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFrilSGYVTG 272
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
609-752 |
3.19e-07 |
|
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: 53.65 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 609 VSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSG--CIRIdGQDISQVTQISL------RSHIGVVPQDTVLF-NDT 679
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRV-GDEWVDMTKPGPdgrgraKRYIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 680 IANNIRygrvtagdseiqaaaqaagihDAI-LSFPE--------------GYETQVGERGL-----KLSGGEKQRVAIAR 739
Cdd:TIGR03269 382 VLDNLT---------------------EAIgLELPDelarmkavitlkmvGFDEEKAEEILdkypdELSEGERHRVALAQ 440
|
170
....*....|...
gi 1958800879 740 TILKAPDIILLDE 752
Cdd:TIGR03269 441 VLIKEPRIVILDE 453
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
594-752 |
4.34e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.10 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 594 NVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ-----VTQISLRSH-IG 667
Cdd:PRK13540 6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyQKQLCFVGHrSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 VVPqdtvlfNDTIANNIRYG-RVTAGDSEIQAAAQAAGIhDAILSFPEGYetqvgerglkLSGGEKQRVAIARTILKAPD 746
Cdd:PRK13540 85 INP------YLTLRENCLYDiHFSPGAVGITELCRLFSL-EHLIDYPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
....*.
gi 1958800879 747 IILLDE 752
Cdd:PRK13540 148 LWLLDE 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
590-752 |
6.85e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLfrfydisSGciriDGQDISQVTQISLRSHIGVV 669
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------SG----ELQPSSGTVFRSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 670 PQDTVLFNDTIANNIRYgrvtagdseiqAAAQAAGIHDAILSFPEGYETQVGERGLK----LSGGEKQRVAIARTILKAP 745
Cdd:PLN03073 578 SQHHVDGLDLSSNPLLY-----------MMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKITFKKP 646
|
....*..
gi 1958800879 746 DIILLDE 752
Cdd:PLN03073 647 HILLLDE 653
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
589-752 |
1.35e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF-RFY--DISsGCIRIDGQ--DISQVTQ-ISL 662
Cdd:NF040905 259 EVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYgrNIS-GTVFKDGKevDVSTVSDaIDA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 663 --------RSHIGVVPQDTVLFNDTIANnirYGRVTAGdseiqaaaqaaGIHDailsfpEGYETQVGER----------- 723
Cdd:NF040905 338 glayvtedRKGYGLNLIDDIKRNITLAN---LGKVSRR-----------GVID------ENEEIKVAEEyrkkmniktps 397
|
170 180 190
....*....|....*....|....*....|...
gi 1958800879 724 ----GLKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:NF040905 398 vfqkVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
611-752 |
2.00e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 611 FTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQ---ISLRSHIGVVPQD-TVLFNDTIANNI-- 684
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsrfMAYLGHLPGLKADlSTLENLHFLCGLhg 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958800879 685 RYGRVTAGDSEiqaaaqaagihdAILSFPEGYETQVGErglkLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK13543 112 RRAKQMPGSAL------------AIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDE 163
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
601-752 |
2.94e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS--------SGCIRIDGQDISQVTQISLRSHIGVVPQD 672
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 TV-LFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPeGYETQVGERGLKLSGGEKQRVAIARTILK-------- 743
Cdd:PRK13547 92 AQpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170
....*....|
gi 1958800879 744 -APDIILLDE 752
Cdd:PRK13547 171 qPPRYLLLDE 180
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
583-752 |
3.22e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 583 LRF------HKGRVEFENVHFSYaDGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIridgqdisq 656
Cdd:PRK15064 307 IRFeqdkklHRNALEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 657 vtQISLRSHIGVVPQDTV--LFND-TIANNIRYGRvTAGDSEiqaaAQAAGIHDAILsFPegyETQVGERGLKLSGGEKQ 733
Cdd:PRK15064 377 --KWSENANIGYYAQDHAydFENDlTLFDWMSQWR-QEGDDE----QAVRGTLGRLL-FS---QDDIKKSVKVLSGGEKG 445
|
170
....*....|....*....
gi 1958800879 734 RVAIARTILKAPDIILLDE 752
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDE 464
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
606-752 |
3.27e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLfRFYDIS----SGCIRIDGQ--DISQVTQISlrshiGVVPQD------- 672
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMpiDAKEMRAIS-----AYVQQDdlfiptl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 673 TVLFNDTIANNIRYGRVTAGDSEIQAaaqaagIHDAI--LSFPEGYETQVGERGLK--LSGGEKQRVAIARTILKAPDII 748
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRER------VDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
....
gi 1958800879 749 LLDE 752
Cdd:TIGR00955 189 FCDE 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
602-688 |
3.38e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 602 GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQISLRSHIGVVPQD-TVLFNDT 679
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRS 89
|
....*....
gi 1958800879 680 IANNIRYGR 688
Cdd:PRK10982 90 VMDNMWLGR 98
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
265-555 |
3.82e-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: 49.31 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 265 VLLCMGLMGLDRALNVLVPIFYRDIVN--LLTSKAPWSSLAWTVTTYVFLKFLQGggtgstgFVSNLRTFLWIRVQQFTS 342
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLSF-------LLQYLQTYLLQKLGQRII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 343 RGVELRLFSHLHELSLRWHLGRRTGevlRIVDRGTS---SVTGLLSYLVFNIIptlADI--IIGIIYFSMFFNAWFGLIV 417
Cdd:cd18544 74 YDLRRDLFSHIQRLPLSFFDRTPVG---RLVTRVTNdteALNELFTSGLVTLI---GDLllLIGILIAMFLLNWRLALIS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 418 FLCMSLYLILTIMVTEW-RAKFRR------DMNT--QENatraravdsLLNFETVKYYNAEGYELER-------YREAIL 481
Cdd:cd18544 148 LLVLPLLLLATYLFRKKsRKAYREvreklsRLNAflQES---------ISGMSVIQLFNREKREFEEfdeinqeYRKANL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 482 K--------FQGLEWKSTASLVLlnqtqnmVIGFGllagsllcAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRM 553
Cdd:cd18544 219 KsiklfalfRPLVELLSSLALAL-------VLWYG--------GGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNI 283
|
..
gi 1958800879 554 IQ 555
Cdd:cd18544 284 LQ 285
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
329-544 |
3.94e-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: 49.42 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 329 LRTFLWIRVqqfTSR-GVEL--RLFSHLHELSLRWHLGRRTGEVL-RIvdRGTSSVTgllSYLVFNIIPTLADIIIGIIY 404
Cdd:cd18588 61 LRTYLFSHT---TNRiDAELgaRLFRHLLRLPLSYFESRQVGDTVaRV--RELESIR---QFLTGSALTLVLDLVFSVVF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 405 FS-MFFNAWF-GLIVFLCMSLYLILTIMVTewrAKFRRDMNTQ-ENATRARA--VDSLLNFETVKYYNAEGYELERYREA 479
Cdd:cd18588 133 LAvMFYYSPTlTLIVLASLPLYALLSLLVT---PILRRRLEEKfQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEEL 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 480 ILKFQglewKSTASLVLLNQTQNMVIGF--GLLAGSLLC--AYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18588 210 LARYV----KASFKTANLSNLASQIVQLiqKLTTLAILWfgAYLVMDGELTIGQLIAFNMLAGQVSQPV 274
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
591-668 |
5.27e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 591 EFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRF--YDISSGCIRIDGQDISQVTQiSLRSHIGV 668
Cdd:CHL00131 9 EIKNLHAS-VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEP-EERAHLGI 86
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
552-752 |
9.55e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 552 RMIQTNFIDMENMFDLLKEET--EVKDVpgagpLRFHKGRVefenvhfsyadgretlQDVSFTVMPGQTVALVGPSGAGK 629
Cdd:PRK09700 244 RELQNRFNAMKENVSNLAHETvfEVRNV-----TSRDRKKV----------------RDISFSVCRGEILGFAGLVGSGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 630 STILRLLFRFYDISSGCIRIDGQDISQVTQ-ISLRSHIGVVPQ---DTVLF-NDTIANNIrygrvtagdsEIQAAAQAAG 704
Cdd:PRK09700 303 TELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSIAQNM----------AISRSLKDGG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958800879 705 IHDAILSFPEGYETQVGERGLK---------------LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK09700 373 YKGAMGLFHEVDEQRTAENQREllalkchsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDE 435
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
588-752 |
1.04e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 588 GRVEFENVHFSYAD----GRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYD-ISSGCIRIDGQDIS-QVTQIS 661
Cdd:PRK13549 256 GEVILEVRNLTAWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 662 LRSHIGVVPQD----------TVLFNDTIANNIRYgrvtAGDSEIQAAAQAAGIHDAIL------SFPEgyeTQVGergl 725
Cdd:PRK13549 336 IAQGIAMVPEDrkrdgivpvmGVGKNITLAALDRF----TGGSRIDDAAELKTILESIQrlkvktASPE---LAIA---- 404
|
170 180
....*....|....*....|....*..
gi 1958800879 726 KLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDE 431
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
601-754 |
1.15e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRS------HIGVVPQDTV 674
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 675 LFNDTIANNIRyGRVTAGDseiqaaaqaagIHDAIlsfpegyeTQVGERGLK------LSGGEKQRVAIARTILKAPDII 748
Cdd:PRK13538 92 LENLRFYQRLH-GPGDDEA-----------LWEAL--------AQVGLAGFEdvpvrqLSAGQQRRVALARLWLTRAPLW 151
|
....*.
gi 1958800879 749 LLDELF 754
Cdd:PRK13538 152 ILDEPF 157
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
340-544 |
1.59e-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: 47.55 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 340 FTSRGVELRLFS----HLHELSLRWHLGRRTGEVL-RIVDRGTssvtgLLSYLVFNIIPTLADIIIGIIYFSMFF--NAW 412
Cdd:cd18568 68 YFANRIDLSLLSdfykHLLSLPLSFFASRKVGDIItRFQENQK-----IRRFLTRSALTTILDLLMVFIYLGLMFyyNLQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 413 FGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEgYEL-----ERYREAILK-FQGL 486
Cdd:cd18568 143 LTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAE-RPIrwrweNKFAKALNTrFRGQ 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 487 EWKSTASLV--LLNQTQNMVIgfgLLAGsllcAYFVSERRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18568 222 KLSIVLQLIssLINHLGTIAV---LWYG----AYLVISGQLTIGQLVAFNMLFGSVINPL 274
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
601-752 |
1.71e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.90 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 601 DGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQDI-SQVTQISLRSHIGVVPQDTVLFN 677
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 678 D-TIANNIRYG-RVTAGDSEIQAAAQAAGIHDAI--LSFPEGYETQ-VGERGlklsGGEKQRVAIARTILKAPDIILLDE 752
Cdd:TIGR02633 92 ElSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLreLQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
590-752 |
1.78e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 590 VEFENVHFSyADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF--RFYDISSGCIRIDGQDISQVTQiSLRSHIG 667
Cdd:PRK09580 2 LSIKDLHVS-VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSP-EDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 668 V---------VPQ-DTVLFNDTIANNIRYGRvtaGDSEIQAAAQAAGIHDAI--LSFPEGYETQVGERGlkLSGGEKQRV 735
Cdd:PRK09580 80 IfmafqypveIPGvSNQFFLQTALNAVRSYR---GQEPLDRFDFQDLMEEKIalLKMPEDLLTRSVNVG--FSGGEKKRN 154
|
170
....*....|....*..
gi 1958800879 736 AIARTILKAPDIILLDE 752
Cdd:PRK09580 155 DILQMAVLEPELCILDE 171
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
366-544 |
2.10e-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: 47.25 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 366 TGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQ 445
Cdd:cd18556 100 SGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLFVINNTIFTKKIVSLRNDLMDA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 446 ENATRARAVDSLLNFETVKYYNAEGYELERYREAILK---FQGLEWKSTASLVLLNQTQNmVIGFGLLAGSLLcaYFVSE 522
Cdd:cd18556 180 GRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNdrnSQKRYWKLTFKMLILNSLLN-VILFGLSFFYSL--YGVVN 256
|
170 180
....*....|....*....|..
gi 1958800879 523 RRLQVGDFVLFGTYITQLYMPL 544
Cdd:cd18556 257 GQVSIGHFVLITSYILLLSTPI 278
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
589-636 |
2.75e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 2.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958800879 589 RVEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL 636
Cdd:PRK10938 260 RIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
603-752 |
3.33e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLF-RFYDIS-SGCIRIDGQDISQvtQISLRshIGVVPQDTVLF---- 676
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK--QILKR--TGFVTQDDILYphlt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 677 -NDTI--ANNIRYGRVTAGDSEIQAAAQAAgihdAILSFPEGYETQVGERGLK-LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PLN03211 157 vRETLvfCSLLRLPKSLTKQEKILVAESVI----SELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
603-752 |
3.78e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDIS-SGCIRIDGQDISQVT-QISLRSHIGVVPQDT------- 673
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgivp 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 674 ---VLFNDTIANNIRYGRVTAGDSEIQAaaqaagihDAILSFPEGYETQVGERGL---KLSGGEKQRVAIARTILKAPDI 747
Cdd:TIGR02633 353 ilgVGKNITLSVLKSFCFKMRIDAAAEL--------QIIGSAIQRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRV 424
|
....*
gi 1958800879 748 ILLDE 752
Cdd:TIGR02633 425 LILDE 429
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
600-752 |
3.89e-05 |
|
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: 45.33 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 600 ADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL---FRFYDISSGCIRIDGQDISQVTQIslrshigvvPQDTVLF 676
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEK---------YPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 677 NdtiannirygrvTAGDseiqaaaqaagIHDAILSFPEGYETQVGERG----LKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03233 88 V------------SEED-----------VHFPTLTVRETLDFALRCKGnefvRGISGGERKRVSIAEALVSRASVLCWDN 144
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
609-752 |
3.91e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 609 VSFTVMPGQTVALVGPSGAGKSTilrLLFRFYDI--SSGCIRIDGQDISQVTQISLRSHIG-VVPQDTVLFNDTIannIR 685
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPV---FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 686 Y--------GRVTAGDSEIQAAAQAAGIHDAIlsfpegyETQVGErglkLSGGEKQRVAIARTILK-APDI------ILL 750
Cdd:PRK03695 89 YltlhqpdkTRTEAVASALNEVAEALGLDDKL-------GRSVNQ----LSGGEWQRVRLAAVVLQvWPDInpagqlLLL 157
|
..
gi 1958800879 751 DE 752
Cdd:PRK03695 158 DE 159
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
612-752 |
4.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 612 TVMPGQTVALVGPSGAGKSTILRLLfrfydisSGCIRIDgqdisqvtqisLRSHIGVVPQDTVL-----------FNDTI 680
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKIL-------SGELIPN-----------LGDYEEEPSWDEVLkrfrgtelqnyFKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 681 ANNIR------Y---------GRVtagdSEIQAAAQAAGIHDAILSFPEgyETQVGERGLK-LSGGEKQRVAIARTILKA 744
Cdd:PRK13409 157 NGEIKvvhkpqYvdlipkvfkGKV----RELLKKVDERGKLDEVVERLG--LENILDRDISeLSGGELQRVAIAAALLRD 230
|
....*...
gi 1958800879 745 PDIILLDE 752
Cdd:PRK13409 231 ADFYFFDE 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
594-752 |
1.34e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 594 NVHFSYADGR-ETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCI------------------------- 647
Cdd:PRK10261 19 NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 648 -RIDGQDISQVTQISLRSHIGVVPqdtvlFNDTIANNIRYGRVTAGDSEIQAAAQAAgihdAILSFPEGyETQVGERGLK 726
Cdd:PRK10261 99 rHVRGADMAMIFQEPMTSLNPVFT-----VGEQIAESIRLHQGASREEAMVEAKRML----DQVRIPEA-QTILSRYPHQ 168
|
170 180
....*....|....*....|....*.
gi 1958800879 727 LSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADE 194
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
601-659 |
2.21e-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: 2.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 601 DGRETLQDVsftvMPGQTVALVGPSGAGKSTILRLLFrfydissGCIRIDGQDISQVTQ 659
Cdd:cd01854 74 EGLDELREL----LKGKTSVLVGQSGVGKSTLLNALL-------PELVLATGEISEKLG 121
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
615-752 |
2.33e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 615 PGQTVALVGPSGAGKSTILRLL-----------------------FR-------FYDISSGCIRIdGQDISQVTQISlRS 664
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlkrFRgtelqdyFKKLANGEIKV-AHKPQYVDLIP-KV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 665 HIGVVpqdtvlfndtiannirygrvtagdSEIQAAAQAAGIHDAILSFPEgyETQVGERGLK-LSGGEKQRVAIARTILK 743
Cdd:COG1245 176 FKGTV------------------------RELLEKVDERGKLDELAEKLG--LENILDRDISeLSGGELQRVAIAAALLR 229
|
....*....
gi 1958800879 744 APDIILLDE 752
Cdd:COG1245 230 DADFYFFDE 238
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
615-650 |
2.46e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.15 E-value: 2.46e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1958800879 615 PGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRID 650
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVRED 229
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
348-526 |
2.61e-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: 43.81 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 348 RLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLAdIIIGIIYFSMFFNAWFGLIVFLCMSLYLIL 427
Cdd:cd18561 74 RLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALL-GPLLILIYLFFLDPLVALILLVFALLIPLS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 428 TIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQglewKSTASLVLLNQTQNMVIGF 507
Cdd:cd18561 153 PALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLR----QATMKVLAVSLLSSGIMGL 228
|
170
....*....|....*....
gi 1958800879 508 GLLAGSLLCAYFVSERRLQ 526
Cdd:cd18561 229 ATALGTALALGVGALRVLG 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
606-652 |
2.83e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 2.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISS--GCIRIDGQ 652
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE 65
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
590-656 |
3.98e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 3.98e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958800879 590 VEFENVHFSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQ 656
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD 67
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
597-752 |
4.18e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.07 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 597 FSYADgRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQ--DISQVTQISLRSHIGVVPQDTv 674
Cdd:PRK13638 9 FRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 675 lfndtiANNIRYgrvTAGDSEIQAAAQAAGIHDA-ILSFPEGYETQVGERGLK------LSGGEKQRVAIARTILKAPDI 747
Cdd:PRK13638 87 ------EQQIFY---TDIDSDIAFSLRNLGVPEAeITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARY 157
|
....*
gi 1958800879 748 ILLDE 752
Cdd:PRK13638 158 LLLDE 162
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
350-533 |
6.74e-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: 42.23 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 350 FSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGL-LSYLVFNiIPTLADIIIgIIYFSMFFNAWFGLIVFLCMSLYLILT 428
Cdd:cd18562 76 FEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLwLGFFREH-LAALVSLIV-LLPVALWMNWRLALLLVVLAAVYAALN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 429 IMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYN---AEGYELERYREAILKFQG--LEWKSTAS-LVLLNQTQN 502
Cdd:cd18562 154 RLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTrlaAETSALRGITRRLLAAQYpvLNWWALASvLTRAASTLT 233
|
170 180 190
....*....|....*....|....*....|.
gi 1958800879 503 MVIGFgllagsLLCAYFVSERRLQVGDFVLF 533
Cdd:cd18562 234 MVAIF------ALGAWLVQRGELTVGEIVSF 258
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
325-539 |
7.26e-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: 42.45 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 325 FVSNLRTFLWIRV-----QQFTSRgvelrLFSHLHELSLRWHLGRRTGEVL-RIvdrgtSSVTGLLSYLVFNIIPTLADI 398
Cdd:cd18567 57 LLSALRSWLVLYLstslnLQWTSN-----LFRHLLRLPLSYFEKRHLGDIVsRF-----GSLDEIQQTLTTGFVEALLDG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 399 IIGIIYFSM--FFNAWFGLIVFLCMSLYLILTImvtewrAKFRRDMNTQENATRARA------VDSLLNFETVKYYNAEG 470
Cdd:cd18567 127 LMAILTLVMmfLYSPKLALIVLAAVALYALLRL------ALYPPLRRATEEQIVASAkeqshfLETIRGIQTIKLFGREA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 471 YELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQ 539
Cdd:cd18567 201 EREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQ 269
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
597-752 |
1.28e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 597 FSYAdgrETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFR-------------------------------FYDISSG 645
Cdd:PRK11147 13 FSDA---PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqqdpprnvegtVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 646 CIRIDGQDISQVTQISLRshIGVVPQDTVLfNdtianniRYGRVTAG---------DSEIQAAAQAAGIH-DAILSfpeg 715
Cdd:PRK11147 90 GIEEQAEYLKRYHDISHL--VETDPSEKNL-N-------ELAKLQEQldhhnlwqlENRINEVLAQLGLDpDAALS---- 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958800879 716 yetqvgerglKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:PRK11147 156 ----------SLSGGWLRKAALGRALVSNPDVLLLDE 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
607-752 |
1.63e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.82 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 607 QDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDIS-QVTQISLRSHIGVVPQDT----VLFNDTIA 681
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDRkaegIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 682 NNI----RYGRVTAGdseiqaaaqaagihdAILSfpEGYETQVGERGLK---------------LSGGEKQRVAIARTIL 742
Cdd:PRK11288 350 DNInisaRRHHLRAG---------------CLIN--NRWEAENADRFIRslniktpsreqlimnLSGGNQQKAILGRWLS 412
|
170
....*....|
gi 1958800879 743 KAPDIILLDE 752
Cdd:PRK11288 413 EDMKVILLDE 422
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
725-752 |
2.04e-03 |
|
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: 39.86 E-value: 2.04e-03
10 20
....*....|....*....|....*...
gi 1958800879 725 LKLSGGEKQRVAIARTILKAPDIILLDE 752
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDE 97
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
601-636 |
2.27e-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: 2.27e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1958800879 601 DGRETLQDVsftvMPGQTVALVGPSGAGKSTILRLL 636
Cdd:pfam03193 95 EGIEALKEL----LKGKTTVLAGQSGVGKSTLLNAL 126
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
603-636 |
3.23e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 3.23e-03
10 20 30
....*....|....*....|....*....|....
gi 1958800879 603 RETLQDVSFTVMPGQTVALVGPSGAGKSTILRLL 636
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALL 47
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
366-480 |
4.28e-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: 40.13 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 366 TGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYfsMFFNAW-FGLIVFLCMSLYLILTIMVTEWRAKF-RRDMN 443
Cdd:cd18578 110 TGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLII--AFVYGWkLALVGLATVPLLLLAGYLRMRLLSGFeEKNKK 187
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958800879 444 TQENATRaRAVDSLLNFETVKYYNAEGYELERYREAI 480
Cdd:cd18578 188 AYEESSK-IASEAVSNIRTVASLTLEDYFLEKYEEAL 223
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
614-642 |
6.02e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 38.25 E-value: 6.02e-03
10 20 30
....*....|....*....|....*....|....
gi 1958800879 614 MPGQTVALVGPSGAGKSTILRLL-----FRFYDI 642
Cdd:PRK00131 2 LKGPNIVLIGFMGAGKSTIGRLLakrlgYDFIDT 35
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
606-664 |
6.21e-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: 6.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800879 606 LQDVSFTVMPGQTVaLVGPSGAGKSTILRLLFRFYDISSGcIRIDGQDISQVTQISLRS 664
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSS-RKFDEEDFYLGDDPDLPE 70
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
621-641 |
7.88e-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: 7.88e-03
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
619-660 |
8.29e-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: 8.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958800879 619 VALVGPSGAGKSTILRLLFRFYD---ISSGCIRID--GQDISQVTQI 660
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAKKLGlpyLDTGGIRTEevGKLASEVAAI 48
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
589-752 |
8.37e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.91 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 589 RVEFENVHFSYAdgRETLQDVSFTVMPGQTVALVGPSGAGKS----TILRLLFRFYDISSGCIRIDGQDISQVtqiSLRS 664
Cdd:PRK10418 4 QIELRNIALQAA--QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPC---ALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 665 -HIGVVPQDT-VLFN--DTIANNIR-----YGRvTAGDSEIQAAAQAAGIHDAilsfpegyetqvgERGLKL-----SGG 730
Cdd:PRK10418 79 rKIATIMQNPrSAFNplHTMHTHARetclaLGK-PADDATLTAALEAVGLENA-------------ARVLKLypfemSGG 144
|
170 180
....*....|....*....|..
gi 1958800879 731 EKQRVAIARTILKAPDIILLDE 752
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADE 166
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
606-753 |
8.62e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLrSHIGvvPQDTVLFNDTIANNIR 685
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958800879 686 YGrvtagdSEIQAAAQAagIHDAILSFPegYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEL 753
Cdd:PRK13541 93 FW------SEIYNSAET--LYAAIHYFK--LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
606-752 |
9.67e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 39.71 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 606 LQDVSFTVMPGQTVALVGPSGAGKSTILRllfrfyDISSgciRIDGQDISQVTQISLRSHIG--VVPQDT--VLFNDTia 681
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLK------TIAS---NTDGFHIGVEGVITYDGITPeeIKKHYRgdVVYNAE-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800879 682 NNIRYGRVTAGD------------------SEIQAAAQAAGIHDAILSFPEGYETQVGE---RGlkLSGGEKQRVAIART 740
Cdd:TIGR00956 146 TDVHFPHLTVGEtldfaarcktpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEA 223
|
170
....*....|..
gi 1958800879 741 ILKAPDIILLDE 752
Cdd:TIGR00956 224 SLGGAKIQCWDN 235
|
|
| |
