|
Name |
Accession |
Description |
Interval |
E-value |
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1-585 |
0e+00 |
|
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: 1071.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 1 MSLFQVYARALQYLAVHKFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFGVFNTIAFVLVSREA 80
Cdd:TIGR01192 1 MSLFQVYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVAREA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 81 DRLAHGRRASLLTEAFGRIVSMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVRLSL 160
Cdd:TIGR01192 81 DRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 161 ILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWA 240
Cdd:TIGR01192 161 VLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 241 LASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLEDFFQLEDSVQDRE 320
Cdd:TIGR01192 241 LASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 321 EPADAGELKGVVGEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIA 400
Cdd:TIGR01192 321 EPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 401 TVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRV 480
Cdd:TIGR01192 401 TVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSN 560
Cdd:TIGR01192 481 AIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKD 560
|
570 580
....*....|....*....|....*
gi 503610856 561 GRFAALLRASGILTDEDVRKSLTAA 585
Cdd:TIGR01192 561 GRFYKLLRRSGLLTNQPATKPLRKA 585
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-585 |
0e+00 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 1002.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 1 MSLFQVYARALQYLAVHKFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFGVFNTIAFVLVSREA 80
Cdd:PRK13657 1 MSLFRLYARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGVLVARHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 81 DRLAHGRRASLLTEAFGRIVSMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVRLSL 160
Cdd:PRK13657 81 DRLAHRRRLAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 161 ILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWA 240
Cdd:PRK13657 161 VLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 241 LASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLEDFFQLEDSVQDRE 320
Cdd:PRK13657 241 LASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 321 EPADAGELKGVVGEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIA 400
Cdd:PRK13657 321 DPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 401 TVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRV 480
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSN 560
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG 560
|
570 580
....*....|....*....|....*
gi 503610856 561 GRFAALLRASGILTDEDVRKSLTAA 585
Cdd:PRK13657 561 GRFAALLRAQGMLQEDERRKQPAAE 585
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-569 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 522.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 2 SLFQVYARALQYLAVHKFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKD---VAPMLLLWAGFGVFNTIAFVLVSR 78
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDlsaLLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 79 EADRLAHGRRASLLTEAFGRIVSMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVRL 158
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 159 SLILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDW 238
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 239 WALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLEDFFQLEDSVQD 318
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 319 REEPADAGELKGVVGEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVD 398
Cdd:COG1132 324 IPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 399 IATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQ 478
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQ 558
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
570
....*....|.
gi 503610856 559 SNGRFAALLRA 569
Cdd:COG1132 564 RGGLYARLYRL 574
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
21-309 |
4.92e-154 |
|
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: 443.22 E-value: 4.92e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFGRIV 100
Cdd:cd18562 1 ALGLALANVALAGVQFAEPVLFGRVVDALSSGGDAFPLLALWAALGLFSILAGVLVALLADRLAHRRRLAVMASYFEHVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 101 SMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVRLSLILVVLGAAYVMISKVVMSRT 180
Cdd:cd18562 81 TLPLSFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAALNRLVMRRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 181 KEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMMAILVI 260
Cdd:cd18562 161 KAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQYPVLNWWALASVLTRAASTLTMVAIFAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 503610856 261 GTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLEDF 309
Cdd:cd18562 241 GAWLVQRGELTVGEIVSFVGFATLLIGRLDQLSGFINRLFMQAPKLQEF 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-568 |
2.19e-123 |
|
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: 379.56 E-value: 2.19e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 11 LQYLAVHKFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAH-GRR- 88
Cdd:COG2274 148 LRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRlGQRi 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 89 -ASLLTEAFGRIVSMPLSWHSQRGTSnALHTLLRAcetlfglwLEFMRQHLATAVALMLL-IPTA-------FAMDVRLS 159
Cdd:COG2274 228 dLRLSSRFFRHLLRLPLSFFESRSVG-DLASRFRD--------VESIREFLTGSLLTALLdLLFVliflivlFFYSPPLA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 160 LILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNrieAETRELKKF---TQRLLSAQYPVL 236
Cdd:COG2274 299 LVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALG---AESRFRRRWenlLAKYLNARFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 237 DWWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLEDFFQLEDSV 316
Cdd:COG2274 376 RLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLP 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 317 QDREEPADAGELKGVVGEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILID 395
Cdd:COG2274 456 PEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 396 GVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGG 475
Cdd:COG2274 536 GIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 476 ERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHE 555
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEE 695
|
570
....*....|...
gi 503610856 556 LSQSNGRFAALLR 568
Cdd:COG2274 696 LLARKGLYAELVQ 708
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-566 |
4.71e-106 |
|
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: 331.40 E-value: 4.71e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 3 LFQVYARALQYLAVHKFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKD--VAPMLLLWA-GFGVFNTIAF-----V 74
Cdd:COG5265 21 RLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAAllVVPVGLLLAyGLLRLLSVLFgelrdA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 75 LVSREADRLAhgRRASLltEAFGRIVSMPLSWHSQRGT----------SNALHTLLRAceTLFGLwlefmrqhLATAV-- 142
Cdd:COG5265 101 LFARVTQRAV--RRLAL--EVFRHLHALSLRFHLERQTgglsrdiergTKGIEFLLRF--LLFNI--------LPTLLei 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 143 ALMLLIpTAFAMDVRLSLILVVLGAAYVMISKVVMS-----RTKEGQAAVEGHYHTVfshvsDSISNVSVVHSYNrieAE 217
Cdd:COG5265 167 ALVAGI-LLVKYDWWFALITLVTVVLYIAFTVVVTEwrtkfRREMNEADSEANTRAV-----DSLLNYETVKYFG---NE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 218 TRELKKFTQRLLSaqypvldwWALA--------SGLNRIASTI---SMMAILVIGTVLVQRGELGVGEVIafigfanlLI 286
Cdd:COG5265 238 AREARRYDEALAR--------YERAavksqtslALLNFGQALIialGLTAMMLMAAQGVVAGTMTVGDFV--------LV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 287 GrldqmkAFATQIF--------------EARAKLEDFFQLEDSVQDREEPADAGELKGVVGEVEFRDISFDFANSAQGVR 352
Cdd:COG5265 302 N------AYLIQLYiplnflgfvyreirQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLG 432
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 433 REDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKD 512
Cdd:COG5265 456 RPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA 535
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 503610856 513 AIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAAL 566
Cdd:COG5265 536 ALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-561 |
1.09e-105 |
|
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: 317.63 E-value: 1.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIA 412
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPI 492
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 493 LVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNG 561
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-566 |
3.69e-95 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 290.67 E-value: 3.69e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILV 494
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 495 LDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAAL 566
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-566 |
5.13e-95 |
|
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: 302.02 E-value: 5.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 7 YARALQYLAVHKFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKD---------VAPMLLLWAGFGVFntIAFVLVS 77
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDrsvlwwvplVVIGLAVLRGICSF--VSTYLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 78 READRLAHGRRASLlteaFGRIVSMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVR 157
Cdd:TIGR02203 80 WVSNKVVRDIRVRM----FEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 158 LSLILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLD 237
Cdd:TIGR02203 156 LTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 238 WWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLEDFFQLEDSVQ 317
Cdd:TIGR02203 236 AGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 318 DreepADAG--ELKGVVGEVEFRDISFDF-ANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILI 394
Cdd:TIGR02203 316 E----KDTGtrAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 395 DGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGR-EDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLS 473
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 474 GGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGF 553
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTH 551
|
570
....*....|...
gi 503610856 554 HELSQSNGRFAAL 566
Cdd:TIGR02203 552 NELLARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-566 |
1.83e-94 |
|
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: 288.75 E-value: 1.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIAT 413
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPIL 493
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAAL 566
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-569 |
1.71e-93 |
|
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: 286.36 E-value: 1.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAN--SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIA 412
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPI 492
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 493 LVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALLRA 569
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-561 |
1.78e-91 |
|
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: 292.43 E-value: 1.78e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 11 LQYLAVHKFRVGAIVIANIVLAAITIAEPILFGRIIDAI----SSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAHG 86
Cdd:COG4988 9 KRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLiiggAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 87 RRASLLTEAFGRIVSMPLSWHSQRGTSNALHTLLRACETL---FGLWLefmrqhlaTAVALMLLIP-----TAFAMDVRL 158
Cdd:COG4988 89 VKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALdgyFARYL--------PQLFLAALVPllilvAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 159 SLILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLdw 238
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVL-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 239 walasglnRIA----------STISM-MAILVIGTVLVQrgelgvGEVIAFIGFANLLIGR-----LDQMKAF--ATQif 300
Cdd:COG4988 239 --------RVAflssavleffASLSIaLVAVYIGFRLLG------GSLTLFAALFVLLLAPefflpLRDLGSFyhARA-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 301 EARAKLEDFFQLEDSVQDREEPADAGELKGVVGEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNL 380
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 381 LQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNG 460
Cdd:COG4988 383 LLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 461 YDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVI 540
Cdd:COG4988 463 LDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRIL 542
|
570 580
....*....|....*....|.
gi 503610856 541 FMDQGRVVEMGGFHELSQSNG 561
Cdd:COG4988 543 VLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
138-568 |
1.52e-86 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 279.73 E-value: 1.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 138 LATAVALMLLIPTAFAmdvrLSLILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTvfsHVSDSISNVSVVHSYNRIEAE 217
Cdd:COG4987 145 AAVAFLAFFSPALALV----LALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRA---RLTDLLQGAAELAAYGALDRA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 218 TRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMMAILVIGTVLVQRGELGvGEVIAFIGFANL-LIGRLDQMKAFA 296
Cdd:COG4987 218 LARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALaLFEALAPLPAAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 297 TQIFEARAKLEDFFQLEDSVQDREEPADAGELKGVVGeVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKT 375
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPS-LELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 376 TLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIE 455
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 456 DRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVRE 535
Cdd:COG4987 456 ALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER 535
|
410 420 430
....*....|....*....|....*....|...
gi 503610856 536 ADLVIFMDQGRVVEMGGFHELSQSNGRFAALLR 568
Cdd:COG4987 536 MDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
24-568 |
8.15e-80 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 265.07 E-value: 8.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 24 IVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGF---GVFNTIAFVLVSREADRLAHGRRASLLTEAFGRIV 100
Cdd:TIGR01846 144 VLLISLALQLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMlavAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 101 SMPLSWHSQRGTSNalhTLLRACEtlfglwLEFMRQHLaTAVALMLLIPTAF-----AMDVRLS--LILVVLGA--AYVM 171
Cdd:TIGR01846 224 GLPLGYFESRRVGD---TVARVRE------LEQIRNFL-TGSALTVVLDLLFvvvflAVMFFYSptLTGVVIGSlvCYAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 172 ISKVVMSRTKEgqaAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRL---LSAQYPVLDWWALASGLNRI 248
Cdd:TIGR01846 294 LSVFVGPILRK---RVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLaayVAASFRVTNLGNIAGQAIEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 249 ASTISMMAILVIGTVLVQRGELGVGEVIAFigfaNLLIGRLDQMKAFATQIFEarakleDFFQ-------LEDSVQDREE 321
Cdd:TIGR01846 371 IQKLTFAILLWFGAHLVIGGALSPGQLVAF----NMLAGRVTQPVLRLAQLWQ------DFQQtgialerLGDILNSPTE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 322 PADAG--ELKGVVGEVEFRDISFDFA-NSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVD 398
Cdd:TIGR01846 441 PRSAGlaALPELRGAITFENIRFRYApDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVD 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 399 IATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQ 478
Cdd:TIGR01846 521 LAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQ 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQ 558
Cdd:TIGR01846 601 RIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA 680
|
570
....*....|
gi 503610856 559 SNGRFAALLR 568
Cdd:TIGR01846 681 LQGLYARLWQ 690
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-546 |
2.03e-76 |
|
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: 239.59 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIAT 413
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLMNRSIGENIrlgredasldevmaaaeaaaasdfiedrlngydtvvgergnrLSGGERQRVAIARAILKNAPIL 493
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGR 546
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
119-567 |
2.53e-72 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 245.40 E-value: 2.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 119 LLRACETLFGLwLEFMRQhLATAVALMLLIPTAFamdvrLSLILVVLGAAYVMISKVVMSRT-KEGQAAVEghyhtvfsh 197
Cdd:TIGR00958 282 LLRNLVMLLGL-LGFMLW-LSPRLTMVTLINLPL-----VFLAEKVFGKRYQLLSEELQEAVaKANQVAEE--------- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 198 vsdSISNVSVVHSYNrieAETRELKKFTQRLlSAQYPVldWW--ALASGL----NRIASTISMMAILVIGTVLVQRGELG 271
Cdd:TIGR00958 346 ---ALSGMRTVRSFA---AEEGEASRFKEAL-EETLQL--NKrkALAYAGylwtTSVLGMLIQVLVLYYGGQLVLTGKVS 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 272 VGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLEDFFQLEDSVQDREEPadaGELK--GVVGEVEFRDISFDFAN--S 347
Cdd:TIGR00958 417 SGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT---GTLAplNLEGLIEFQDVSFSYPNrpD 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 348 AQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGE 427
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 NIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETE 507
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 508 ARVKDaiDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALL 567
Cdd:TIGR00958 654 QLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
335-566 |
3.10e-72 |
|
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: 231.61 E-value: 3.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDF-ANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIAT 413
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPIL 493
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAAL 566
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
315-568 |
5.86e-72 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 241.46 E-value: 5.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 315 SVQDREEPADAG--ELKGVVGEVEFRDISFDFANSAQ-GVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQ 391
Cdd:PRK11176 320 AILDLEQEKDEGkrVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 392 ILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDA-SLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGN 470
Cdd:PRK11176 400 ILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 471 RLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEM 550
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
250
....*....|....*...
gi 503610856 551 GGFHELSQSNGRFAALLR 568
Cdd:PRK11176 560 GTHAELLAQNGVYAQLHK 577
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-542 |
7.49e-69 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 231.79 E-value: 7.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 23 AIVIANIVLAAIT----IAEPILFGRIIDAISSQKdvAPMLLLWAGFGVFNTIAFV------LVSREADRLAHGRRASLL 92
Cdd:TIGR02857 3 RALALLALLGVLGalliIAQAWLLARVVDGLISAG--EPLAELLPALGALALVLLLrallgwLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 93 TEAFGRIVSMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVrLSLILVVLGAAYV-- 170
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDW-ISGLILLLTAPLIpi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 171 -MIskVVMSRTkegQAAVEGHYHT---VFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLdwwalasgln 246
Cdd:TIGR02857 160 fMI--LIGWAA---QAAARKQWAAlsrLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVL---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 247 RIAsTISMMAILVIGTvlvqrgeLGVGEVIAFIGFaNLLIGRLDQMKAFATQIF-------------------EARAKLE 307
Cdd:TIGR02857 225 RIA-FLSSAVLELFAT-------LSVALVAVYIGF-RLLAGDLDLATGLFVLLLapefylplrqlgaqyharaDGVAAAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 308 DFFQLEDSvQDREEPADAGELKGVVGEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEP 387
Cdd:TIGR02857 296 ALFAVLDA-APRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 388 KHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGE 467
Cdd:TIGR02857 375 TEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGE 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 468 RGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFM 542
Cdd:TIGR02857 455 GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-547 |
6.80e-66 |
|
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: 214.64 E-value: 6.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFAN--SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRS 410
Cdd:cd03248 10 GIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNA 490
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRV 547
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-548 |
1.05e-63 |
|
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: 208.60 E-value: 1.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQ-GVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAP 491
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVV 548
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-551 |
4.78e-62 |
|
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: 204.26 E-value: 4.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIR-LGRedASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNA 490
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
116-568 |
8.29e-59 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 208.27 E-value: 8.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 116 LHTLLRACETLFGLWLEFMRQHLATAVALMLLiptafamdvrLSLILVVLGAAYVMISKVvmSRTKEGQAAVEGHYHTVF 195
Cdd:TIGR03797 254 LTTLLSGIFALLNLGLMFYYSWKLALVAVALA----------LVAIAVTLVLGLLQVRKE--RRLLELSGKISGLTVQLI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 196 shvsDSISNVSVVHSYNRieAETRELKKFTQRL---LSAQYpvldWWALASGLNRIASTISMMAILVIGTVLVQRGELGV 272
Cdd:TIGR03797 322 ----NGISKLRVAGAENR--AFARWAKLFSRQRkleLSAQR----IENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 273 GEVIAFIGFANLLIGRLDQMKAFATQIFEA-----RAKLedffQLEDSVQDREEPADAGELKGvvgEVEFRDISFDFA-N 346
Cdd:TIGR03797 392 GSFLAFNTAFGSFSGAVTQLSNTLISILAViplweRAKP----ILEALPEVDEAKTDPGKLSG---AIEVDRVTFRYRpD 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 347 SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIG 426
Cdd:TIGR03797 465 GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIF 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIrLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVET 506
Cdd:TIGR03797 545 ENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT 623
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 507 EARVKDAIDALRKDRttFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALLR 568
Cdd:TIGR03797 624 QAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
162-551 |
8.17e-56 |
|
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: 197.66 E-value: 8.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 162 LVVLGAAYVMISKVVMS--RTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWW 239
Cdd:COG4618 159 LLALVGALVLVALALLNerLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 240 ALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAfigfANLLIGR----LDQMKAFATQIFEARAKLEdffQLEDS 315
Cdd:COG4618 239 GGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIA----ASILMGRalapIEQAIGGWKQFVSARQAYR---RLNEL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 316 VQDREEPADAGELKGVVGEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILI 394
Cdd:COG4618 312 LAAVPAEPERMPLPRPKGRLSVENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 395 DGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENI-RLGreDASLDEVMAAAEAAAASDFIEdRL-NGYDTVVGERGNRL 472
Cdd:COG4618 392 DGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMIL-RLpDGYDTRIGEGGARL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 473 SGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTT-FIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
240-569 |
1.45e-52 |
|
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: 191.11 E-value: 1.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 240 ALASGLNRIASTIsmmaILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARA---KLEDFFQLEDSV 316
Cdd:TIGR01193 383 AIKAVTKLILNVV----ILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVannRLNEVYLVDSEF 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 317 QDREEPAdagELKGVVGEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG 396
Cdd:TIGR01193 459 INKKKRT---ELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 397 VDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLG-REDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGG 475
Cdd:TIGR01193 536 FSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 476 ERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALrKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHE 555
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
330
....*....|....
gi 503610856 556 LSQSNGRFAALLRA 569
Cdd:TIGR01193 695 LLDRNGFYASLIHN 708
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
347-569 |
1.06e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 186.97 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 347 SAQGVR---NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHePKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNR 423
Cdd:PRK11174 359 SPDGKTlagPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 424 SIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALD 503
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 504 VETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALLRA 569
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
138-530 |
2.44e-51 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 184.49 E-value: 2.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 138 LATAVALMLLIPTAFAMDVRLSLILVVLGAayvmISKVVMSRTKEGQAAVEGHYhtvFSHVSDSISNVSVVHSYNRIEAE 217
Cdd:TIGR02868 143 AAVAAIAVLSVPAALILAAGLLLAGFVAPL----VSLRAARAAEQALARLRGEL---AAQLTDALDGAAELVASGALPAA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 218 TRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMMAILVIGTVLVQRGELGvGEVIAFIGFANL-LIGRLDQMKAFA 296
Cdd:TIGR02868 216 LAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLaAFEAFAALPAAA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 297 TQIFEARAKLEDFFQLEDSVQDREEPADAGELKGVVGEV--EFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGK 374
Cdd:TIGR02868 295 QQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPtlELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 375 TTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFI 454
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWL 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 455 EDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRL 530
Cdd:TIGR02868 455 RALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
333-568 |
2.15e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 180.02 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRlNGYDTVVGERGNRLSGGERQRVAIARAILKNAP 491
Cdd:PRK11160 417 SVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDD-KGLNAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALLR 568
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
197-551 |
5.80e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 175.61 E-value: 5.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 197 HVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVI 276
Cdd:TIGR01842 182 LADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 277 AfigfANLLIGR----LDQMKAFATQIFEARA---KLEDFFQLEDSvqdreePADAGELKGVVGEVEFRDISFDFANSAQ 349
Cdd:TIGR01842 262 A----GSILVGRalapIDGAIGGWKQFSGARQaykRLNELLANYPS------RDPAMPLPEPEGHLSVENVTIVPPGGKK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 350 G-VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGEN 428
Cdd:TIGR01842 332 PtLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAEN 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEA 508
Cdd:TIGR01842 412 IARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503610856 509 RVKDAIDALRKDR-TTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:TIGR01842 492 ALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
252-563 |
6.78e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 173.75 E-value: 6.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 252 ISMMAILVIGTVLVQ-----RGELGVGEVIAFIGFanllIGRLDQ-MKAFATQ---IFEARAKLEDFFQLEDSVQDREEP 322
Cdd:PRK10790 256 LSLFSALILCGLLMLfgfsaSGTIEVGVLYAFISY----LGRLNEpLIELTTQqsmLQQAVVAGERVFELMDGPRQQYGN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 323 aDAGELKGvvGEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATV 402
Cdd:PRK10790 332 -DDRPLQS--GRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 403 TRKSLRRSIATVFQDAGLMNRSIGENIRLGReDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAI 482
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 483 ARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGR 562
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGR 567
|
.
gi 503610856 563 F 563
Cdd:PRK10790 568 Y 568
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
335-551 |
2.34e-46 |
|
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: 162.68 E-value: 2.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSA---QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT---RKSLR 408
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 409 RSIATVFQDAGL-MN--RSIGENIRlgredasldEVMAAAEAAAASDFIEDRLNGYDTVVG---ERGNR----LSGGERQ 478
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIA---------EPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRypheLSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-551 |
2.96e-46 |
|
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: 161.81 E-value: 2.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFA-NSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:cd03369 5 GEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIrlgredasldevmaaaeaaaasdfieDRLNGYDTV-------VGERGNRLSGGERQRVAIAR 484
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNL--------------------------DPFDEYSDEeiygalrVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
248-561 |
1.08e-45 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 169.89 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 248 IASTISMMAILVI--GTVLVQRGELGVGEVIAFIGFANLLIGrldQMKAFA--TQIFE----ARAKLEDFFQLEDSVQDR 319
Cdd:PRK10789 227 IYIAIGMANLLAIggGSWMVVNGSLTLGQLTSFVMYLGLMIW---PMLALAwmFNIVErgsaAYSRIRAMLAEAPVVKDG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 320 EE--PADAGELkgvvgEVEFRDISFDfANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGV 397
Cdd:PRK10789 304 SEpvPEGRGEL-----DVNIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 398 DIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGER 477
Cdd:PRK10789 378 PLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 478 QRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELS 557
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
....
gi 503610856 558 QSNG 561
Cdd:PRK10789 538 QQSG 541
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
336-547 |
4.01e-45 |
|
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: 157.38 E-value: 4.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:cd03246 2 EVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLMNRSIGENIrlgredasldevmaaaeaaaasdfiedrlngydtvvgergnrLSGGERQRVAIARAILKNAPILV 494
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503610856 495 LDEATSALDVETEARVKDAIDALRKDRTTFI-IAHRLSTVREADLVIFMDQGRV 547
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIvIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
296-551 |
1.78e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 162.38 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 296 ATQIFEARAKLEDFFQLEDSVQDREEPADAGElkgVVgeVEFRDISFDFANSAQG----VRNVSFKAKAGQTIAIVGPTG 371
Cdd:COG1123 227 PEEILAAPQALAAVPRLGAARGRAAPAAAAAE---PL--LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESG 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 372 AGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKS---LRRSIATVFQD--AGLMNR-SIGEnirlgredaSLDEVMAAA 445
Cdd:COG1123 302 SGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQDpySSLNPRmTVGD---------IIAEPLRLH 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 446 EAAAASDfIEDRLNGYDTVVG---ERGNR----LSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALR 518
Cdd:COG1123 373 GLLSRAE-RRERVAELLERVGlppDLADRypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQ 451
|
250 260 270
....*....|....*....|....*....|....*.
gi 503610856 519 KDR-TTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:COG1123 452 RELgLTYLfISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-551 |
5.18e-43 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 152.08 E-value: 5.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtRKSLRRSIAT 413
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLMNRSIGENIrlgredasldevmaaaeaaaasdfiedrlngydtvvgerGNRLSGGERQRVAIARAILKNAPIL 493
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
21-289 |
9.48e-43 |
|
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: 154.34 E-value: 9.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIANIVLAAITIAEPILFGRIIDAISSQKD-----VAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEA 95
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDpetqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 96 FGRIVSMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVRLSLILVVLGAAYVMISKV 175
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 176 VMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMM 255
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 503610856 256 AILVIGTVLVQRGELGVGEVIAFIGFANLLIGRL 289
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-551 |
4.76e-42 |
|
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: 150.95 E-value: 4.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDA---------------GLMNRSIGENIRLGREDASLDEVmaaaeaaaasdfiedRLNGY-DTVVgergNRLSGGERQ 478
Cdd:COG1122 81 FQNPddqlfaptveedvafGPENLGLPREEIRERVEEALELV---------------GLEHLaDRPP----HELSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADG 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
138-572 |
5.22e-42 |
|
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: 162.81 E-value: 5.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 138 LATAVALMLLIPTAfamdvrlSLILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIE-- 215
Cdd:TIGR00957 1094 IGALIVILLATPIA-------AVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQErf 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 216 AETRELK-KFTQRllsAQYP--VLDWWaLASGLNRIASTISMMAIL--VIGTVLVQRGELG--VGEVIAFIGFANLLIGR 288
Cdd:TIGR00957 1167 IHQSDLKvDENQK---AYYPsiVANRW-LAVRLECVGNCIVLFAALfaVISRHSLSAGLVGlsVSYSLQVTFYLNWLVRM 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 289 LDQMKafaTQIFeARAKLEDFFQLEDS----VQDREEPADAGElkgvVGEVEFRDISFDFANSAQGV-RNVSFKAKAGQT 363
Cdd:TIGR00957 1243 SSEME---TNIV-AVERLKEYSETEKEapwqIQETAPPSGWPP----RGRVEFRNYCLRYREDLDLVlRHINVTIHGGEK 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 364 IAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRlGREDASLDEVMA 443
Cdd:TIGR00957 1315 VGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWW 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 444 AAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTT 523
Cdd:TIGR00957 1394 ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTV 1473
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 503610856 524 FIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALLRASGI 572
Cdd:TIGR00957 1474 LTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
336-546 |
7.65e-42 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 149.92 E-value: 7.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDA--GLMNRSIGENIRLGREDASLDEVMaaaeaaaasdfIEDRLNGYDTVVGERGNR------LSGGERQRVAIARAI 486
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEE-----------IEERVEEALELVGLEGLRdrspftLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 487 LKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGR 546
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
351-500 |
7.80e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.79 E-value: 7.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNR-SIGENI 429
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 430 RLGREDASLDEvmaaAEAAAASDFIEDRLNGY---DTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATS 500
Cdd:pfam00005 81 RLGLLLKGLSK----REKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-573 |
2.27e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 149.95 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQG---VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGL-------MNRSIGE---NIRLGREDASLDEVMaaaeaaaasdfieDRLNGYDTVVGERGNRLSGGERQRVA 481
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEplrIHGLPDREERIAELL-------------EQVGLPPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 482 IARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHELSQ 558
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*..
gi 503610856 559 --SNGRFAALLRASGIL 573
Cdd:COG1124 229 gpKHPYTRELLAASLAF 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
261-561 |
3.45e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 160.19 E-value: 3.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 261 GTVLVQRGELGVGE----VIAFIgFANLLIGRLDQMKAFATQifeARAKLEDFFQL---EDSVQDReepaDAGELK---- 329
Cdd:PTZ00265 1088 GSFLIRRGTILVDDfmksLFTFL-FTGSYAGKLMSLKGDSEN---AKLSFEKYYPLiirKSNIDVR----DNGGIRiknk 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 330 -GVVGEVEFRDISFDFAN--SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKH----------------- 389
Cdd:PTZ00265 1160 nDIKGKIEIMDVNFRYISrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtne 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 390 -------------------------------------GQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLG 432
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 433 REDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKD 512
Cdd:PTZ00265 1320 KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 513 AIDALRK--DRTTFIIAHRLSTVREAD-LVIFMD---QGRVVEMGGFHE--LSQSNG 561
Cdd:PTZ00265 1400 TIVDIKDkaDKTIITIAHRIASIKRSDkIVVFNNpdrTGSFVQAHGTHEelLSVQDG 1456
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-551 |
2.16e-40 |
|
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: 146.56 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFdFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHE-----PKHGQILIDGVDIAT--VTRKSL 407
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RRSIATVFQDAGLMNRSIGENIRLG------REDASLDEVMAAAEAAAA-SDFIEDRLNGYdtvvgergnRLSGGERQRV 480
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAAlWDEVKDRLHAL---------GLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTV-READLVIFMDQGRVVEMG 551
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFG 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-546 |
3.48e-40 |
|
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: 144.25 E-value: 3.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT--RKSLRRSIA 412
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLMNR-SIGENIRLGredasldevmaaaeaaaasdfiedrlngydtvvgergnrLSGGERQRVAIARAILKNAP 491
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALRKD--RTTFIIAHRLSTVRE-ADLVIFMDQGR 546
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-549 |
1.95e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.65 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKS---LRRSI 411
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGL-MNRSIGENIRL-----GREDASldevmaaaeaaaasdfIEDRLNGYDTVVG--ERGNR----LSGGERQR 479
Cdd:COG2884 82 GVVFQDFRLlPDRTVYENVALplrvtGKSRKE----------------IRRRVREVLDLVGlsDKAKAlpheLSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 480 VAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVREADL-VIFMDQGRVVE 549
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
336-546 |
3.79e-39 |
|
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: 140.84 E-value: 3.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVF 415
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 416 QdaglmnrsigenirlgredasldevmaaaeaaaasdfiedrlngydtvvgergnrLSGGERQRVAIARAILKNAPILVL 495
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503610856 496 DEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVREA-DLVIFMDQGR 546
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-568 |
1.08e-38 |
|
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: 148.90 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSA-QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPK---HGQILIDGVDIATVTRKSLRRS 410
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQDAG--LMNRSIGENIR--LGREDASLDEVMAAAEAAAASDFIEDRLNGYDtvvgergNRLSGGERQRVAIARAI 486
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 487 LKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQSNGRF 563
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
....*
gi 503610856 564 AALLR 568
Cdd:COG1123 238 AAVPR 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-549 |
1.91e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.95 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL---- 407
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RRSIATVFQDAGLMNR-SIGENIRLGREDASLD-EVMAAAEAAAASDF-IEDRLNgydtvvgERGNRLSGGERQRVAIAR 484
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLLLAGVSrKERRERARELLERVgLGDRLD-------HRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFIIA-HRLSTVREADLVIFMDQGRVVE 549
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-556 |
2.11e-38 |
|
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: 141.18 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQG---VRNVSFKAKAGQTIAIVGPTGAGKTTLV---NLLQRvhePKHGQILIDGVDIATVTRKSL- 407
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLER---PTSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 --RRSIATVFQDAGLMN-RSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLNGYDTVVG--ERGNR----LSGGERQ 478
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSsRTVFENVALPLEIAGVPK-----------AEIEERVLELLELVGleDKADAypaqLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHE 555
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
.
gi 503610856 556 L 556
Cdd:cd03258 228 V 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
336-562 |
5.95e-38 |
|
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: 140.38 E-value: 5.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKsLRRSIATVF 415
Cdd:COG4555 3 EVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 416 QDAGLMNR-SIGENIRLgreDASLDEVMAAAEAAAASDFIEdrLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILV 494
Cdd:COG4555 81 DERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIE--LLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 495 LDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQSNGR 562
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-547 |
2.84e-37 |
|
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: 135.99 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATvTRKSLRRSIATV 414
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLMnrsigenirlgredasldevmaaaeaaaasdfieDRLNGYDTVvgergnRLSGGERQRVAIARAILKNAPILV 494
Cdd:cd03230 79 PEEPSLY----------------------------------ENLTVRENL------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 495 LDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRV 547
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-556 |
2.88e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.27 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANsAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATvTRKSLRRSIATV 414
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLM-NRSIGENIRLGredASLDEVMAAAEAAAASDFIED-RLNGY-DTVVGErgnrLSGGERQRVAIARAILKNAP 491
Cdd:COG1131 79 PQEPALYpDLTVRENLRFF---ARLYGLPRKEARERIDELLELfGLTDAaDRKVGT----LSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-551 |
3.09e-37 |
|
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: 137.27 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTrkSLRRSIATV 414
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLM-NRSIGENIRLG-------------REDASLDEVMaaaeaaaasdfIEDRLNGYdtvVGErgnrLSGGERQRV 480
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGlklrgvpkaeiraRVRELLELVG-----------LEGLLNRY---PHE----LSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
335-546 |
4.37e-37 |
|
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: 136.45 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISF----DFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVN-LLQRVHePKHGQILIDGvdiatvtrkslrr 409
Cdd:cd03250 1 ISVEDASFtwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 410 SIATVFQDAGLMNRSIGENIRLGREdasldevmaaaeaaaasdFIEDRLN-----------------GYDTVVGERGNRL 472
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKP------------------FDEERYEkvikacalepdleilpdGDLTEIGEKGINL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 473 SGGERQRVAIARAILKNAPILVLDEATSALDVETEARV-KDAI-DALRKDRTTFIIAHRLSTVREADLVIFMDQGR 546
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-551 |
4.76e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 140.60 E-value: 4.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLV---NLLQRvhePKHGQILIDGVDIATVTRKSL- 407
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 --RRSIATVFQDAGLMN-RSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLNGYDTVVG--ERGNR----LSGGERQ 478
Cdd:COG1135 79 aaRRKIGMIFQHFNLLSsRTVAENVALPLEIAGVPK-----------AEIRKRVAELLELVGlsDKADAypsqLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 479 RVAIARAiLKNAP-ILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:COG1135 148 RVGIARA-LANNPkVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
335-560 |
1.61e-36 |
|
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: 136.26 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRK---SLRRSI 411
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGL---MnrSIGENIRLG-REDASLDEvmaaaeaaaasDFIEDRLNGYDTVVGERG------NRLSGGERQRVA 481
Cdd:COG1127 85 GMLFQGGALfdsL--TVFENVAFPlREHTDLSE-----------AEIRELVLEKLELVGLPGaadkmpSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 482 IARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQ 558
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
..
gi 503610856 559 SN 560
Cdd:COG1127 232 SD 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-547 |
3.97e-36 |
|
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: 134.54 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL---- 407
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RRSIATVFQDAGLMNR-SIGENIRLG-----------REDAS--LDEVMaaaeaaaasdfIEDRLNGYdtvVGErgnrLS 473
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPlllagvpkkerRERAEelLERVG-----------LGDRLNHY---PSE----LS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 474 GGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFIIA-HRLSTVREADLVIFMDQGRV 547
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
333-571 |
5.53e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 144.50 E-value: 5.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIRLGRE--DASLDEVMAAAEAaaaSDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKN 489
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEhnDADLWESLERAHL---KDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRR 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 490 APILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHEL-SQSNGRFAALLR 568
Cdd:PLN03130 1393 SKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQ 1472
|
...
gi 503610856 569 ASG 571
Cdd:PLN03130 1473 STG 1475
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
335-548 |
9.06e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.41 E-value: 9.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL---RRSI 411
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNR-SIGENI---RLGR-------------ED-----ASLDEVMaaaeaaaasdfIEDRLNgydtvvgERG 469
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVlagRLGRtstwrsllglfppEDreralEALERVG-----------LADKAY-------QRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 470 NRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDAL-RKDRTTFIIA-HRLSTVRE-ADLVIFMDQGR 546
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNlHQVDLARRyADRIIGLRDGR 224
|
..
gi 503610856 547 VV 548
Cdd:COG3638 225 VV 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
352-551 |
1.42e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.58 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTL---VNLLQrvhEPKHGQILIDGVDIaTVTRKSL---RRSIATVFQDAGL-MNRS 424
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLE---EPDSGTITVDGEDL-TDSKKDInklRRKVGMVFQQFNLfPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLG--------REDAS------LDEVMaaaeaaaasdfIEDRLNGYDtvvgergNRLSGGERQRVAIARAILKNA 490
Cdd:COG1126 94 VLENVTLApikvkkmsKAEAEeramelLERVG-----------LADKADAYP-------AQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVtHEMGFAREvADRVVFMDGGRIVEEG 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
351-556 |
2.42e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 135.18 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKH---GQILIDGVDIATVTRKSLR----RSIATVFQDAglMN- 422
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRkirgREIQMIFQDP--MTs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 --------RSIGENIR----LGREDAS------LDEVmaaaeaaaasdfiedRLNGYDTVVGERGNRLSGGERQRVAIAR 484
Cdd:COG0444 99 lnpvmtvgDQIAEPLRihggLSKAEAReraielLERV---------------GLPDPERRLDRYPHELSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGRIVEEGPVEEL 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-551 |
5.04e-35 |
|
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: 132.47 E-value: 5.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAG-----------LMNRS--IGENIRLGREDASL-DEVMAAAEAaaaSDFIEDRLNgydtvvgergnRLSGGERQRV 480
Cdd:COG1120 81 PQEPPapfgltvrelvALGRYphLGLFGRPSAEDREAvEEALERTGL---EHLADRPVD-----------ELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKD--RTTFIIAHRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
336-551 |
6.56e-35 |
|
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: 129.86 E-value: 6.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVF 415
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 416 QdaglmnrsigenirlgredaSLDEVmaaaeaaAASDFIEDRLNgydtvvgergnRLSGGERQRVAIARAILKNAPILVL 495
Cdd:cd03214 80 Q--------------------ALELL-------GLAHLADRPFN-----------ELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 496 DEATSALDVETEARVKDAIDALRKDRTTFIIA--HRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMvlHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
336-547 |
7.50e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVF 415
Cdd:COG4619 2 ELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 416 QDAGLMNRSIGENIRLG---REDASLDEVMAaaeaaaasDFIEdRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPI 492
Cdd:COG4619 81 QEPALWGGTVRDNLPFPfqlRERKFDRERAL--------ELLE-RLGLPPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 493 LVLDEATSALDVETEARVKDAIDALR--KDRTTFIIAH-RLSTVREADLVIFMDQGRV 547
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-559 |
1.03e-34 |
|
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: 131.08 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAnSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRK---SLRRSI 411
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNR-SIGENIRLG-REDASLDEVMaaaeaaaASDFIEDRLNgydtVVGERGNR------LSGGERQRVAIA 483
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlREHTRLSEEE-------IREIVLEKLE----AVGLRGAEdlypaeLSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 484 RAILKNAPILVLDEATSALDVETEARVKDAIDALRK--DRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQS 559
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
21-307 |
8.37e-34 |
|
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: 130.36 E-value: 8.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIANIVLAAITIAEPILFGRIIDAISSQKD---VAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFG 97
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDlslLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 98 RIVSMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVRLSLILVVLGAAYVMISKVVM 177
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 178 SRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMMAI 257
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 503610856 258 LVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-551 |
2.11e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 127.80 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLM-NRSIGENIRL---------GREDASLDEVMaaaeaaaasdfiedRLNGYDTvvGERGNR----LSGGERQRV 480
Cdd:cd03295 81 IQQIGLFpHMTVEENIALvpkllkwpkEKIRERADELL--------------ALVGLDP--AEFADRypheLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKD--RTTFIIAHRL-STVREADLVIFMDQGRVVEMG 551
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVG 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
335-547 |
2.20e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 126.88 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANsAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRK--SLRRSIA 412
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLM-NRSIGENIRLG--------REDAS------LDEVMaaaeaaaasdfIEDRLNGYDtvvgergNRLSGGER 477
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLApikvkgmsKAEAEeralelLEKVG-----------LADKADAYP-------AQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 478 QRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRV 547
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVtHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-551 |
3.34e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 127.76 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 350 GVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL----RRSIATVFQDAGLM-NRS 424
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLGREDASLDEVMAAAEAAAASDFI--EDRLNGYDtvvgergNRLSGGERQRVAIARAILKNAPILVLDEATSAL 502
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVglEGWEHKYP-------DELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503610856 503 DVETEARVKDAIDALRKD--RTTFIIAHRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:cd03294 192 DPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
336-548 |
4.00e-33 |
|
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: 126.91 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL---RRSIA 412
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLMNR-SIGENI---RLGR-------------ED-----ASLDEVmaaaeaaaasdfiedrlnGYDTVVGERGN 470
Cdd:cd03256 82 MIFQQFNLIERlSVLENVlsgRLGRrstwrslfglfpkEEkqralAALERV------------------GLLDKAYQRAD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 471 RLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA--HRLSTVRE-ADLVIFMDQGRV 547
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAREyADRIVGLKDGRI 223
|
.
gi 503610856 548 V 548
Cdd:cd03256 224 V 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
321-546 |
9.30e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 134.77 E-value: 9.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 321 EPADAGELKGVVGEVEFRDISF--DFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILI-DGV 397
Cdd:PTZ00265 369 ENNDDGKKLKDIKKIQFKNVRFhyDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSH 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 398 DIATVTRKSLRRSIATVFQDAGLMNRSIGENIRLG--------------REDASL------------------------- 438
Cdd:PTZ00265 449 NLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGNDsqenknkrnscrakcagdlndmsnt 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 439 ------------------DEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATS 500
Cdd:PTZ00265 529 tdsneliemrknyqtikdSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 503610856 501 ALDVETEARVKDAIDALR--KDRTTFIIAHRLSTVREADlVIFMDQGR 546
Cdd:PTZ00265 609 SLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYAN-TIFVLSNR 655
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-556 |
1.51e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.54 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR---KSLRRSIATVFQD--AGLMNR-- 423
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDpyASLNPRmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 424 ---SIGENIRLgREDASLDEVMaaaeaaaasDFIEDRLngydTVVG---ERGNR----LSGGERQRVAIARAILKNAPIL 493
Cdd:COG4608 114 vgdIIAEPLRI-HGLASKAERR---------ERVAELL----ELVGlrpEHADRypheFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:COG4608 180 VCDEPVSALDVSIQAQVLNLLEDLQDELglTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-551 |
1.77e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.87 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANS-AQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIAT 413
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGlmNRSIG----ENIRLGREDASLD-EVMaaaeaaaaSDFIEDrlngYDTVVG-------ERGNrLSGGERQRVA 481
Cdd:PRK13632 88 IFQNPD--NQFIGatveDDIAFGLENKKVPpKKM--------KDIIDD----LAKKVGmedyldkEPQN-LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 482 IARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRT-TFI-IAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
328-569 |
2.33e-32 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 125.41 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 328 LKGVVGEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKS 406
Cdd:cd03288 13 LVGLGGEIKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 407 LRRSIATVFQDAGLMNRSIGENIRLGREdASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAI 486
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 487 LKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHEL-SQSNGRFAA 565
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFAS 251
|
....
gi 503610856 566 LLRA 569
Cdd:cd03288 252 LVRT 255
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
335-551 |
1.58e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 123.31 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSA-QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiaTVTRKSL---RRS 410
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQ--DaglmNRSIG-----------ENIRLGRE------DASLDEV-MaaaeaaaaSDFIEdrlngydtvvgeRG- 469
Cdd:TIGR04520 79 VGMVFQnpD----NQFVGatveddvafglENLGVPREemrkrvDEALKLVgM--------EDFRD------------REp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 470 NRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVREADLVIFMDQGRV 547
Cdd:TIGR04520 135 HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKI 214
|
....
gi 503610856 548 VEMG 551
Cdd:TIGR04520 215 VAEG 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
349-580 |
1.89e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 124.69 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIA---TVTRKSLRRSIATVFQDA-GLMN-- 422
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPyGSLNpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSIGE--------NIRLGRED--ASLDEVMAAaeaaaasdfiedrlngydtvVG---ERGNR----LSGGERQRVAIARA 485
Cdd:PRK11308 109 KKVGQileeplliNTSLSAAErrEKALAMMAK--------------------VGlrpEHYDRyphmFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 486 ILKNAPILVLDEATSALDVETEARVKDAIDALRKD-RTTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELsqsngr 562
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI------ 242
|
250 260
....*....|....*....|....*.
gi 503610856 563 FA--------ALLRASGILTDEDVRK 580
Cdd:PRK11308 243 FNnprhpytqALLSATPRLNPDDRRE 268
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-547 |
3.61e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtrkslRRSIATV 414
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQ----DAG---------LMNR--SIGENIRLGRED-----ASLDEV-MaaaeaaaaSDFiEDRLngydtvVGErgnrLS 473
Cdd:COG1121 81 PQraevDWDfpitvrdvvLMGRygRRGLFRRPSRADreavdEALERVgL--------EDL-ADRP------IGE----LS 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 474 GGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRV 547
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVtHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
351-567 |
4.53e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 120.90 E-value: 4.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtrKSLRRSIATVFQDAGLM-NRSIGENI 429
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 RLGREDASLDEVMAAAEAAAASDFIedrlnGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEAR 509
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 510 VKDAI-DALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL--SQSNGRFAALL 567
Cdd:cd03299 168 LREELkKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVfkKPKNEFVAEFL 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
333-571 |
5.13e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 129.33 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:PLN03232 1233 GSIKFEDVHLRYRPGLPPVlHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIRLGRE--DASLDEVMAAAEAaaaSDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKN 489
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNIDPFSEhnDADLWEALERAHI---KDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 490 APILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHE-LSQSNGRFAALLR 568
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQElLSRDTSAFFRMVH 1469
|
...
gi 503610856 569 ASG 571
Cdd:PLN03232 1470 STG 1472
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-527 |
5.70e-31 |
|
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: 120.21 E-value: 5.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKS---LRRSI 411
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLM-NRSIGENIRLGRE--DASLDEVMAAAEAAAASDFIEDRLNGYdtvvgerGNRLSGGERQRVAIARAILK 488
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFALEvtGVPPREIRKRVPAALELVGLSHKHRAL-------PAELSGGEQQRVAIARAIVN 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 503610856 489 NAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA 527
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-551 |
2.07e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.76 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHE--PK---HGQILIDGVDI--ATVTRKSL 407
Cdd:COG1117 12 IEVRNLNVYYGDK-QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RRSIATVFQDAGLMNRSIGENIRLG-R------------------EDASL-DEVmaaaeaaaasdfiEDRLNgydtvvgE 467
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlRlhgikskseldeiveeslRKAALwDEV-------------KDRLK-------K 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 468 RGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLS-TVREADLVIFMDQGR 546
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGE 230
|
....*
gi 503610856 547 VVEMG 551
Cdd:COG1117 231 LVEFG 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-548 |
4.91e-30 |
|
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: 115.60 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANsAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRSIAT 413
Cdd:cd03216 1 LELRGITKRFGG-VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQdaglmnrsigenirlgredasldevmaaaeaaaasdfiedrlngydtvvgergnrLSGGERQRVAIARAILKNAPIL 493
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVV 548
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-549 |
6.10e-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: 118.27 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGvdiATVTRKSLRRSI 411
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtalDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG---KPVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 atVFQDAGLMN-RSIGENIRLGREDASLDevmaaaeaaaaSDFIEDRLNGYDTVVG--ERGNR----LSGGERQRVAIAR 484
Cdd:COG1116 85 --VFQEPALLPwLTVLDNVALGLELRGVP-----------KAERRERARELLELVGlaGFEDAyphqLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAIDAL--RKDRTTFIIAHrlsTVREA----DLVIFMDQ--GRVVE 549
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH---DVDEAvflaDRVVVLSArpGRIVE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
335-551 |
6.34e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.68 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL---R 408
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 409 RSIATVFQDAGLMN-RSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLNGYDTVVG--ERGNR----LSGGERQRVA 481
Cdd:PRK11153 82 RQIGMIFQHFNLLSsRTVFDNVALPLELAGTPK-----------AEIKARVTELLELVGlsDKADRypaqLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 482 IARAiLKNAP-ILVLDEATSALDVETearvKDAIDALRKD--R----TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK11153 151 IARA-LASNPkVLLCDEATSALDPAT----TRSILELLKDinRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-551 |
7.00e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.59 E-value: 7.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAnSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKslRRSIATV 414
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLM-NRSIGENI-------RLGREDAS------LDEVmaaaeaaaasdfiedRLNGYdtvvgerGNR----LSGGE 476
Cdd:COG3842 83 FQDYALFpHLTVAENVafglrmrGVPKAEIRarvaelLELV---------------GLEGL-------ADRyphqLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 477 RQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFIIA-HRLStvrEA----DLVIFMDQGRVVEM 550
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgITFIYVtHDQE---EAlalaDRIAVMNDGRIEQV 217
|
.
gi 503610856 551 G 551
Cdd:COG3842 218 G 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
351-545 |
7.23e-30 |
|
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: 116.86 E-value: 7.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIaTVTRKSL-----RRSI-----ATVFQDAGL 420
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-EKERKRIgyvpqRRSIdrdfpISVRDVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 421 -MNRSIGENIRLGREDAslDEVMAAAEAAAASDFIEDRLngydtvvGErgnrLSGGERQRVAIARAILKNAPILVLDEAT 499
Cdd:cd03235 94 gLYGHKGLFRRLSKADK--AKVDEALERVGLSELADRQI-------GE----LSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503610856 500 SALDVETEARVKDAIDALRKD-RTTFIIAHRLSTVRE-ADLVIFMDQG 545
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-548 |
9.17e-30 |
|
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: 116.20 E-value: 9.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 339 DISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIAtvtRKSLRRSIATVFQDA 418
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 G--LMNRSIGENIRLGREDASLDEvmaaaeaAAASDFIED-RLNGYDtvvgERGNR-LSGGERQRVAIARAILKNAPILV 494
Cdd:cd03226 81 DyqLFTDSVREELLLGLKELDAGN-------EQAETVLKDlDLYALK----ERHPLsLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 495 LDEATSALDVETEARVKDAIDAL-RKDRTTFIIAHR---LSTVreADLVIFMDQGRVV 548
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDyefLAKV--CDRVLLLANGAIV 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
334-551 |
1.17e-29 |
|
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: 115.73 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 334 EVEFRDISF-----DFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLL--QRVHEPKHGQILIDGVDIatvTRKS 406
Cdd:cd03213 3 TLSFRNLTVtvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 407 LRRSIATVFQDaglmnrsigenirlgredasldevmaaaeaaaasdfieDRLNGYDTV-------VGERGnrLSGGERQR 479
Cdd:cd03213 80 FRKIIGYVPQD--------------------------------------DILHPTLTVretlmfaAKLRG--LSGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 480 VAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKD-RTTFIIAHRLST--VREADLVIFMDQGRVVEMG 551
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
360-551 |
2.91e-29 |
|
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: 115.28 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 360 AGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtrKSLRRSIATVFQDAGLMNR-SIGENIRLGREDA-S 437
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRPVSMLFQENNLFAHlTVEQNVGLGLSPGlK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 438 LDEVMAAAEAAAAsdfiedRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDAL 517
Cdd:cd03298 101 LTAEDRQAIEVAL------ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 503610856 518 RKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:cd03298 175 HAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
335-558 |
5.20e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAnsaqGVR---NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATvTRKSLRR 409
Cdd:COG1129 5 LEMRGISKSFG----GVKaldGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRS-PRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 410 SIATVFQDAGLM-NRSIGENIRLGREDAS---LD---------EVMaaaeaaaasdfieDRLnGYD----TVVGErgnrL 472
Cdd:COG1129 80 GIAIIHQELNLVpNLSVAENIFLGREPRRgglIDwramrrrarELL-------------ARL-GLDidpdTPVGD----L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 473 SGGERQRVAIARAILKNAPILVLDEATSAL-DVETEaRVKDAIDALRKDRTTFI-IAHRLSTVRE-AD-LVIFMDqGRVV 548
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLtEREVE-RLFRIIRRLKAQGVAIIyISHRLDEVFEiADrVTVLRD-GRLV 219
|
250
....*....|
gi 503610856 549 EMGGFHELSQ 558
Cdd:COG1129 220 GTGPVAELTE 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
355-567 |
8.17e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.47 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 355 SFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTrkSLRRSIATVFQDAGLMNR-SIGENIRLG- 432
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--PAERPVSMLFQENNLFPHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 433 REDASLDE-----VMAAAEAAAASDFiEDRLNGydtvvgergnRLSGGERQRVAIARAILKNAPILVLDEATSALDVETE 507
Cdd:COG3840 97 RPGLKLTAeqraqVEQALERVGLAGL-LDRLPG----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 508 ARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQSNG--RFAALL 567
Cdd:COG3840 166 QEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPppALAAYL 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-552 |
1.00e-28 |
|
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: 113.72 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtrkslRRSI 411
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMN-RSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLNGYDTVVGERGNR------LSGGERQRVAIAR 484
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPK-----------AEARERAEELLELVGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAI-DALRKDRTTFI-IAHRLStvrEAdlvIFMDQgRVVEMGG 552
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETGKTVLlVTHDID---EA---VFLAD-RVVVLSA 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
351-551 |
3.12e-28 |
|
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: 118.63 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHePKHGQILIDGVDIATVTRK---SLRRSIATVFQD--AGL---MN 422
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDpfGSLsprMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 --RSIGE-----NIRLGRED------ASLDEVmaaaeaaaasdfiedrlnGYDTVVGER-GNRLSGGERQRVAIARA-IL 487
Cdd:COG4172 381 vgQIIAEglrvhGPGLSAAErrarvaEALEEV------------------GLDPAARHRyPHEFSGGQRQRIAIARAlIL 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 488 KnaP-ILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:COG4172 443 E--PkLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQG 508
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
335-556 |
3.30e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDF-ANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIAT 413
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGlmNRSIGENIR----LGREDASLD-EVMAAAEAAAASDFieDRLNGYDTvvgeRGNRLSGGERQRVAIARAILK 488
Cdd:PRK13648 88 VFQNPD--NQFVGSIVKydvaFGLENHAVPyDEMHRRVSEALKQV--DMLERADY----EPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 489 NAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA--HRLSTVREADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
349-556 |
7.65e-27 |
|
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: 108.68 E-value: 7.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATV-TRKSLRRSIATVFQDAGLMNR-SIG 426
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLG-------REDASLDEVMAAaeaaaasdF--IEDRLNgydtvvgERGNRLSGGERQRVAIARAILKNAPILVLDE 497
Cdd:cd03224 94 ENLLLGayarrraKRKARLERVYEL--------FprLKERRK-------QLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 498 ATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVeQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-551 |
8.63e-27 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 108.86 E-value: 8.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtrKSLRRSIATV 414
Cdd:cd03300 1 IELENVSKFYGGF-VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLMNR-SIGENIRLGREDASLDEVMAAAEAAAASDFIedRLNGYDtvvGERGNRLSGGERQRVAIARAILKNAPIL 493
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLV--QLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKD-RTTFI-IAHRLStvrEA----DLVIFMDQGRVVEMG 551
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVfVTHDQE---EAltmsDRIAVMNKGKIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-578 |
8.98e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.10 E-value: 8.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAN-SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIAT 413
Cdd:PRK13635 6 IRVEHISFRYPDaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDA---------------GLMNRSIGENIRLGREDASLDEVmaaaeaaAASDFIEdrlngydtvvgERGNRLSGGERQ 478
Cdd:PRK13635 86 VFQNPdnqfvgatvqddvafGLENIGVPREEMVERVDQALRQV-------GMEDFLN-----------REPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 479 RVAIArAILKNAP-ILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHE 555
Cdd:PRK13635 148 RVAIA-GVLALQPdIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 503610856 556 LSQSNG-------------RFAALLRASGILTDEDV 578
Cdd:PRK13635 227 IFKSGHmlqeigldvpfsvKLKELLKRNGILLPNTY 262
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
298-568 |
1.15e-26 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 115.81 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 298 QIFEARAKLEdffqlEDSVQDReePADAGELKGVVgeveFRDISFDFANSAQGVRN-VSFKAKAGQTIAIVGPTGAGKTT 376
Cdd:TIGR00957 611 RIFLSHEELE-----PDSIERR--TIKPGEGNSIT----VHNATFTWARDLPPTLNgITFSIPEGALVAVVGQVGCGKSS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 377 LVNLLQRVHEPKHGQILIDGvdiatvtrkslrrSIATVFQDAGLMNRSIGENIRLGR--EDASLDEVMAAAEAAAASDFI 454
Cdd:TIGR00957 680 LLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEACALLPDLEIL 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 455 EdrlNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAI---DALRKDRTTFIIAHRLS 531
Cdd:TIGR00957 747 P---SGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGIS 823
|
250 260 270
....*....|....*....|....*....|....*..
gi 503610856 532 TVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALLR 568
Cdd:TIGR00957 824 YLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLR 860
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-556 |
1.88e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 108.30 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 354 VSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR--------KSLRRSIATVFQDAGLM-NRS 424
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNFNLFpHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLGR---EDASLDEVMAAAEAAAASDFIEDRLNGYDtvvgergNRLSGGERQRVAIARAILKNAPILVLDEATSA 501
Cdd:PRK11264 102 VLENIIEGPvivKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 502 LDVETEARVKDAIDALRKD-RTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
351-555 |
3.81e-26 |
|
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: 107.14 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRSIATVFQDAGLMNR-SIGEN 428
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLGREDASLDEVMAAAEAAAASDFIE------DRLnGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSAL 502
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREAREraeellERV-GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 503 DVETEARVKDAIDALRKDRTTF-IIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHE 555
Cdd:cd03219 175 NPEETEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-568 |
4.41e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 334 EVEFRDISFdFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG------VDIATVTRKSL 407
Cdd:COG4161 2 SIQLKNINC-FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RRSIATVFQDAGLM-NRSIGENI--------RLGREDAsLDEVMAAAEAAAASDFiEDRLNgydtvvgergNRLSGGERQ 478
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLieapckvlGLSKEQA-REKAMKLLARLRLTDK-ADRFP----------LHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDASHF 228
|
250
....*....|...
gi 503610856 557 SQ-SNGRFAALLR 568
Cdd:COG4161 229 TQpQTEAFAHYLS 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
336-556 |
7.30e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 106.85 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFANSA--------QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL 407
Cdd:COG4167 6 EVRNLSKTFKYRTglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RRSIATVFQDAglmNRSIGENIRLGRedaSLDEVMaaaeaaaasdfiedRLNGyDTVVGERGNR---------------- 471
Cdd:COG4167 86 CKHIRMIFQDP---NTSLNPRLNIGQ---ILEEPL--------------RLNT-DLTAEEREERifatlrlvgllpehan 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 472 -----LSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFI-IAHRLSTVRE-ADLVIFMD 543
Cdd:COG4167 145 fyphmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLgISYIyVSQHLGIVKHiSDKVLVMH 224
|
250
....*....|...
gi 503610856 544 QGRVVEMGGFHEL 556
Cdd:COG4167 225 QGEVVEYGKTAEV 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-556 |
7.52e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.54 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANsAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHE--PK---HGQILIDGVDIATVTRKSLRR 409
Cdd:PRK14247 4 IEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 410 SIATVFQDAG-LMNRSIGENIRLG-------REDASLDE-VMAAAEAAAASDFIEDRLNGydtvvgeRGNRLSGGERQRV 480
Cdd:PRK14247 83 RVQMVFQIPNpIPNLSIFENVALGlklnrlvKSKKELQErVRWALEKAQLWDEVKDRLDA-------PAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAH-RLSTVREADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-551 |
7.99e-26 |
|
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: 105.53 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRsIATVFQDAGLMNR-SIGE 427
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 NIR-LGR-----EDASLDEVMAAAEAAAASDFIEDRLNGydtvvgergnrLSGGERQRVAIARAILKNAPILVLDEATSA 501
Cdd:cd03266 98 NLEyFAGlyglkGDELTARLEELADRLGMEELLDRRVGG-----------FSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503610856 502 LDVETEARVKDAIDALRKDRTTFIIA-HRLSTV-READLVIFMDQGRVVEMG 551
Cdd:cd03266 167 LDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-551 |
8.20e-26 |
|
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: 8.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKslRRSIA 412
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLM-NRSIGENI----RLGREDAS------------LDevmaaaeaaaasdfIEDRLNGYdtvVGErgnrLSGG 475
Cdd:COG3839 79 MVFQSYALYpHMTVYENIafplKLRKVPKAeidrrvreaaelLG--------------LEDLLDRK---PKQ----LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 476 ERQRVAIARAILKNAPILVLDEATSALD----VETEARVKdaiDALRKDRTTFIIA-HRLStvrEA----DLVIFMDQGR 546
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIK---RLHRRLGTTTIYVtHDQV---EAmtlaDRIAVMNDGR 211
|
....*
gi 503610856 547 VVEMG 551
Cdd:COG3839 212 IQQVG 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
336-551 |
1.01e-25 |
|
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: 111.31 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFANSAQG---VRNVSFKAKAGQTIAIVGPTGAGKT----TLVNLLQRVHEPKHGQILIDGVDIATVTRKSLR 408
Cdd:COG4172 8 SVEDLSVAFGQGGGTveaVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 409 R----SIATVFQDAG-----LMN--RSIGENIRL----GREDAS------LDEVMaaaeaaaasdfI---EDRLNGYDtv 464
Cdd:COG4172 88 RirgnRIAMIFQEPMtslnpLHTigKQIAEVLRLhrglSGAAARaralelLERVG-----------IpdpERRLDAYP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 465 vgergNRLSGGERQRVAIARAILkNAP-ILVLDEATSALDVETEARVKDAIDALRKDRTTFI--IAHRLSTVRE-ADLVI 540
Cdd:COG4172 155 -----HQLSGGQRQRVMIAMALA-NEPdLLIADEPTTALDVTVQAQILDLLKDLQRELGMALllITHDLGVVRRfADRVA 228
|
250
....*....|.
gi 503610856 541 FMDQGRVVEMG 551
Cdd:COG4172 229 VMRQGEIVEQG 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-551 |
1.08e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 109.35 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 350 GVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT----RKSLRRSIATVFQDAGLM-NRS 424
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLGREDASL--DEVMAAAEAAAASDFIEDRLNGYDtvvgergNRLSGGERQRVAIARAILKNAPILVLDEATSAL 502
Cdd:PRK10070 123 VLDNTAFGMELAGInaEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503610856 503 DVETEARVKDAIDAL--RKDRTTFIIAHRL-STVREADLVIFMDQGRVVEMG 551
Cdd:PRK10070 196 DPLIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
351-549 |
1.25e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.31 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR---KSLRRSIATVFQDA-GLMN--RS 424
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRaqrKAFRRDIQMVFQDSiSAVNprKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLG-REDASLDEVMAAAEAAAASDFIEDRlngyDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALD 503
Cdd:PRK10419 108 VREIIREPlRHLLSLDKAERLARASEMLRAVDLD----DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503610856 504 VETEARVKDAIDALRKDRTT--FIIAHRLSTV-READLVIFMDQGRVVE 549
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-556 |
1.57e-25 |
|
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: 108.28 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 354 VSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATvTRKSL-----RRSIATVFQDAGLM-NRSIGE 427
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIflppeKRRIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 NIRLGREDASLDEVMAAAEAAAasdfiedRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDvetE 507
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVI-------ELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD---D 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 508 ARVKDAIDALRKDRTTF-----IIAHRLSTV-READLVIFMDQGRVVEMGGFHEL 556
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFgipilYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
351-556 |
3.19e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 103.99 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKsLRRSIATVFQDAGLmnrsigENIR 430
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSV------DDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGREDASLDEVMAAAEAAAASDFIEDRLNGYDtvVGERGNRL----SGGERQRVAIARAILKNAPILVLDEATSALDVET 506
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDFVG--LLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503610856 507 EARVKDAIDALRK--DRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:cd03265 167 RAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
351-551 |
3.27e-25 |
|
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: 104.74 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIAT-----VTRKSLRRSiatvFQDAGLMNR-S 424
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphrIARLGIART----FQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLGREdASLDEVMAAAEAAAASDFIEDRLN-----------GYDTVVGERGNRLSGGERQRVAIARAILKNAPIL 493
Cdd:COG0411 96 VLENVLVAAH-ARLGRGLLAALLRLPRARREEREAreraeellervGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEG 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-565 |
3.95e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.02 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSI 411
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIRLGREdASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAP 491
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 492 ILVL-DEATS----ALDVETEARVKDAIDALrkdrTTFIIAHRLSTVREADLVIFMDQGRVVEMGG-----------FHE 555
Cdd:PTZ00243 1466 GFILmDEATAnidpALDRQIQATVMSAFSAY----TVITIAHRLHTVAQYDKIIVMDHGAVAEMGSprelvmnrqsiFHS 1541
|
250
....*....|
gi 503610856 556 LSQSNGRFAA 565
Cdd:PTZ00243 1542 MVEALGRSEA 1551
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
353-583 |
6.53e-25 |
|
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: 104.12 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATV---TRKSLRRSIATVFQDA-GLMN--RSIG 426
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDSpSAVNprMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLG-REDASLDEVMAAAEAAAASDFIEDRlngyDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVE 505
Cdd:TIGR02769 109 QIIGEPlRHLTSLDESEQKARIAELLDMVGLR----SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 506 TEARVKDAIDALRKDRTT--FIIAHRLSTV-READLVIFMDQGRVVEMGGFHELSQSNGRFAALLRASgILTDEDVRKSL 582
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTayLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSA-VLPEHPVRRSI 263
|
.
gi 503610856 583 T 583
Cdd:TIGR02769 264 T 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
78-571 |
6.64e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.07 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 78 READRLAHGRRASLlteAFGRIVSMPLSwhsqrgTSNALHTLlraCETLFGLWLEFMRqhlaTAVALMLLIPTAFAMDVR 157
Cdd:PLN03232 382 HKSLRLTHEARKNF---ASGKVTNMITT------DANALQQI---AEQLHGLWSAPFR----IIVSMVLLYQQLGVASLF 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 158 LSLILVVLGAAYVMISKVVMSRTKEGQaaveghyhtvfsHVSD---SISNvSVVHSYNRIEAETRElKKFTQRLLSAQYP 234
Cdd:PLN03232 446 GSLILFLLIPLQTLIVRKMRKLTKEGL------------QWTDkrvGIIN-EILASMDTVKCYAWE-KSFESRIQGIRNE 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 235 VLDWW---ALASGLNR-IASTISMMAILV-IGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARA---KL 306
Cdd:PLN03232 512 ELSWFrkaQLLSAFNSfILNSIPVVVTLVsFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVslqRI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 307 EDFFQLEDSVQDREEPADAGELKGVVGEVEFrdiSFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLqrVHE 386
Cdd:PLN03232 592 EELLLSEERILAQNPPLQPGAPAISIKNGYF---SWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGE 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 387 PKHgqilidgvdiATVTRKSLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFieDRLNGYD-TVV 465
Cdd:PLN03232 667 LSH----------AETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDL--DLLPGRDlTEI 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 466 GERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDA-IDALRKDRTTFIIAHRLSTVREADLVIFMDQ 544
Cdd:PLN03232 735 GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSE 814
|
490 500
....*....|....*....|....*..
gi 503610856 545 GRVVEMGGFHELSQSNGRFAALLRASG 571
Cdd:PLN03232 815 GMIKEEGTFAELSKSGSLFKKLMENAG 841
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
335-565 |
1.71e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.19 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQgVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiatVTRKSLR-RSIAT 413
Cdd:PRK11432 7 VVLKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQqRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLM-NRSIGENI-----RLGREDASLDEVMAAAEAAAASDFIEDRLNgydtvvgergNRLSGGERQRVAIARAIL 487
Cdd:PRK11432 83 VFQSYALFpHMSLGENVgyglkMLGVPKEERKQRVKEALELVDLAGFEDRYV----------DQISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 488 KNAPILVLDEATSALDVETEARVKDAIDALRK--DRTTFIIAHRLStvrEA----DLVIFMDQGRVVEMGGFHEL-SQSN 560
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQS---EAfavsDTVIVMNKGKIMQIGSPQELyRQPA 229
|
....*
gi 503610856 561 GRFAA 565
Cdd:PRK11432 230 SRFMA 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
344-551 |
2.08e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 344 FANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATVTR----KSLRRSIATVFQD 417
Cdd:PRK11124 11 FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSdkaiRELRRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 AGL------MNRSIGENIR---LGREDAsldevmaaaeaAAASDFIEDRLNgydtvVGERGNR----LSGGERQRVAIAR 484
Cdd:PRK11124 91 YNLwphltvQQNLIEAPCRvlgLSKDQA-----------LARAEKLLERLR-----LKPYADRfplhLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
351-551 |
2.99e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 100.79 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKslRRSIATVFQDAGLM-NRSIGENI 429
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALYpHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 RLGREDASLDEvmaaaeaaaasDFIEDRLN------GYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALD 503
Cdd:cd03301 94 AFGLKLRKVPK-----------DEIDERVRevaellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503610856 504 VETEARVKDAIDALRKD-RTTFI-IAH-RLSTVREADLVIFMDQGRVVEMG 551
Cdd:cd03301 163 AKLRVQMRAELKRLQQRlGTTTIyVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
355-567 |
4.86e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.81 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 355 SFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiATVTRKSlRRSIATVFQDAGLMNR-SIGENIRLG- 432
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPS-RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 433 ----REDASL-DEVMAAAEAAAASDFIEdRLNGydtvvgergnRLSGGERQRVAIARAILKNAPILVLDEATSALDVETE 507
Cdd:PRK10771 97 npglKLNAAQrEKLHAIARQMGIEDLLA-RLPG----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 508 ARVKDAIDALRKDR--TTFIIAHRLS-TVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALL 567
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
335-551 |
5.30e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.08 E-value: 5.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIaTVTRKSL---RRSI 411
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQ--DAGLMNRSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLNGYDTVVGERG------NRLSGGERQRVAIA 483
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFGPLNLGLSK-----------EEVEKRVKEALKAVGMEGfenkppHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 484 RAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTV-READLVIFMDQGRVVEMG 551
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
335-556 |
6.55e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.80 E-value: 6.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQ--DAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASdfiedRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPI 492
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSAL-----HMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 493 LVLDEATSALDVETEARVKDAIDALRKD--RTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
352-527 |
6.88e-24 |
|
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: 99.48 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtRKSLRRSIATVFQDAGLMNR-SIGENIR 430
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 L-------GREDASLDEVMAAAEaaaasdfIEDRLNgydtvvgERGNRLSGGERQRVAIARAILKNAPILVLDEATSALD 503
Cdd:COG4133 98 FwaalyglRADREAIDEALEAVG-------LAGLAD-------LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180
....*....|....*....|....
gi 503610856 504 VETEARVKDAIDALRKDRTTFIIA 527
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLT 187
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
334-551 |
9.51e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.92 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 334 EVEFRDISFDFANsAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiATVTRKSLRRSIAT 413
Cdd:COG1118 2 SIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLM-NRSIGENIRLG-----------REDAS--LDEVmaaaeaaaasdfiedRLNGYdtvvgerGNR----LSGG 475
Cdd:COG1118 80 VFQHYALFpHMTVAENIAFGlrvrppskaeiRARVEelLELV---------------QLEGL-------ADRypsqLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 476 ERQRVAIARAILKNAPILVLDEATSALDveteARVKDAIDA-LRK-----DRTTFIIAH-RLSTVREADLVIFMDQGRVV 548
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALD----AKVRKELRRwLRRlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIE 213
|
...
gi 503610856 549 EMG 551
Cdd:COG1118 214 QVG 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
353-555 |
1.05e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.28 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIA--TVTRKSLRRSIATVFQ--DAGLMNRSIGEN 428
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQypEYQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLGREDASLDEvmaaaeaaaasDFIEDRLN--------GYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATS 500
Cdd:PRK13637 105 IAFGPINLGLSE-----------EEIENRVKramnivglDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 501 ALDVETEARVKDAIDALRKDR--TTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHE 555
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-556 |
1.56e-23 |
|
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: 102.10 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG---VDIAT-VTRKSLRRSIATVFQDAGLM-NRSIGE 427
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 NIRLGREDASLDEvmaaaeaaaasdfiedRLNGYDTVVG--------ERG-NRLSGGERQRVAIARAILKNAPILVLDEA 498
Cdd:COG4148 97 NLLYGRKRAPRAE----------------RRISFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 499 TSALDVETEARVKDAIDALRKDRTTFII--AHRLSTV-READLVIFMDQGRVVEMGGFHEL 556
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILyvSHSLDEVaRLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
349-551 |
2.27e-23 |
|
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: 98.42 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTiAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIaTVTRKSLRRSIATVFQDAGLMNRSIGE- 427
Cdd:cd03264 14 RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVYPNFTVRe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 ---------NIRLGREDASLDEVMaaaeaaaasdfieDRLNGYDtVVGERGNRLSGGERQRVAIARAILKNAPILVLDEA 498
Cdd:cd03264 92 fldyiawlkGIPSKEVKARVDEVL-------------ELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503610856 499 TSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-547 |
3.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.81 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQG--VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIA 412
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKytLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQ--DAGLMNRSIGENIRLGREDASLD------EVMAAAEAAAASDFiEDRlngydtvvgeRGNRLSGGERQRVAIAR 484
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENKGIPheemkeRVNEALELVGMQDF-KER----------EPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVREADLVIFMDQGRV 547
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
335-556 |
3.19e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDI--ATVTRKSLRRSIA 412
Cdd:PRK09493 2 IEFKNVSKHFGPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLMNRSIG-ENIRLG--------REDAS------LDEVMaaaeaaaasdfIEDRLNGYDtvvgergNRLSGGER 477
Cdd:PRK09493 81 MVFQQFYLFPHLTAlENVMFGplrvrgasKEEAEkqarelLAKVG-----------LAERAHHYP-------SELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 478 QRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFII-AHRLSTVRE-ADLVIFMDQGRVVEMGGFHE 555
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
.
gi 503610856 556 L 556
Cdd:PRK09493 223 L 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
352-548 |
4.94e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.62 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiatVTRKSL-RRS--IATVFQD-----AGLMnr 423
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD---VTKLPEyKRAkyIGRVFQDpmmgtAPSM-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 424 SIGEN--------------IRLGRED--------ASLDevMAaaeaaaasdfIEDRLngyDTVVGErgnrLSGGERQRVA 481
Cdd:COG1101 98 TIEENlalayrrgkrrglrRGLTKKRrelfrellATLG--LG----------LENRL---DTKVGL----LSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 482 IARAILKNAPILVLDEATSALDVETEARVKDAIDAL--RKDRTTFIIAHRLstvREA----DLVIFMDQGRVV 548
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
353-551 |
8.10e-23 |
|
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: 96.98 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKaGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVdIATVTRKSL-----RRSIATVFQDAGLM-NRSIG 426
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGLVFQQYALFpHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLGredasldevMAAAEAAAASDFIEDRLN--GYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDV 504
Cdd:cd03297 94 ENLAFG---------LKRKRNREDRISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503610856 505 ETEARVKDAIDALRKD--RTTFIIAHRLSTV-READLVIFMDQGRVVEMG 551
Cdd:cd03297 165 ALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
334-551 |
1.17e-22 |
|
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: 97.02 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 334 EVEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiatVTRKSLR-RSIA 412
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED---ATDVPVQeRNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLMNR-SIGENIRLGREdasldevMAAAEAAAASDFIEDRLNGYDTVVGERG------NRLSGGERQRVAIARA 485
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLR-------VKPRSERPPEAEIRAKVHELLKLVQLDWladrypAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 486 ILKNAPILVLDEATSALDveteARVKDAIDA-LRK--DR---TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:cd03296 151 LAVEPKVLLLDEPFGALD----AKVRKELRRwLRRlhDElhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVG 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
351-567 |
1.40e-22 |
|
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: 96.59 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATV-TRKSLRRSIATVFQDAGLMNR-SIGEN 428
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVPEGRRIFPSlTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLG--------REDASLDEVMAAaeaaaasdF--IEDRLNgydtvvgERGNRLSGGERQRVAIARAILKNAPILVLDEA 498
Cdd:COG0410 99 LLLGayarrdraEVRADLERVYEL--------FprLKERRR-------QRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 499 TSALD---VEteaRVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQSNGRFAALL 567
Cdd:COG0410 164 SLGLApliVE---EIFEIIRRLNREGVTILLVeQNARFALEiADRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
338-556 |
1.96e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.77 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 338 RDISFdFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHE--PK---HGQILIDGVDIATVTRKS--LRRS 410
Cdd:PRK14239 9 SDLSV-YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQDAGLMNRSIGENIRLG------REDASLDE-VMAAAEAAAASDFIEDRLngYDTVVGergnrLSGGERQRVAIA 483
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKDRL--HDSALG-----LSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 484 RAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-551 |
2.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR-KSLRRSIAT 413
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQ--DAGLMNRSIGENIRLGREDASLDEVMAAAEAAAAsdFIEDRLNGYDTvvgERGNRLSGGERQRVAIARAILKNAP 491
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA--LAEIGLEKYRH---RSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDAL-RKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
351-555 |
2.82e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.24 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQD----AGLMNR--- 423
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHhltpEGITVRelv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 424 SIGENI------RLGREDASLdeVMAAAEAAAASDFIEDRLngydtvvgergNRLSGGERQRVAIARAILKNAPILVLDE 497
Cdd:PRK11231 98 AYGRSPwlslwgRLSAEDNAR--VNQAMEQTRINHLADRRL-----------TDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 498 ATSALDVETEARVKDAIDALR-KDRTTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHE 555
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEE 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
335-548 |
2.96e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDF----ANsaqgvRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATvTRKSLR 408
Cdd:COG3845 6 LELRGITKRFggvvAN-----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS-PRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 409 RSIATVFQDAGLMNR-SIGENIRLGREDA-----SLDEVMAAaeaaaasdfIEDRLNGY------DTVVGErgnrLSGGE 476
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIVLGLEPTkggrlDRKAARAR---------IRELSERYgldvdpDAKVED----LSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 477 RQRVAIARAILKNAPILVLDEATSAL-DVETEaRVKDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVV 548
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLtPQEAD-ELFEILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
352-549 |
3.09e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 95.58 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT---RKSLR-RSIATVFQDAGLM-NRSIG 426
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLRaRHVGFVFQSFQLLpTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRL-----GREDAS------LDEVMaaaeaaaasdfIEDRLNGYDtvvgergNRLSGGERQRVAIARAILKNAPILVL 495
Cdd:COG4181 109 ENVMLplelaGRRDARararalLERVG-----------LGHRLDHYP-------AQLSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 496 DEATSALDVETEARVKDAIDALRKDR-TTFIIA-HRLSTVREADLVIFMDQGRVVE 549
Cdd:COG4181 171 DEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
335-552 |
3.69e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQ-GVRNVSFKAKAGQTIAIVGPTGAGKTT---LVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRS 410
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQ--DAGLMNRSIGENIRLGREDASLD-EVMAAAEAAAASDFieDRLNGYDTvvgERGNrLSGGERQRVAIArAIL 487
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLENRAVPrPEMIKIVRDVLADV--GMLDYIDS---EPAN-LSGGQKQRVAIA-GIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 488 KNAP-ILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVREADLVIFMDQGRVVEMGG 552
Cdd:PRK13640 159 AVEPkIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
335-565 |
4.47e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDI--SFDfanSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtrKSLRRSIA 412
Cdd:PRK11607 20 LEIRNLtkSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLM-NRSIGENIRLGREDASLdevmaaaeaaaASDFIEDRLNGYDTVV------GERGNRLSGGERQRVAIARA 485
Cdd:PRK11607 95 MMFQSYALFpHMTVEQNIAFGLKQDKL-----------PKAEIASRVNEMLGLVhmqefaKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 486 ILKNAPILVLDEATSALDVETEARVK-DAIDAL-RKDRTTFIIAH-RLSTVREADLVIFMDQGRVVEMGGFHELSQS-NG 561
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHpTT 243
|
....
gi 503610856 562 RFAA 565
Cdd:PRK11607 244 RYSA 247
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
335-551 |
5.34e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 5.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAnSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGL-MNRSIGENIRLGR-------------EDASLDEVMAAAeaaaasdfiedrlnGYDTVVGERGNRLSGGERQRV 480
Cdd:PRK09536 83 PQDTSLsFEFDVRQVVEMGRtphrsrfdtwtetDRAAVERAMERT--------------GVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-551 |
1.79e-21 |
|
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: 92.73 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAnSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATvtrkslRRSIA 412
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAA------RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLM-NRSIGENIR-------LGREDASLDevmaaaeaaaasdfIEDRLNGYDtvVGERGNR----LSGGERQRV 480
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVylaqlkgLKKEEARRR--------------IDEWLERLE--LSEYANKrveeLSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFII-AHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
351-551 |
2.41e-21 |
|
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: 92.57 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATvTRKSLRRSIATVFQDAGLM-NRSIGENI 429
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFdELTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 RL-----GREDASLDEVMAAaeaaaasDFIEDRLNGY-DTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEATSALD 503
Cdd:cd03263 97 RFyarlkGLPKSEIKEEVEL-------LLRVLGLTDKaNKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503610856 504 VETEARVKDAIDALRKDRTTFIIAHrlsTVREADL----VIFMDQGRVVEMG 551
Cdd:cd03263 166 PASRRAIWDLILEVRKGRSIILTTH---SMDEAEAlcdrIAIMSDGKLRCIG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
351-551 |
3.43e-21 |
|
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: 91.89 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiaTVTRKSLRRSIATVFQDAGL-MNRSIGENI 429
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIGALIEAPGFyPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 R-----LGREDASLDEVMAAAeaaaasdfiedrlnGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDV 504
Cdd:cd03268 94 RllarlLGIRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503610856 505 ETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
351-567 |
5.39e-21 |
|
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: 93.38 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQIlidgvdiatvtRKSLRRSIATvfQDAGLMNRSIGENIR 430
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRISFSS--QFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGredASLDE------VMAAAEAAAASDFIEDRlngyDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDV 504
Cdd:cd03291 120 FG---VSYDEyryksvVKACQLEEDITKFPEKD----NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 505 ETEARVKDA-IDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALL 567
Cdd:cd03291 193 FTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
351-551 |
5.44e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGvdiatvtrkslrrSIATVFQDAGLMNRSI-G-EN 428
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSALLELGAGFHPELtGrEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRL-----GREDASLDEVMaaaeaaaasDFIED--RLNGY-DTVVGergnRLSGGERQRVAIARAILKNAPILVLDEATS 500
Cdd:COG1134 109 IYLngrllGLSRKEIDEKF---------DEIVEfaELGDFiDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503610856 501 ALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:COG1134 176 VGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
346-551 |
5.93e-21 |
|
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: 91.95 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 346 NSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLL-QRVHEPK--HGQILIDGVDiatVTRKSLRRSIATVFQ-DAGLM 421
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQP---RKPDQFQKCVAYVRQdDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 422 NRSIGE------NIRLGREDASldevmaAAEAAAASDFIEDRLNgyDTVVGerGNR---LSGGERQRVAIARAILKNAPI 492
Cdd:cd03234 95 GLTVREtltytaILRLPRKSSD------AIRKKRVEDVLLRDLA--LTRIG--GNLvkgISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 493 LVLDEATSALDVETEAR-VKDAIDALRKDRTTFIIAH--RLSTVREADLVIFMDQGRVVEMG 551
Cdd:cd03234 165 LILDEPTSGLDSFTALNlVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
76-575 |
1.00e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.12 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 76 VSREADRLAHGRRASLLTeafGRIVSMPlswhsqrgTSNAlHTLLRACETLFGLWLEFMRqhlaTAVALMLLIPTAFAMD 155
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTS---GKITNLM--------TTDA-EALQQICQQLHTLWSAPFR----IIIAMVLLYQQLGVAS 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 156 VRLSLILVVLgaayVMISKVVMSR----TKEGQAAVEghyhTVFSHVSDSISNVSVVHSYnrieaeTRElKKFTQRLLSA 231
Cdd:PLN03130 444 LIGSLMLVLM----FPIQTFIISKmqklTKEGLQRTD----KRIGLMNEVLAAMDTVKCY------AWE-NSFQSKVQTV 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 232 QYPVLDWWALASGLNRIASTIsMMAILVIGTVLvqrgelgvgeviAFiGFANLLIGRLDQMKAFA--------------- 296
Cdd:PLN03130 509 RDDELSWFRKAQLLSAFNSFI-LNSIPVLVTVV------------SF-GVFTLLGGDLTPARAFTslslfavlrfplfml 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 297 ----TQIFEARA---KLEDFFQLEDSVQDREEPADAGELKGVVGEVEFrdiSFDFANSAQGVRNVSFKAKAGQTIAIVGP 369
Cdd:PLN03130 575 pnliTQAVNANVslkRLEELLLAEERVLLPNPPLEPGLPAISIKNGYF---SWDSKAERPTLSNINLDVPVGSLVAIVGS 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 370 TGAGKTTLVNLLQRVHEPKHGQILIdgvdiatvtrksLRRSIATVFQDAGLMNRSIGENIRLGREDASLDEVMAAAEAAA 449
Cdd:PLN03130 652 TGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTAL 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 450 ASDFieDRLNGYD-TVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAI--DALRKdRTTFII 526
Cdd:PLN03130 720 QHDL--DLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCikDELRG-KTRVLV 796
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 503610856 527 AHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALLRASGILTD 575
Cdd:PLN03130 797 TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEE 845
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
336-540 |
1.01e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDfANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVF 415
Cdd:PRK10247 9 QLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 416 QDAGLMNRSIGEN------IRLGR--EDASLDEVMaaaeaaaasdfiedRLNGYDTVVGERGNRLSGGERQRVAIARAIL 487
Cdd:PRK10247 88 QTPTLFGDTVYDNlifpwqIRNQQpdPAIFLDDLE--------------RFALPDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 488 KNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFII--AHRLSTVREADLVI 540
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
329-556 |
1.67e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.85 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 329 KGVVGEVEFRDISFDFANSAQ----------GVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVD 398
Cdd:PRK15079 5 KKVLLEVADLKVHFDIKDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 399 I---ATVTRKSLRRSIATVFQD--AGLMNRS-----IGENIRLGREDASLDEVMaaaeaaaasdfieDRLNGYDTVVGER 468
Cdd:PRK15079 85 LlgmKDDEWRAVRSDIQMIFQDplASLNPRMtigeiIAEPLRTYHPKLSRQEVK-------------DRVKAMMLKVGLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 469 GN-------RLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADL 538
Cdd:PRK15079 152 PNlinryphEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDR 231
|
250
....*....|....*...
gi 503610856 539 VIFMDQGRVVEMGGFHEL 556
Cdd:PRK15079 232 VLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
335-569 |
1.81e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAG--LMNRSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLNGYDTVVGERGNR------LSGGERQRVAIARAI 486
Cdd:PRK13647 85 FQDPDdqVFSSTVWDDVAFGPVNMGLDK-----------DEVERRVEEALKAVRMWDFRdkppyhLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 487 LKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQSNGRFA 564
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
....*
gi 503610856 565 ALLRA 569
Cdd:PRK13647 234 AGLRL 238
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-545 |
4.09e-20 |
|
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: 89.31 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 342 FDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLV----NLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQD 417
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlailGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 AGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDfIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDE 497
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503610856 498 ATSALDVETEARVKDA--IDALRKD-RTTFIIAHRLSTVREADLVIFMDQG 545
Cdd:cd03290 167 PFSALDIHLSDHLMQEgiLKFLQDDkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
351-551 |
4.49e-20 |
|
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: 89.13 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGvdiatvtrkslrrSIATVFQ-DAGLMNRSIG-EN 428
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSLLGlGGGFNPELTGrEN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IR-----LGREDASLDEVMaaaeaaaasDFIED--RLNGY-DTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEATS 500
Cdd:cd03220 105 IYlngrlLGLSRKEIDEKI---------DEIIEfsELGDFiDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503610856 501 ALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-559 |
7.89e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.34 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 344 FANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGV------DIATVTRKSLRRSIATVFQD 417
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 AG-LMNRSIGENIRLGREDASLDEVMAAAEAAAAS-------DFIEDRLNgydtvvgERGNRLSGGERQRVAIARAILKN 489
Cdd:PRK14246 99 PNpFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEClrkvglwKEVYDRLN-------SPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 490 APILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHELSQS 559
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
353-558 |
2.69e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEP---KHGQILIDGVDIatvTRKSLRRSIATVFQD------------ 417
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDdlfiptltvreh 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 ----AGL-MNRSIGENIRLGREDASLDEVMAaaeaaaasdfiedrLNGYDTVVGERGNR--LSGGERQRVAIARAILKNA 490
Cdd:TIGR00955 120 lmfqAHLrMPRRVTKKEKRERVDEVLQALGL--------------RKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLST--VREADLVIFMDQGRVVEMGGFHELSQ 558
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
351-552 |
3.17e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVH--------EPK---HGQILIDG-VDIATVtrkslRRSIATVFQDA 418
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfrvEGKvtfHGKNLYAPdVDPVEV-----RRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 GLMNRSIGENIRLGRE----DASLDE-VMAAAEAAAASDFIEDRLNgydtvvgERGNRLSGGERQRVAIARAILKNAPIL 493
Cdd:PRK14243 101 NPFPKSIYDNIAYGARingyKGDMDElVERSLRQAALWDEVKDKLK-------QSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTV-READLVIFMDQgRVVEMGG 552
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFNV-ELTEGGG 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
349-551 |
3.56e-19 |
|
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: 91.02 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQI-------LIDGVDIATVTRKSLRRSIATVFQDAGLM 421
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 422 -NRSIGEN------IRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDtvvgergNRLSGGERQRVAIARAILKNAPILV 494
Cdd:TIGR03269 378 pHRTVLDNlteaigLELPDELARMKAVITLKMVGFDEEKAEEILDKYP-------DELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 495 LDEATSALDVETEARVKDAIDALRKD--RTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
349-551 |
3.88e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.29 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG-----VDIATVTRKSLRRSIAT----VFQDA- 418
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTewgfVHQHPr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 -GL-MNRSIGENI--RL---G-------REDAS--LDEVmaaaeaAAASDFIEDRLNGYdtvvgergnrlSGGERQRVAI 482
Cdd:PRK11701 100 dGLrMQVSAGGNIgeRLmavGarhygdiRATAGdwLERV------EIDAARIDDLPTTF-----------SGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 483 ARAiLKNAPILVL-DEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVR-EADLVIFMDQGRVVEMG 551
Cdd:PRK11701 163 ARN-LVTHPRLVFmDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
338-551 |
3.89e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.13 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 338 RDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQD 417
Cdd:PRK13548 6 RNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 AGL-----------MNRSIGENIRlGREDASLDEVMAAaeaaaasdfiedrlngydTVVGERGNR----LSGGERQRVAI 482
Cdd:PRK13548 85 SSLsfpftveevvaMGRAPHGLSR-AEDDALVAAALAQ------------------VDLAHLAGRdypqLSGGEQQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 483 ARAIL------KNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA--HRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-556 |
4.05e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.07 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG----------VDIATVTRKSLRR----SIATV 414
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgaDMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGL-------MNRSIGENIRL----GREDA------SLDEVmaaaeaaaasdfiedRLNGYDTVVGERGNRLSGGER 477
Cdd:PRK10261 110 FQEPMTslnpvftVGEQIAESIRLhqgaSREEAmveakrMLDQV---------------RIPEAQTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 478 QRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRT--TFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFH 554
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVE 254
|
..
gi 503610856 555 EL 556
Cdd:PRK10261 255 QI 256
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
336-549 |
4.42e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFAnsaqGVR---NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIA-TVTRKSLRRSI 411
Cdd:PRK11288 6 SFDGIGKTFP----GVKaldDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLM-NRSIGENIRLGREDASLDEVMAAAEAAAASDFIEdRLnGYDTVVGERGNRLSGGERQRVAIARAILKNA 490
Cdd:PRK11288 82 AIIYQELHLVpEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLE-HL-GVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 491 PILVLDEATSALDV-ETEaRVKDAIDALRKDRTTFI-IAHRLSTV-READLV-IFMDqGRVVE 549
Cdd:PRK11288 160 RVIAFDEPTSSLSArEIE-QLFRVIRELRAEGRVILyVSHRMEEIfALCDAItVFKD-GRYVA 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
335-551 |
5.83e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.85 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKslRRSIATV 414
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLM-NRSIGENIRLG-----REDASLDE-VMAAAEAAAASDFIEdrlngydtvvgERGNRLSGGERQRVAIARAIL 487
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqkTPAAEITPrVMEALRMVQLEEFAQ-----------RKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 488 KNAPILVLDEATSALDVETEARVKDAIDAL-RKDRTTFI-IAHrlsTVREA----DLVIFMDQGRVVEMG 551
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVfVTH---DQEEAltmsDRIVVMRDGRIEQDG 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
335-556 |
6.66e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.21 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATVTRKSLRRSIA 412
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAG--LMNRSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLN------GYDTVVGERGNRLSGGERQRVAIAR 484
Cdd:PRK13636 86 MVFQDPDnqLFSASVYQDVSFGAVNLKLPE-----------DEVRKRVDnalkrtGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 485 AILKNAPILVLDEATSALDVETEARVKDAIDALRK--DRTTFIIAHRLSTVR-EADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
352-553 |
7.01e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 7.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIatvTRKSLRRSIATV-FQDAGLMNRSIGENIR 430
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 -----LGREDASLDEVMAAAEAAAasdfIEDRLNGYdtvvgergnrLSGGERQRVAIARAILKNAPILVLDEATSALDVE 505
Cdd:PRK13539 96 fwaafLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503610856 506 TEARVKDAIDALRKDRTTFIIA-HrlstvreADLVIfmDQGRVVEMGGF 553
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIAAtH-------IPLGL--PGARELDLGPF 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
351-582 |
7.54e-19 |
|
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: 91.13 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQIlidgvdiatvtRKSLRRSIATvfQDAGLMNRSIGENIR 430
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFSP--QTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGredASLDEVMAAAEAAAASdfIEDRL----NGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVET 506
Cdd:TIGR01271 509 FG---LSYDEYRYTSVIKACQ--LEEDIalfpEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 507 EARV-KDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHELSQSNGRFAALL------------RASGIL 573
Cdd:TIGR01271 584 EKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaeRRNSIL 663
|
....*....
gi 503610856 574 TDEDVRKSL 582
Cdd:TIGR01271 664 TETLRRVSI 672
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
351-547 |
8.69e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.41 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIAT-VTRKSLRRSIATVFQD---AGL-MNRSI 425
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIAYVPEDrkrEGLvLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 GENIRLGRedasldevmaaaeaaaasdfiedrlngydtvvgergnRLSGGERQRVAIARAILKNAPILVLDEATSALDVE 505
Cdd:cd03215 96 AENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503610856 506 TEARVKDAIDALRKDRTTFIIahrLST-----VREADLVIFMDQGRV 547
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
217-540 |
8.75e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 8.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 217 ETRELKKFTQRLLSaqypVLD-WWALA------SGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRL 289
Cdd:COG4178 240 EAAERRRLRRRFDA----VIAnWRRLIrrqrnlTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGAL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 290 ----DQMKAFATQifeaRAKLEDFFQLEDSVQDREEPADAGELKGVV--GEVEFRDISFDFANSAQGVRNVSFKAKAGQT 363
Cdd:COG4178 316 swfvDNYQSLAEW----RATVDRLAGFEEALEAADALPEAASRIETSedGALALEDLTLRTPDGRPLLEDLSLSLKPGER 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 364 IAIVGPTGAGKTTLVNLL--------QRVHEPKHGQIL--------IDGvdiatvtrkSLRRSI-----ATVFQDAGLmn 422
Cdd:COG4178 392 LLITGPSGSGKSTLLRAIaglwpygsGRIARPAGARVLflpqrpylPLG---------TLREALlypatAEAFSDAEL-- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSIGENIRLGREDASLDEvmaaaeaaaasdfiEDRLngydtvvgerGNRLSGGERQRVAIARAILKNAPILVLDEATSAL 502
Cdd:COG4178 461 REALEAVGLGHLAERLDE--------------EADW----------DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
330 340 350
....*....|....*....|....*....|....*....
gi 503610856 503 DVETEARVKDAIDALRKDrTTFI-IAHRLSTVREADLVI 540
Cdd:COG4178 517 DEENEAALYQLLREELPG-TTVIsVGHRSTLAAFHDRVL 554
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
351-551 |
8.95e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.32 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGL-MNRSIGENI 429
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 RLGR---------EDASLDEVMAAaeaaaasdfiedrlngydTVVGERGNR----LSGGERQRVAIARAI--LKNAP--- 491
Cdd:COG4559 97 ALGRaphgssaaqDRQIVREALAL------------------VGLAHLAGRsyqtLSGGEQQRVQLARVLaqLWEPVdgg 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 492 --ILVLDEATSALD------VETEARvkdaiDALRKDRTTFIIAHRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:COG4559 159 prWLFLDEPTSALDlahqhaVLRLAR-----QLARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQG 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
336-546 |
9.70e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.60 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFAnsaqGVR---NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRV--HEPKHGQILIDGVDI-ATVTRKSLRR 409
Cdd:PRK13549 7 EMKNITKTFG----GVKaldNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 410 SIATVFQDAGLM-NRSIGENIRLGREdASLDEVMAAAEAAAASDFIEDRLNgYDTVVGERGNRLSGGERQRVAIARAILK 488
Cdd:PRK13549 83 GIAIIHQELALVkELSVLENIFLGNE-ITPGGIMDYDAMYLRAQKLLAQLK-LDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 489 NAPILVLDEATSALdVETEARV-KDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGR 546
Cdd:PRK13549 161 QARLLILDEPTASL-TESETAVlLDIIRDLKAHGIACIyISHKLNEVKAiSDTICVIRDGR 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
346-556 |
1.06e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 346 NSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILI-----------DGVDIATVTRK-----SLRR 409
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnHELITNPYSKKiknfkELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 410 SIATVFQ--DAGLMNRSIGENIRLG-------REDASLDEVMAAAEAAAASDFIEDRLNGydtvvgergnrLSGGERQRV 480
Cdd:PRK13631 117 RVSMVFQfpEYQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFG-----------LSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 481 AIArAILKNAP-ILVLDEATSALDVETEARVKDAI-DALRKDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13631 186 AIA-GILAIQPeILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
360-547 |
1.32e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 360 AGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtrkslRRSIATVFQDAGLMN-RSIGENIRLG-----R 433
Cdd:PRK11247 37 AGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDNVGLGlkgqwR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 434 EDA--SLDEVMaaaeaaaasdfIEDRLNGYDTVvgergnrLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVK 511
Cdd:PRK11247 112 DAAlqALAAVG-----------LADRANEWPAA-------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 503610856 512 DAIDALRKDR--TTFIIAHRLS-TVREADLVIFMDQGRV 547
Cdd:PRK11247 174 DLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
346-537 |
1.48e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 346 NSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILI-DGVDIATVTRKS-LRRSI-ATVfQDAGLMN 422
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRSeVPDSLpLTV-RDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 R--SIGENIRLGRED-ASLDEVMaaaeaaaasdfieDRLnGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEAT 499
Cdd:NF040873 82 RwaRRGLWRRLTRDDrAAVDDAL-------------ERV-GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 503610856 500 SALDVETEARVKDAIDALRKD-RTTFIIAHRLSTVREAD 537
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRAD 186
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
327-552 |
1.82e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 327 ELKGVVGEVEFRDIsfdfansaqgVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLL--QRVHEPKHGQILIDGVDI--ATV 402
Cdd:COG0396 2 EIKNLHVSVEGKEI----------LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDIleLSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 403 TRKSlRRSIATVFQD----AGLMN----RSIGENIRLGREDAS-----LDEVMAAAEAAaaSDFIEDRLNgydtvVGerg 469
Cdd:COG0396 72 DERA-RAGIFLAFQYpveiPGVSVsnflRTALNARRGEELSAReflklLKEKMKELGLD--EDFLDRYVN-----EG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 470 nrLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAH--RLSTVREADLVIFMDQGR 546
Cdd:COG0396 141 --FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGR 218
|
....*.
gi 503610856 547 VVEMGG 552
Cdd:COG0396 219 IVKSGG 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
349-546 |
2.59e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 84.02 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILID----GVDIATVT-RKSL---RRSIATVFQDAGL 420
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpREILalrRRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 421 MNRSIGENI------RLGR-EDASLDEVMAaaeaaaasdfIEDRLNgydtvVGERGNRL-----SGGERQRVAIARAILK 488
Cdd:COG4778 105 IPRVSALDVvaepllERGVdREEARARARE----------LLARLN-----LPERLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 489 NAPILVLDEATSALDVETEARVKDAIDALRKDRTTFI-IAHRLStVRE--ADLVIFMDQGR 546
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEE-VREavADRVVDVTPFS 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-551 |
2.68e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPK-----HGQILIDGVDIAT--VTRKSLRRSIATVFQDAG-LMN 422
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNpFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSIGENIRLG-------REDASLDEVMA-AAEAAAASDFIEDRLNGYDTvvgergnRLSGGERQRVAIARAILKNAPILV 494
Cdd:PRK14267 100 LTIYDNVAIGvklnglvKSKKELDERVEwALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 495 LDEATSALDVETEARVKDAIDALRKDRTTFIIAHR-LSTVREADLVIFMDQGRVVEMG 551
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-497 |
4.81e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.55 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 23 AIVIANIVLAAITIAepiLFGRIIDAISSQKDVAPMLLLW-----AGFGVFNTIAFVLVSREADRLAHGRRASLLteafG 97
Cdd:COG4615 17 LALLLGLLSGLANAG---LIALINQALNATGAALARLLLLfagllVLLLLSRLASQLLLTRLGQHAVARLRLRLS----R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 98 RIVSMPLSWHSQRGTSNALHTLLRACETL--FGLWLEFMRQHLATAVA----LMLLIPTAFAMdvrlSLILVVLGAA--Y 169
Cdd:COG4615 90 RILAAPLERLERIGAARLLAALTEDVRTIsqAFVRLPELLQSVALVLGclayLAWLSPPLFLL----TLVLLGLGVAgyR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 170 VMISKVV--MSRTKEGQAAVEGHYHTVF---------SHVSDSISNVSVVHSYNRIeaetRELKKFTQRllsaqypvldW 238
Cdd:COG4615 166 LLVRRARrhLRRAREAEDRLFKHFRALLegfkelklnRRRRRAFFDEDLQPTAERY----RDLRIRADT----------I 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 239 WALASGLnriastISMMAILVIGTVL---VQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARA---KLEDFFQL 312
Cdd:COG4615 232 FALANNW------GNLLFFALIGLILfllPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANValrKIEELELA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 313 EDSVQDREEPADAGELKGVVGEVEFRDISFDFANSAQG----VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPK 388
Cdd:COG4615 306 LAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 389 HGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSigenirLGREDASLDEvmaaaeaaaasdfiedRLNGY------D 462
Cdd:COG4615 386 SGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPA----------------RARELlerlelD 443
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 503610856 463 TVVGERGNR-----LSGGERQRVAIARAILKNAPILVLDE 497
Cdd:COG4615 444 HKVSVEDGRfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
348-559 |
4.98e-18 |
|
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: 83.34 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 348 AQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATV-TRKSLRRSIATVFQDAGLMNR-SI 425
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLpPHERARAGIAYVPQGREIFPRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 GENIRLGREdasldevmaaaEAAAASDFIEDRLngYD------TVVGERGNRLSGGERQRVAIARAILKNAPILVLDEAT 499
Cdd:TIGR03410 93 EENLLTGLA-----------ALPRRSRKIPDEI--YElfpvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 500 SALDVETEARVKDAIDALRKDRTTFII--AHRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQS 559
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILlvEQYLDFARElADRYYVMERGRVVASGAGDELDED 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-571 |
6.11e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.78 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIatvtRKSLRRSIatvfqdaGLM--------N 422
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRI-------GYLpeerglypK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSIGENIR-------LGREDA--SLDEVMaaaeaaaasdfieDRLNgydtvVGERGNR----LSGGERQRVAIARAILKN 489
Cdd:COG4152 86 MKVGEQLVylarlkgLSKAEAkrRADEWL-------------ERLG-----LGDRANKkveeLSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 490 APILVLDEATSALD---VETearVKDAIDALRKDRTTfII--AHRLSTV-READLVIFMDQGRVVEMGGFHELSQSNGRF 563
Cdd:COG4152 148 PELLILDEPFSGLDpvnVEL---LKDVIRELAAKGTT-VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGRN 223
|
....*...
gi 503610856 564 AALLRASG 571
Cdd:COG4152 224 TLRLEADG 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
333-547 |
7.10e-18 |
|
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: 84.14 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKhGQILIDGVDIATVTRKSLRRSI 411
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIRlGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAP 491
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRV 547
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
319-548 |
7.58e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.15 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 319 REEPADAGELKGVVGEvEFRDIsfdfansaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVd 398
Cdd:cd03267 14 SKEPGLIGSLKSLFKR-KYREV--------EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 399 IATVTRKSLRRSIATVF-QDAGLM-NRSIGENIRLGREDASLDEVMAAAEAAAASDF--IEDRLngyDTVVgergNRLSG 474
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFgQKTQLWwDLPVIDSFYLLAAIYDLPPARFKKRLDELSELldLEELL---DTPV----RQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 475 GERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFII--AHRLSTV-READLVIFMDQGRVV 548
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLL 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
351-551 |
8.21e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRK-------------SLRRSIATVFQD 417
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 AGLMNR-SIGENIR------LGREDASLDEvmaaaeaaaASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNA 490
Cdd:PRK10619 101 FNLWSHmTVLENVMeapiqvLGLSKQEARE---------RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDALRKD-RTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
351-558 |
1.02e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEP----KHGQILIDGVDIATvtrKSLR-RSIATVFQDA-GLMN-- 422
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP---CALRgRKIATIMQNPrSAFNpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSIGENIR-----LGRE--DASLDEVMAAAEaaaasdfIEDRlngyDTVVGERGNRLSGGERQRVAIARAILKNAPILVL 495
Cdd:PRK10418 96 HTMHTHARetclaLGKPadDATLTAALEAVG-------LENA----ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 496 DEATSALDVETEARVKDAIDALRKDRT--TFIIAHRLSTV-READLVIFMDQGRVVEMGGFHELSQ 558
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
335-551 |
1.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.21 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQG-----VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiaTVTRKSL-- 407
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLwd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 -RRSIATVFQ--DAGLMNRSIGENIRLGREDASLDevmaaaeaaaaSDFIEDRLNGYDTVVGERGNR------LSGGERQ 478
Cdd:PRK13633 83 iRNKAGMVFQnpDNQIVATIVEEDVAFGPENLGIP-----------PEEIRERVDESLKKVGMYEYRrhaphlLSGGQKQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-571 |
1.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.34 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAN----SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR----KS 406
Cdd:PRK13641 3 IKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 407 LRRSIATVFQ--DAGLMNRSIGENIRLGRED--ASLDEVMAAAEAAAAsdfiedRLNGYDTVVGERGNRLSGGERQRVAI 482
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKALKWLK------KVGLSEDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 483 ARAILKNAPILVLDEATSALDVETEARVKDA-IDALRKDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGG----F--- 553
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASpkeiFsdk 236
|
250 260
....*....|....*....|....
gi 503610856 554 -----HELSQ-SNGRFAALLRASG 571
Cdd:PRK13641 237 ewlkkHYLDEpATSRFASKLEKGG 260
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
335-551 |
1.92e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQgVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATV 414
Cdd:COG4604 2 IEIKNVSKRYGGKVV-LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGLMNR--------------SIGeniRLGRED-ASLDEVMaaaeaaaasDF-----IEDRlngY-DTvvgergnrLS 473
Cdd:COG4604 81 RQENHINSRltvrelvafgrfpySKG---RLTAEDrEIIDEAI---------AYldledLADR---YlDE--------LS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 474 GGERQRVAIARAILKNAPILVLDEATSALD----VETEARVKDAIDALrkDRTTFIIAHRLS-TVREADLVIFMDQGRVV 548
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL--GKTVVIVLHDINfASCYADHIVAMKDGRVV 215
|
...
gi 503610856 549 EMG 551
Cdd:COG4604 216 AQG 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-503 |
2.08e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKS---LRRSI 411
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAG-LMNRSIGEN--IRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTvvgergnRLSGGERQRVAIARAILK 488
Cdd:PRK10908 82 GMIFQDHHlLMDRTVYDNvaIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170
....*....|....*
gi 503610856 489 NAPILVLDEATSALD 503
Cdd:PRK10908 155 KPAVLLADEPTGNLD 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-551 |
2.19e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGK-TTLVNLLQRVhePKHGQILIDGVDIATVTRKSL---RRSIATVFQD--AGLMNRS 424
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKsTTGLALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 -----IGENIRL-------GREDASLDEVMAAAeaaaasdfiedrlnGYDTVVGER-GNRLSGGERQRVAIARAILKNAP 491
Cdd:PRK15134 380 nvlqiIEEGLRVhqptlsaAQREQQVIAVMEEV--------------GLDPETRHRyPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALR-KDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLfISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
352-549 |
3.17e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVdiaTVTRKSLRRSIatVFQDAGLMN-RSIGENIR 430
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAERGV--VFQNEGLLPwRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGREDASLDEVMAAAEAAAASDFIEdrLNGYDTvvgERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARV 510
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKKVG--LEGAEK---RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503610856 511 KDAIDAL--RKDRTTFIIAHrlsTVREA-----DLVIFM-DQGRVVE 549
Cdd:PRK11248 168 QTLLLKLwqETGKQVLLITH---DIEEAvfmatELVLLSpGPGRVVE 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
354-509 |
4.38e-17 |
|
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: 79.84 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 354 VSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtRKSLRRSIATVFQDAGLMNR-SIGENIRLG 432
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 433 REDASLDEVMAAAEAAAasdfiedrLNGYDTVVGergNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEAR 509
Cdd:cd03231 98 HADHSDEQVEEALARVG--------LNGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-551 |
4.59e-17 |
|
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: 80.90 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQ---IL---IDGVDIATvtrksLR 408
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDVWE-----LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 409 RSIATVfqDAGLMNR-----------------SIGENIRLGREDASL-DEVMaaaeaaaasdfieDRLNgydtvVGERGN 470
Cdd:COG1119 78 KRIGLV--SPALQLRfprdetvldvvlsgffdSIGLYREPTDEQRERaRELL-------------ELLG-----LAHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 471 R----LSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIahrLSTVREADL------VI 540
Cdd:COG1119 138 RpfgtLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLV---LVTHHVEEIppgithVL 214
|
250
....*....|.
gi 503610856 541 FMDQGRVVEMG 551
Cdd:COG1119 215 LLKDGRVVAAG 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
351-556 |
5.03e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 80.59 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIatvTRKSLRRSIatVFQDAGLMN-RSIGENI 429
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRMV--VFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 RLgredaSLDEVMAAAEAAAASDFIEDRLN--GYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETE 507
Cdd:TIGR01184 76 AL-----AVDRVLPDLSKSERRAIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 508 ARVKDAIDALRKDR--TTFIIAHrlsTVREA----DLVIFMDQGRVVEMGGFHEL 556
Cdd:TIGR01184 151 GNLQEELMQIWEEHrvTVLMVTH---DVDEAlllsDRVVMLTNGPAANIGQILEV 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
351-551 |
5.55e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR---KSLRRSIATVFQD--AGLMNR-- 423
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDpyASLDPRqt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 424 ---SIGENIR---LGREDASLDEVMaaaeaaaasdFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDE 497
Cdd:PRK10261 420 vgdSIMEPLRvhgLLPGKAAAARVA----------WLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 498 ATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTV-READLVIFMDQGRVVEMG 551
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
338-549 |
5.75e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 338 RDISFDFANSAQG---VRNVSFKAKAGQTIAIVGPTGAGKT-TLVNLLQRVHEPK----HGQILIDGVDIATVTRKSLRR 409
Cdd:PRK15134 9 ENLSVAFRQQQTVrtvVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 410 ----SIATVFQDAGL-------MNRSIGENIRLGR---EDASLDEVMAAAEAAAASDfIEDRLNGYDtvvgergNRLSGG 475
Cdd:PRK15134 89 vrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLHRgmrREAARGEILNCLDRVGIRQ-AAKRLTDYP-------HQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 476 ERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRK--DRTTFIIAHRLSTVRE-ADLVIFMDQGRVVE 549
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVE 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
361-528 |
7.16e-17 |
|
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: 80.53 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 361 GQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKslrrsIATVFQdaglmnrsigenirlGREDASLDE 440
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-----IKADYE---------------GTVRDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 441 VmaAAEAAAASDFIEDRLN--GYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAID--A 516
Cdd:cd03237 85 I--TKDFYTHPYFKTEIAKplQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfA 162
|
170
....*....|..
gi 503610856 517 LRKDRTTFIIAH 528
Cdd:cd03237 163 ENNEKTAFVVEH 174
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
351-551 |
8.43e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.69 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKT----TLVNLLQrvhepKHGQI----LIDGVDIATVTRKSLRR----SIATVFQDA 418
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-----ANGRIggsaTFNGREILNLPEKELNKlraeQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 glMNrSIGENIRLGREdasLDEVMAAAEAAAASDFIEDRLNGYDTV-VGERGNRL-------SGGERQRVAIARAILKNA 490
Cdd:PRK09473 107 --MT-SLNPYMRVGEQ---LMEVLMLHKGMSKAEAFEESVRMLDAVkMPEARKRMkmyphefSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDALRKDRTTFI--IAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGiCDKVLVMYAGRTMEYG 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-549 |
9.11e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVdiaTVTRKSLRRsiA 412
Cdd:COG4525 5 TVRHVSVRYPGGGQPQpalQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 413 TVFQDAGLMN-RSIGENIRLGREdasLDEVMAAAEAAAASDFIedRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAP 491
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLR---LRGVPKAERRARAEELL--ALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDAL--RKDRTTFIIAHrlsTVREA-----DLVIfMD--QGRVVE 549
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVEEAlflatRLVV-MSpgPGRIVE 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-556 |
1.55e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.14 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 334 EVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIAT 413
Cdd:PRK13642 6 EVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQ--DAGLMNRSIGENIRLGREDASL--DEVMAAAEAAAASdfiedrLNGYDTVVGERGnRLSGGERQRVAIARAILKN 489
Cdd:PRK13642 86 VFQnpDNQFVGATVEDDVAFGMENQGIprEEMIKRVDEALLA------VNMLDFKTREPA-RLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 490 APILVLDEATSALDVETEARVKDAIDALrKDR---TTFIIAHRLSTVREADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
351-553 |
1.88e-16 |
|
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: 77.95 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPK--HGQILIDGVDI--ATVTRKSlRRSIATVFQdaglmnrsig 426
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDItdLPPEERA-RLGIFLAFQ---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 enirlgrEDASLDEVmaaaeaaAASDFIEDrLNgydtvVGergnrLSGGERQRVAIARAILKNAPILVLDEATSALDVET 506
Cdd:cd03217 85 -------YPPEIPGV-------KNADFLRY-VN-----EG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503610856 507 EARVKDAIDALRKDRTTF-IIAH--RLSTVREADLVIFMDQGRVVEMGGF 553
Cdd:cd03217 140 LRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
21-304 |
3.20e-16 |
|
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: 79.40 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIAnIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGF----GVFNTIAFVLVSREADRLAHGRRASLlteaF 96
Cdd:cd18551 2 ILALLLS-LLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALfllqAVLSALSSYLLGRTGERVVLDLRRRL----W 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 97 GRIVSMPLSWHSQRGTSNALH------TLLRacetlfglwlEFMRQHLATAVALMLLIPTAFAM----DVRLSLI----L 162
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSrvtndtTLLR----------ELITSGLPQLVTGVLTVVGAVVLmfllDWVLTLVtlavV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 163 VVLGAAYVMISKVVMSRTKEGQAAVeGHYHTVFSHVsdsISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALA 242
Cdd:cd18551 147 PLAFLIILPLGRRIRKASKRAQDAL-GELSAALERA---LSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALI 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 243 SGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARA 304
Cdd:cd18551 223 GPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALG 284
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
351-580 |
4.23e-16 |
|
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: 77.97 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRSIATVFQDAGLMNR-SIGEN 428
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLGREDASLDEvmaaaeaaaasDFIEDRLN------GYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSAL 502
Cdd:cd03218 96 ILAVLEIRGLSK-----------KEREEKLEelleefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 503 DVETEARVKDAIDALrKDRT--TFIIAHrlsTVRE----ADLVIFMDQGRVVEMGGFHElsqsngrfaallrasgILTDE 576
Cdd:cd03218 165 DPIAVQDIQKIIKIL-KDRGigVLITDH---NVREtlsiTDRAYIIYEGKVLAEGTPEE----------------IAANE 224
|
....
gi 503610856 577 DVRK 580
Cdd:cd03218 225 LVRK 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
351-516 |
5.74e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.63 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATvTRKSLRRSIATVFQDAGLMNR-SIGENI 429
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGHLPGLKPElSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 RLGREDASLDEVMaaaeaaaasdfIEDRLngydTVVGERG------NRLSGGERQRVAIARAILKNAPILVLDEATSALD 503
Cdd:TIGR01189 95 HFWAAIHGGAQRT-----------IEDAL----AAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170
....*....|...
gi 503610856 504 VETEARVKDAIDA 516
Cdd:TIGR01189 160 KAGVALLAGLLRA 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
334-555 |
6.16e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 334 EVEFRDISFDF----ANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR----- 404
Cdd:PRK13651 2 QIKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 405 -------------------KSLRRSIATVFQDA--GLMNRSIGENIRLG-------REDAsldevmaaaeAAAASDFIEd 456
Cdd:PRK13651 82 kvleklviqktrfkkikkiKEIRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEA----------KKRAAKYIE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 457 rLNGYDTVVGERGN-RLSGGERQRVAIArAILKNAP-ILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTV 533
Cdd:PRK13651 151 -LVGLDESYLQRSPfELSGGQKRRVALA-GILAMEPdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLDNV 228
|
250 260
....*....|....*....|...
gi 503610856 534 RE-ADLVIFMDQGRVVEMGGFHE 555
Cdd:PRK13651 229 LEwTKRTIFFKDGKIIKDGDTYD 251
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-556 |
1.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSA----QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR----KS 406
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 407 LRRSIATVFQ--DAGLMNRSIGENIRLGRED--ASLDEVMAAAEaaaasDFIEDrLNGYDTVVGERGNRLSGGERQRVAI 482
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYAH-----RLLMD-LGFSRDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 483 ARAILKNAPILVLDEATSALDVETEARVKDAIDALRKD--RTTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-553 |
1.06e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.38 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKhGQILIDG--------VDIATVTRKS 406
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 407 LRRSIATVFQDAGLMNRSIGENIRLG------REDASLDEVMAAAEAAAAS-DFIEDRLNgydtvvgERGNRLSGGERQR 479
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDADLwDEIKHKIH-------KSALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 480 VAIARAILKNAPILVLDEATSALDVETEARVKDAIDA--LRKDRTTFIIAHRLSTV-READLVIFM--DQGRVVEMGGF 553
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVsRLSDFTAFFkgNENRIGQLVEF 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
365-559 |
1.11e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.76 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 365 AIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG---VDIATvtRKSL---RRSIATVFQDAGLM-NRSIGENIRLG--RED 435
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEK--GICLppeKRRIGYVFQDARLFpHYKVRGNLRYGmaKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 436 ASL-DEVMAAAEaaaasdfIEDRLNGYDTvvgergnRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAI 514
Cdd:PRK11144 106 VAQfDKIVALLG-------IEPLLDRYPG-------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503610856 515 DALRKDRTTFII--AHRLSTV-READLVIFMDQGRVVEMGGFHELSQS 559
Cdd:PRK11144 172 ERLAREINIPILyvSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
360-559 |
1.17e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 360 AGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQD----AGLMNRSI---------G 426
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlpaaEGMTVRELvaigrypwhG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLGRED-ASLDEVMAaaeaaaasdfiedrLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVE 505
Cdd:PRK10575 116 ALGRFGAADrEKVEEAIS--------------LVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 506 TEARVKDAIDALRKDRTTFIIA--HRLS-TVREADLVIFMDQGRVVEMGGFHELSQS 559
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-559 |
1.21e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAgqTIAIVGPTGAGKTTLVNLLQRVHEP-----KHGQILIDGVDIATVTRK-SLRRSIATVFQDAGLMNRSIG 426
Cdd:PRK14271 41 SMGFPARA--VTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFPMSIM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLG--------RED------ASLDEVmaaaeaaAASDFIEDRLNgydtvvgERGNRLSGGERQRVAIARAILKNAPI 492
Cdd:PRK14271 119 DNVLAGvrahklvpRKEfrgvaqARLTEV-------GLWDAVKDRLS-------DSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 493 LVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLS-TVREADLVIFMDQGRVVEMGGFHELSQS 559
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-566 |
1.23e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.75 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 334 EVEFRDISF------DFANSAQGVRNVSFKAkaGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR--- 404
Cdd:PRK13634 2 DITFQKVEHryqyktPFERRALYDVNVSIPS--GSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 405 -KSLRRSIATVFQ--DAGLMNRSIGENIRLG-------REDAsldevmaaaeAAAASDFIEdrLNGYDTVVGERGN-RLS 473
Cdd:PRK13634 80 lKPLRKKVGIVFQfpEHQLFEETVEKDICFGpmnfgvsEEDA----------KQKAREMIE--LVGLPEELLARSPfELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 474 GGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTV-READLVIFMDQGRVVEM 550
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAaRYADQIVVMHKGTVFLQ 227
|
250
....*....|....*.
gi 503610856 551 GGFHELSQSNGRFAAL 566
Cdd:PRK13634 228 GTPREIFADPDELEAI 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
351-551 |
1.32e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.59 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDgvdiatvtrkslrRSIATVFQDAGLMNRSIGENIR 430
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGREDASLDEVMAAAEAAAASDfIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEAR- 509
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERv 821
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503610856 510 VKDAIDALRKDRTTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
349-552 |
1.63e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAglmNRSIGEN 428
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLGRedasLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNR-------LSGGERQRVAIARAILKNAPILVLDEATSA 501
Cdd:PRK15112 104 QRISQ----ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHasyyphmLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503610856 502 LDVETEARVKDAIDALR-KDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMGG 552
Cdd:PRK15112 180 LDMSMRSQLINLMLELQeKQGISYIyVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
351-531 |
2.06e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT---RKSLR-RSIATVFQDAGLM-NRSI 425
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRnQKLGFIYQFHHLLpDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 GENIrlgredasldeVMAAAEAAAASDFIEDRLNGYDTVVG------ERGNRLSGGERQRVAIARAiLKNAPILVL-DEA 498
Cdd:PRK11629 105 LENV-----------AMPLLIGKKKPAEINSRALEMLAAVGlehranHRPSELSGGERQRVAIARA-LVNNPRLVLaDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503610856 499 TSALDveteARVKDAIDAL-----RKDRTTFII-------AHRLS 531
Cdd:PRK11629 173 TGNLD----ARNADSIFQLlgelnRLQGTAFLVvthdlqlAKRMS 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-555 |
2.13e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILI-DGVDIATVT--RKSLRrsi 411
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDqhQEELD--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 atvfqdaglMNRSIGENIRLGREDASLDEVMaaaeaaaasDFIEDRLNGYDTV---VGergnRLSGGERQRVAIARAILK 488
Cdd:COG0488 392 ---------PDKTVLDELRDGAPGGTEQEVR---------GYLGRFLFSGDDAfkpVG----VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 489 NAPILVLDEATSALDVETearvKDAI-DALRK-DRTTFIIAH-R--LSTVreADLVIFMDQGRVVE-MGGFHE 555
Cdd:COG0488 450 PPNVLLLDEPTNHLDIET----LEALeEALDDfPGTVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-580 |
3.19e-15 |
|
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: 78.69 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRV--HEPKHGQIL------------------- 393
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 394 --------------IDGVDIATVTRKSLRRSIATVFQD--AGLMNRSIGENIRLGREDA--SLDEVMAAAEAAAASDFIE 455
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRtfALYGDDTVLDNVLEALEEIgyEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 456 DRLNgydtvvgERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR-TTFIIAHRLSTVR 534
Cdd:TIGR03269 160 HRIT-------HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEVI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 535 E--ADLVIFMDQGRVVEMGG-------FHELSQSNGRFAALLRASGILTDEDVRK 580
Cdd:TIGR03269 233 EdlSDKAIWLENGEIKEEGTpdevvavFMEGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-529 |
3.96e-15 |
|
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: 73.34 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQ--------RVHEPKHGQILIdgvdiatVTRK- 405
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLF-------LPQRp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 406 -----SLRRSIATVFQDAglmnrsigenirlgredasldevmaaaeaaaasdfiedrlngydtvvgergnrLSGGERQRV 480
Cdd:cd03223 74 ylplgTLREQLIYPWDDV-----------------------------------------------------LSGGEQQRL 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVkdaIDALRKDRTTFI-IAHR 529
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-556 |
4.16e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.66 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATvTRKSLRRSIATVF------------QDA 418
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVFgqrsqlwwdlpaIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 GLMNRSIgenIRLGRED-----ASLDEVMAaaeaaaasdfIEDRLNgydTVVgeRgnRLSGGERQRVAIARAILKNAPIL 493
Cdd:COG4586 117 FRLLKAI---YRIPDAEykkrlDELVELLD----------LGELLD---TPV--R--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRKDR-TTFIIA-HRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEEL 242
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
354-555 |
5.18e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 354 VSFKAKAGQTIAIVGPTGAGKTTlvnLLQRVH--EPKHGQILIDGVDIATVTRKSLRRSIATVFQD---AGLMnrSIGEN 428
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST---LLARMAglLPGQGEILLNGRPLSDWSAAELARHRAYLSQQqspPFAM--PVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLGREDASLDEVMAAAEAAAASDF-IEDRLNgydtvvgeRG-NRLSGGERQRVAIARAILK-------NAPILVLDEAT 499
Cdd:COG4138 90 LALHQPAGASSEAVEQLLAQLAEALgLEDKLS--------RPlTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 500 SALDVETEArvkdAIDAL-----RKDRTTFIIAHRLS-TVREADLVIFMDQGRVVEMGGFHE 555
Cdd:COG4138 162 NSLDVAQQA----ALDRLlrelcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
336-561 |
5.97e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.84 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFANSAQGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL----R 408
Cdd:PRK10535 6 ELKDIRRSYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 409 RSIATVFQDAGLMNR--------------SIGENIRLGREDASLDevmaaaeaaaasdfiedRLnGYDTVVGERGNRLSG 474
Cdd:PRK10535 86 EHFGFIFQRYHLLSHltaaqnvevpavyaGLERKQRLLRAQELLQ-----------------RL-GLEDRVEYQPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 475 GERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAHRLSTVREADLVIFMDQGRVVEMGGF 553
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPA 227
|
....*...
gi 503610856 554 HELSQSNG 561
Cdd:PRK10535 228 QEKVNVAG 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
352-556 |
6.49e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLM-NRSIGENIR 430
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPgDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGR-------------EDASLDEVMaaaeaaaasdfiedRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDE 497
Cdd:PRK10253 104 RGRyphqplftrwrkeDEEAVTKAM--------------QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 498 ATSALDVETEARVKDAIDALRKDR--TTFIIAHRLS-TVREADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-556 |
6.94e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSA----QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRK--- 405
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 406 --SLRRSIATVFQ--DAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRlngyDTVVGERGNRLSGGERQRVA 481
Cdd:PRK13645 85 vkRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP----EDYVKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 482 IARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFII--AHRLSTV-READLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVlRIADEVIVMHEGKVISIGSPFEI 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-535 |
7.67e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.41 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEVEFRDISFDFANSAQGV-RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKhGQILIDGVDIATVTRKSLRRSI 411
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLMNRSIGENIRlGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAP 491
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVRE 535
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
335-551 |
9.24e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.89 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiatVTRKSLR-RSIAT 413
Cdd:PRK10851 3 IEIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTD---VSRLHARdRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLMNR-SIGENIRLG------REDASLDEVMAAAEAAAASDFIEDRLNGYDTvvgergnRLSGGERQRVAIARAI 486
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPA-------QLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 487 LKNAPILVLDEATSALD--VETEARvkdaiDALRK-----DRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK10851 152 AVEPQILLLDEPFGALDaqVRKELR-----RWLRQlheelKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAG 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-528 |
1.37e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 358 AKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDgVDIA----------TVTRKSLRRSIATVFqDAGLMNRSIGE 427
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISykpqyikpdyDGTVEDLLRSITDDL-GSSYYKSEIIK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 NIRLgredasldevmaaaeaaaasdfieDRLngYDTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEATSALDVETE 507
Cdd:PRK13409 440 PLQL------------------------ERL--LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180
....*....|....*....|...
gi 503610856 508 ARVKDAID--ALRKDRTTFIIAH 528
Cdd:PRK13409 490 LAVAKAIRriAEEREATALVVDH 512
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
353-551 |
1.87e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR----KSLRRSIATVFQ--DAGLMNRSIG 426
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQfpESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLGRED--ASLDEVMAAAEAAAasdfiedRLNGYDTVVGERGN-RLSGGERQRVAIArAILKNAP-ILVLDEATSAL 502
Cdd:PRK13649 105 KDVAFGPQNfgVSQEEAEALAREKL-------ALVGISESLFEKNPfELSGGQMRRVAIA-GILAMEPkILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503610856 503 DVETEARVKDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
351-512 |
2.26e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 72.13 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPK---HGQILIDGVDIATVtrKSLRRSIATVFQDAGLM-NRSIG 426
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIGILFQDDLLFpHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLG------------REDASLDEVmaaaeaaaasdfiedRLNGYdtvvgerGNR----LSGGERQRVAIARAILKNA 490
Cdd:COG4136 95 ENLAFAlpptigraqrraRVEQALEEA---------------GLAGF-------ADRdpatLSGGQRARVALLRALLAEP 152
|
170 180
....*....|....*....|..
gi 503610856 491 PILVLDEATSALDVETEARVKD 512
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFRE 174
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-578 |
2.33e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFA-NS---AQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR----KS 406
Cdd:PRK13643 2 IKFEKVNYTYQpNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 407 LRRSIATVFQ--DAGLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIedrlnGYDTVVGERGN-RLSGGERQRVAIA 483
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 484 RAILKNAPILVLDEATSALDVETEARVKDAIDALRKD-RTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG---------- 551
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGtpsdvfqevd 236
|
250 260 270
....*....|....*....|....*....|
gi 503610856 552 --GFHELSQSNG-RFAALLRASGILTDEDV 578
Cdd:PRK13643 237 flKAHELGVPKAtHFADQLQKTGAVTFEKL 266
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
349-557 |
2.42e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRK-SLRRSIATVFQDAGLMNR-SIG 426
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLGR---EDASLDEVMAAAEAAAASDFIEDRLN---GYDTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEATS 500
Cdd:PRK09700 99 ENLYIGRhltKKVCGVNIIDWREMRVRAAMMLLRVGlkvDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 501 ALDVETEARVKDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELS 557
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVS 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
351-551 |
2.48e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIA-----TVTRKSLRRSiatvFQdaglmnrsi 425
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghQIARMGVVRT----FQ--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 geNIRLGREDASLDEVMAAAEAAAASDFIE-----------------------DRLNGYDTVVGERGNrLSGGERQRVAI 482
Cdd:PRK11300 88 --HVRLFREMTVIENLLVAQHQQLKTGLFSgllktpafrraesealdraatwlERVGLLEHANRQAGN-LAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 483 ARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
336-549 |
6.04e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.44 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 336 EFRDISFDFAnsaqGVR---NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEpkH----GQILIDGV-----DIatvt 403
Cdd:NF040905 3 EMRGITKTFP----GVKaldDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--HgsyeGEILFDGEvcrfkDI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 404 RKSLRRSIATVFQDAGLM-NRSIGENIRLGREDASL-----DEVMAAAEAAAASDFIEDRLngyDTVVGERGNrlsgGER 477
Cdd:NF040905 73 RDSEALGIVIIHQELALIpYLSIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESP---DTLVTDIGV----GKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 478 QRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVE 549
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
333-548 |
6.11e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 333 GEV--EFRDISfdfanSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATVtRKSLR 408
Cdd:COG1129 253 GEVvlEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSP-RDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 409 RSIATVFQD---AGL-MNRSIGENIRLgredASLDEVMAA------AEAAAASDFIED---RLNGYDTVVGErgnrLSGG 475
Cdd:COG1129 327 AGIAYVPEDrkgEGLvLDLSIRENITL----ASLDRLSRGglldrrRERALAEEYIKRlriKTPSPEQPVGN----LSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 476 ERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFI-----------IAHRlstvreadlVIFMDQ 544
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIvisselpellgLSDR---------ILVMRE 469
|
....
gi 503610856 545 GRVV 548
Cdd:COG1129 470 GRIV 473
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
351-497 |
6.20e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.60 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTT----LVNLLQrvhePKHGQILIDGVDIatvTRKSL----RRSI------ATVFQ 416
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDI---THLPMhkraRLGIgylpqeASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 417 daGLmnrSIGENIRLGREDASLDEvmaaaeaaaasDFIEDRLN------GYDTVVGERGNRLSGGERQRVAIARAILKNA 490
Cdd:COG1137 92 --KL---TVEDNILAVLELRKLSK-----------KEREERLEelleefGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
....*..
gi 503610856 491 PILVLDE 497
Cdd:COG1137 156 KFILLDE 162
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
352-554 |
6.58e-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: 71.52 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLqrVHEPK----HGQILIDGVDIATV-TRKSLRRSIATVFQD----AGLMN 422
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTI--AGHPSyevtSGTILFKGQDLLELePDERARAGLFLAFQYpeeiPGVSN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 ----RSIGENIRLGREDASLDevmaaaeaaaASDF---IEDRLNGYDtVVGERGNR-----LSGGERQRVAIARAILKNA 490
Cdd:TIGR01978 95 leflRSALNARRSARGEEPLD----------LLDFeklLKEKLALLD-MDEEFLNRsvnegFSGGEKKRNEILQMALLEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAH--RLSTVREADLVIFMDQGRVVEMGGFH 554
Cdd:TIGR01978 164 KLAILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSGDVE 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
21-286 |
6.72e-14 |
|
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: 72.44 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIANIVLAAItiaePILFGRIIDAISSQKDVAPMLLLWAGF--------GVFNTIAFVLVSREADRLAHGRRASLl 92
Cdd:cd18541 5 ILFLILVDLLQLLI----PRIIGRAIDALTAGTLTASQLLRYALLilllalliGIFRFLWRYLIFGASRRIEYDLRNDL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 93 teaFGRIVSMPLSWHSQRGT-------SNALHTLLRACEtlFGLwlefmrQHLATAVALMLLIPTA-FAMDVRLSLI--- 161
Cdd:cd18541 80 ---FAHLLTLSPSFYQKNRTgdlmaraTNDLNAVRMALG--PGI------LYLVDALFLGVLVLVMmFTISPKLTLIall 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 162 -LVVLGAAYVMISKVVMSRTKEGQAAveghyhtvFSHVSD----SISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVL 236
Cdd:cd18541 149 pLPLLALLVYRLGKKIHKRFRKVQEA--------FSDLSDrvqeSFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 503610856 237 DWWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLI 286
Cdd:cd18541 221 RVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLI 270
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
303-532 |
1.61e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 303 RAKLEDFFQLEDsvQDREEPADAGELKGVVGE------VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTT 376
Cdd:TIGR03719 287 KARLARYEELLS--QEFQKRNETAEIYIPPGPrlgdkvIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 377 LVNLLQRVHEPKHGQILI-DGVDIATV--TRKSLrrsiatvfqDAglmNRSIGENIRLGredasLDEVMAAAEAAAASDF 453
Cdd:TIGR03719 364 LFRMITGQEQPDSGTIEIgETVKLAYVdqSRDAL---------DP---NKTVWEEISGG-----LDIIKLGKREIPSRAY 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 454 IeDRLN--GYDT--VVGErgnrLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKdrTTFIIAH- 528
Cdd:TIGR03719 427 V-GRFNfkGSDQqkKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHd 499
|
....*....
gi 503610856 529 -----RLST 532
Cdd:TIGR03719 500 rwfldRIAT 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
335-557 |
1.97e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFAnsaqGV---RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRS 410
Cdd:PRK15439 12 LCARSISKQYS----GVevlKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQDAGLM-NRSIGENI--RLGREDASLdEVMAAAEAAAASDFIEDRLNGydtvvgergnRLSGGERQRVAIARAIL 487
Cdd:PRK15439 88 IYLVPQEPLLFpNLSVKENIlfGLPKRQASM-QKMKQLLAALGCQLDLDSSAG----------SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 488 KNAPILVLDEATSALD-VETEaRVKDAIDALR-KDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELS 557
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETE-RLFSRIRELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLS 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
352-506 |
2.08e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIdgvdiatvtRKSLRrsIATVFQDAGLM-NRSIGENIR 430
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQEPPLDdDLTVLDTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LG----------REDASLDEVMAAAEAAAASDFIE--DRLNGY--------------------DTVVGErgnrLSGGERQ 478
Cdd:COG0488 84 DGdaelraleaeLEELEAKLAEPDEDLERLAELQEefEALGGWeaearaeeilsglgfpeedlDRPVSE----LSGGWRR 159
|
170 180
....*....|....*....|....*...
gi 503610856 479 RVAIARAILKNAPILVLDEATSALDVET 506
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
29-286 |
2.42e-13 |
|
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: 70.67 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 29 IVLAAITIAEPILFGRIIDAISSQKDVAP-------MLLLWAGFGVFNTIAFVLVSREADRLAhgrrASLLTEAFGRIVS 101
Cdd:cd18557 6 LISSAAQLLLPYLIGRLIDTIIKGGDLDVlnelaliLLAIYLLQSVFTFVRYYLFNIAGERIV----ARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 102 MPLSWHSQRGTSNALHTLLRACETL---FGLWLEFMRQHLATAVALMLLIptaFAMDVRLSLILVVLGAAYVMISKVVMS 178
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLqsaVTDNLSQLLRNILQVIGGLIIL---FILSWKLTLVLLLVIPLLLIASKIYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 179 RTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMMAIL 258
Cdd:cd18557 159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVL 238
|
250 260
....*....|....*....|....*...
gi 503610856 259 VIGTVLVQRGELGVGEVIAFIGFANLLI 286
Cdd:cd18557 239 WYGGYLVLSGQLTVGELTSFILYTIMVA 266
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
335-569 |
2.68e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFansaQGVRNVSFKAKAGQTIAIVGPTGAGKTT-------LVNLLQRVHEPKhgqILIDGVDIATVTRKSL 407
Cdd:PRK11022 11 VHFGDESAPF----RAVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRVMAEK---LEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RR----SIATVFQDAglMNR-----SIGENI-----------RLGREDASLDEVMAAAEAAAASdfiedRLNGYDtvvge 467
Cdd:PRK11022 84 RNlvgaEVAMIFQDP--MTSlnpcyTVGFQImeaikvhqggnKKTRRQRAIDLLNQVGIPDPAS-----RLDVYP----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 468 rgNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDAL--RKDRTTFIIAHRLSTVRE-ADLVIFMDQ 544
Cdd:PRK11022 152 --HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEaAHKIIVMYA 229
|
250 260
....*....|....*....|....*..
gi 503610856 545 GRVVEMGGFHELSQS--NGRFAALLRA 569
Cdd:PRK11022 230 GQVVETGKAHDIFRAprHPYTQALLRA 256
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
346-569 |
2.69e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 346 NSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRV-----HEPKHGQILIDGVDIATVTRKSLRRSIAT---VFQD 417
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGSHIELLGRTVQREGRLARDIRKSRANtgyIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 AGLMNR-SIGENIRLGredASLDEVMAAAEAAAASDFIEDRLNGYDTVVG------ERGNRLSGGERQRVAIARAILKNA 490
Cdd:PRK09984 95 FNLVNRlSVLENVLIG---ALGSTPFWRTCFSWFTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 491 PILVLDEATSALDVETEARVKDAI-DALRKDRTTFIIA-HRLS-TVREADLVIFMDQGRVVEMGGFHELsqSNGRFAALL 567
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLrDINQNDGITVVVTlHQVDyALRYCERIVALRQGHVFYDGSSQQF--DNERFDHLY 249
|
..
gi 503610856 568 RA 569
Cdd:PRK09984 250 RS 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
335-534 |
2.72e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.55 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFaNSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRV--HEPKHGQILIDGVDI-ATVTRKSLRRSI 411
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGLM-NRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNA 490
Cdd:TIGR02633 81 VIIHQELTLVpELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503610856 491 PILVLDEATSAL-DVETEARVKDAIDALRKDRTTFIIAHRLSTVR 534
Cdd:TIGR02633 161 RLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-526 |
3.21e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.09 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQI-LIDGVDIATVTRkslrrsiat 413
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 vfqdaglmnrsigenirlgredasldevmaaaeaaaasdfiedrlngydtvvgergnrLSGGERQRVAIARAILKNAPIL 493
Cdd:cd03221 71 ----------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....
gi 503610856 494 VLDEATSALDVETearvKDA-IDALRKDRTTFII 526
Cdd:cd03221 93 LLDEPTNHLDLES----IEAlEEALKEYPGTVIL 122
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
310-552 |
3.39e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 310 FQLEDSVQDREEPADAGELKgvvgEVEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKH 389
Cdd:PRK10522 302 LALAPYKAEFPRPQAFPDWQ----TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 390 GQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGenirlGREDASLDEVMAaaeaaaasDFIEdRLNGYDTVVGERG 469
Cdd:PRK10522 378 GEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLG-----PEGKPANPALVE--------KWLE-RLKMAHKLELEDG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 470 N----RLSGGERQRVAIARAILKNAPILVLDEAtsALDVETEAR---VKDAIDALR-KDRTTFIIAHRLSTVREADLVIF 541
Cdd:PRK10522 444 RisnlKLSKGQKKRLALLLALAEERDILLLDEW--AADQDPHFRrefYQVLLPLLQeMGKTIFAISHDDHYFIHADRLLE 521
|
250
....*....|.
gi 503610856 542 MDQGRVVEMGG 552
Cdd:PRK10522 522 MRNGQLSELTG 532
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
335-560 |
3.78e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFdfansAQGVR----NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSL--- 407
Cdd:PRK11831 8 VDMRGVSF-----TRGNRcifdNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 408 RRSIATVFQDAGLM-NRSIGENIRLG-REDASLDEVMAAAEAAAASDfiedrlngydtVVGERG------NRLSGGERQR 479
Cdd:PRK11831 83 RKRMSMLFQSGALFtDMNVFDNVAYPlREHTQLPAPLLHSTVMMKLE-----------AVGLRGaaklmpSELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 480 VAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDR--TTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
....
gi 503610856 557 sQSN 560
Cdd:PRK11831 232 -QAN 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-518 |
4.26e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRSIATVFQDAGLMNR-SIGEN 428
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLG---REDASLDEVMAAAEAAAASDFIEDRLNGYdtvvgerGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVE 505
Cdd:PRK10895 99 LMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170
....*....|...
gi 503610856 506 TEARVKDAIDALR 518
Cdd:PRK10895 172 SVIDIKRIIEHLR 184
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-528 |
4.29e-13 |
|
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: 72.12 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 357 KAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDgVDIA------------TVtRKSLRRSIATVFQDAGLMNRs 424
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISykpqyispdydgTV-EEFLRSANTDDFGSSYYKTE- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLgredasldevmaaaeaaaasdfieDRLngYDTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEATSALDV 504
Cdd:COG1245 439 IIKPLGL------------------------EKL--LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180
....*....|....*....|....*.
gi 503610856 505 ETEARVKDAID--ALRKDRTTFIIAH 528
Cdd:COG1245 489 EQRLAVAKAIRrfAENRGKTAMVVDH 514
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
25-303 |
5.50e-13 |
|
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: 69.82 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAISSQKDVAPM----------LLLWAGFGVFNTIAFVLVSreaDRLAhgrrASLLTE 94
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLnqiallllglFLLQAVFSFFRIYLFARVG---ERVV----ADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 95 AFGRIVSMPLSWHSQRGT-------SNALhTLLRacETLFGLWLEFMRQHLATAVALMLLiptaFAMDVRLSLILVVLGA 167
Cdd:cd18576 75 LYRHLQRLPLSFFHERRVgeltsrlSNDV-TQIQ--DTLTTTLAEFLRQILTLIGGVVLL----FFISWKLTLLMLATVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 168 AYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRieaETRELKKFTQRLLSAQYPVLD---WWALASG 244
Cdd:cd18576 148 VVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTR---EDYEIERYRKALERVVKLALKrarIRALFSS 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 245 LNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEAR 303
Cdd:cd18576 225 FIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
347-547 |
6.57e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 347 SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRSIATVFQDA---GL-M 421
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdGLvL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 422 NRSIGENIRL----------GREDASlDEVMAAaeaaaaSDFIED---RLNGYDTVVGErgnrLSGGERQRVAIARAILK 488
Cdd:PRK10762 344 GMSVKENMSLtalryfsragGSLKHA-DEQQAV------SDFIRLfniKTPSMEQAIGL----LSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 489 NAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHrlSTVRE----ADLVIFMDQGRV 547
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVS--SEMPEvlgmSDRILVMHEGRI 473
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
339-551 |
7.62e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 339 DISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRR--------- 409
Cdd:PRK15056 11 DVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAyvpqseevd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 410 -SIATVFQDAGLMNR--SIGENIRLGRED-ASLDEVMAAAeaaaasDFIEDRlngyDTVVGErgnrLSGGERQRVAIARA 485
Cdd:PRK15056 91 wSFPVLVEDVVMMGRygHMGWLRRAKKRDrQIVTAALARV------DMVEFR----HRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 486 ILKNAPILVLDEATSALDVETEARVKDAIDALRKD-RTTFIIAHRLSTVREADLVIFMDQGRVVEMG 551
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
351-566 |
7.86e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.01 E-value: 7.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKH-GQILIDGVDIATVT-RKSLRRSIATVFQDA---GLMNR-S 424
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhGIVPIlG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 425 IGENIRLGREDA-----SLDEVMAAAEAAAASDFIEDRLNGYDTVVGergnRLSGGERQRVAIARAILKNAPILVLDEAT 499
Cdd:TIGR02633 356 VGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 500 SALDVETEARVKDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGRVveMGGF--HELSQSNGRFAAL 566
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIvVSSELAEVLGlSDRVLVIGEGKL--KGDFvnHALTQEQVLAAAL 500
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-543 |
1.05e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 350 GVR---NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDiatVTRKSLRRS----IATVFQDAGLM- 421
Cdd:PRK10762 16 GVKalsGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE---VTFNGPKSSqeagIGIIHQELNLIp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 422 NRSIGENIRLGREDASLDEVMAAAEAAAASDFIEDRLN---GYDTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEA 498
Cdd:PRK10762 93 QLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNlrfSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503610856 499 TSAL-DVETEARVKdAIDALR-KDRTTFIIAHRLSTVREA--DLVIFMD 543
Cdd:PRK10762 169 TDALtDTETESLFR-VIRELKsQGRGIVYISHRLKEIFEIcdDVTVFRD 216
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
25-286 |
1.80e-12 |
|
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: 68.23 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAISSQKD---VAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFGRIVS 101
Cdd:cd18542 5 ILALLLATALNLLIPLLIRRIIDSVIGGGLrelLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 102 MPLSWHS--------QRGTS------NALHT-LLRACETLFglwlefmrqHLATAVALMlliptaFAMDVRLSLIL---- 162
Cdd:cd18542 85 LSFSFHDkartgdlmSRCTSdvdtirRFLAFgLVELVRAVL---------LFIGALIIM------FSINWKLTLISlaii 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 163 -VVLGAAYVMISKV----VMSRTKEGqaaveghyhTVFSHVSDSISNVSVVHSYNRieaETRELKKFT---QRLLSAQYP 234
Cdd:cd18542 150 pFIALFSYVFFKKVrpafEEIREQEG---------ELNTVLQENLTGVRVVKAFAR---EDYEIEKFDkenEEYRDLNIK 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 503610856 235 VLDWWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLI 286
Cdd:cd18542 218 LAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLI 269
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
321-566 |
3.52e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 321 EPADAGElkgVVGEVefRDIS-FDFANSA-QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKH-GQILIDG- 396
Cdd:PRK13549 251 EPHTIGE---VILEV--RNLTaWDPVNPHiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGk 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 397 -VDIATvTRKSLRRSIATVFQD------AGLMnrSIGENIRLgredASLDE-----VMAAAEAAAASDFIEDRLNGYDTV 464
Cdd:PRK13549 326 pVKIRN-PQQAIAQGIAMVPEDrkrdgiVPVM--GVGKNITL----AALDRftggsRIDDAAELKTILESIQRLKVKTAS 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 465 VGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFM 542
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIvISSELPEVLGlSDRVLVM 478
|
250 260
....*....|....*....|....*.
gi 503610856 543 DQGRVveMGGF--HELSQSNGRFAAL 566
Cdd:PRK13549 479 HEGKL--KGDLinHNLTQEQVMEAAL 502
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-559 |
3.68e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSlRRSIATVFQDAGL-MNRSIGENI 429
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQFDNLdPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 430 RLGREDASLDEVMAAAEAAAASDFIedRL-NGYDTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEATSALDVETEA 508
Cdd:PRK13537 102 LVFGRYFGLSAAAARALVPPLLEFA--KLeNKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503610856 509 RVKDAIDAL-RKDRTTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHELSQS 559
Cdd:PRK13537 176 LMWERLRSLlARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
301-547 |
3.95e-12 |
|
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: 69.66 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 301 EARAkLEDFFQLEDSVQDREEPADAG------ELKGVVGEVEFRDISFDFANSAQ-GVRNVSFKAKAGQTIAIVGPTGAG 373
Cdd:TIGR01257 890 EERA-LEKTEPLTEEMEDPEHPEGINdsfferELPGLVPGVCVKNLVKIFEPSGRpAVDRLNITFYENQITAFLGHNGAG 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 374 KTTLVNLLQRVHEPKHGQILIDGVDIATvTRKSLRRSIATVFQDAGLMNR-SIGENIRL-----GR--EDASLD-EVMaa 444
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGRswEEAQLEmEAM-- 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 445 aeaaaasdfIEDrlNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTF 524
Cdd:TIGR01257 1046 ---------LED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTII 1114
|
250 260
....*....|....*....|....*..
gi 503610856 525 IIAHRLStvrEADL----VIFMDQGRV 547
Cdd:TIGR01257 1115 MSTHHMD---EADLlgdrIAIISQGRL 1138
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-530 |
4.66e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 359 KAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQiLIDGVDIATVtrksLRRSIATVFQD--AGLMNRSI----------- 425
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDEV----LKRFRGTELQNyfKKLYNGEIkvvhkpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 ---------GENIRLGREDASLDEVMaaaeaaaasdfieDRLNgYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLD 496
Cdd:PRK13409 172 ipkvfkgkvRELLKKVDERGKLDEVV-------------ERLG-LENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....
gi 503610856 497 EATSALDVETEARVKDAIDALRKDRTTFIIAHRL 530
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
352-549 |
4.77e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDgVDIATVTRkslrrsiatvfqdaglmNRSIGENIrl 431
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFGR-----------------EASLIDAI-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 432 GREDASLDEVmaaaeaaaasdfieDRLN--GYDTVVG--ERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETE 507
Cdd:COG2401 107 GRKGDFKDAV--------------ELLNavGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503610856 508 ARVKDAI-DALRKDRTTFIIAHRLSTVREA---DLVIFMDQGRVVE 549
Cdd:COG2401 173 KRVARNLqKLARRAGITLVVATHHYDVIDDlqpDLLIFVGYGGVPE 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-533 |
1.31e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILID-GVDIATVTRKslrrsiat 413
Cdd:PRK09544 5 VSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYVPQK-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLmNRSIGENIRLgREDASLDEVMAAAEAAAASDFIEDRLNgydtvvgergnRLSGGERQRVAIARAILKNAPIL 493
Cdd:PRK09544 76 LYLDTTL-PLTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503610856 494 VLDEATSALDVETEARVKDAIDALRK--DRTTFIIAHRLSTV 533
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
168-543 |
1.90e-11 |
|
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: 66.70 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 168 AYVMISKVVMSR--------TKEgQAAVEGHYHTVFSHVsdsISNVSVVHSYNRIEAETRELKKFTQRLLS--------- 230
Cdd:TIGR00954 247 AYLFATGVVLTKlrppigklTVE-EQALEGEYRYVHSRL---IMNSEEIAFYQGNKVEKETVMSSFYRLVEhlnliikfr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 231 AQYPVLD-----WWALASGLNRIASTISMMAILVIGTVlvQRGELGVgeviAFIGFANLL------IGRLDQMKAFATQI 299
Cdd:TIGR00954 323 FSYGFLDnivakYTWSAVGLVAVSIPIFDKTHPAFLEM--SEEELMQ----EFYNNGRLLlkaadaLGRLMLAGRDMTRL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 300 FEARAKLEDFFQLEDSVQ--DREEPAD-----------AGELKGVVGEVEFRD--ISFD-----FANSAQGVRNVSFKAK 359
Cdd:TIGR00954 397 AGFTARVDTLLQVLDDVKsgNFKRPRVeeiesgreggrNSNLVPGRGIVEYQDngIKFEniplvTPNGDVLIESLSFEVP 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 360 AGQTIAIVGPTGAGKTTLVNLLQ--------RVHEPKHGQILIdgvdIAT---VTRKSLRRSIatVFQDaglmnrSIGEN 428
Cdd:TIGR00954 477 SGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----VPQrpyMTLGTLRDQI--IYPD------SSEDM 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLGREDASLDEVMAAAEAaaasDFIEDRLNGYDtVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEA 508
Cdd:TIGR00954 545 KRRGLSDKDLEQILDNVQL----THILEREGGWS-AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
410 420 430
....*....|....*....|....*....|....*.
gi 503610856 509 RVkdaIDALRKDRTTFI-IAHRLSTVREADLVIFMD 543
Cdd:TIGR00954 620 YM---YRLCREFGITLFsVSHRKSLWKYHEYLLYMD 652
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
23-304 |
2.11e-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: 65.12 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 23 AIVIANIVLAAITIAEPILFGRIIDAISSQKD---------VAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLT 93
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAIDLIIEGLGggggvdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 94 EAFGRIVSMPLSWHSQRGT--------------SNALH----TLLRACETLFGlwlefmrqhlatAVALMLLIptafamD 155
Cdd:cd18547 83 DLFEKLQRLPLSYFDTHSHgdimsrvtndvdniSQALSqsltQLISSILTIVG------------TLIMMLYI------S 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 156 VRLSLILVVLGAAYVMISKVVMSRT----KEGQAAVeGHyhtVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSA 231
Cdd:cd18547 145 PLLTLIVLVTVPLSLLVTKFIAKRSqkyfRKQQKAL-GE---LNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 232 qypvlDWWA-LASGL----NRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARA 304
Cdd:cd18547 221 -----SFKAqFYSGLlmpiMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALA 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
21-285 |
3.10e-11 |
|
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: 64.33 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIAnIVLAAITIAEPILFGRIIDA--ISSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAH-GRRA--SLLTEA 95
Cdd:cd18544 2 ILALLLL-LLATALELLGPLLIKRAIDDyiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKlGQRIiyDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 96 FGRIVSMPLSWHSQ--------RGTSNalhtllraCETLFGLWLEFMRQhLATAVALMLLIPTA-FAMDVRLSLIL---- 162
Cdd:cd18544 81 FSHIQRLPLSFFDRtpvgrlvtRVTND--------TEALNELFTSGLVT-LIGDLLLLIGILIAmFLLNWRLALISllvl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 163 -VVLGAAYV--MISKVVMSRTKEGQAAVEghyhtvfSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWW 239
Cdd:cd18544 152 pLLLLATYLfrKKSRKAYREVREKLSRLN-------AFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 503610856 240 ALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLL 285
Cdd:cd18544 225 ALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRF 270
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
366-551 |
3.35e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 366 IVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATVTRKSLRRSIATVFQDAG--LMNRSIGENIRLGREDASLDEv 441
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPEqqIFYTDIDSDIAFSLRNLGVPE- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 442 maaaeaaaasDFIEDRLNGYDTVVGERGNR------LSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAID 515
Cdd:PRK13638 111 ----------AEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIR 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 503610856 516 AL-RKDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK13638 181 RIvAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
349-548 |
3.86e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIAT-VTRKSLRRSIATVFQDAGLMNR-SIG 426
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVPEGRRVFSRmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 427 ENIRLGREDASLDEVMAAAEAAAA--SDFIEDRLngydtvvgERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDV 504
Cdd:PRK11614 99 ENLAMGGFFAERDQFQERIKWVYElfPRLHERRI--------QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503610856 505 ETEARVKDAIDALRKD-RTTFIIAHRLS-TVREADLVIFMDQGRVV 548
Cdd:PRK11614 171 IIIQQIFDTIEQLREQgMTIFLVEQNANqALKLADRGYVLENGHVV 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
352-551 |
3.99e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKslRRSIATVFQDAGLM-NRSIGENIR 430
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYpHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGREDASLDEVMAAAEAAAASDFIEdrlngYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARV 510
Cdd:PRK11000 98 FGLKLAGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503610856 511 KDAIDALRK--DRTTFIIAH-RLSTVREADLVIFMDQGRVVEMG 551
Cdd:PRK11000 173 RIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
354-526 |
7.01e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 354 VSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT---RKSLR-RSIATVFQD-------AGLMN 422
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRaKHVGFVFQSfmliptlNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSI-----GENIRLGREDA-SLDEVMAaaeaaaasdfIEDRLNGYDTvvgergnRLSGGERQRVAIARAILKNAPILVLD 496
Cdd:PRK10584 109 VELpallrGESSRQSRNGAkALLEQLG----------LGKRLDHLPA-------QLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190
....*....|....*....|....*....|
gi 503610856 497 EATSALDVETEARVKDAIDALRKDRTTFII 526
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLI 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
347-547 |
9.55e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 9.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 347 SAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDI-ATVTRKSLR---------RSIATVFQ 416
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLArglvylpedRQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 417 DA-------GLMNRSIGENIRLGREDASLDEVMAAaeaaaasdfIEDRLNGYDTVVGergnRLSGGERQRVAIARAILKN 489
Cdd:PRK15439 355 DAplawnvcALTHNRRGFWIKPARENAVLERYRRA---------LNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 490 APILVLDEATSALDVETEARVKDAIDALRKDRTTFI-IAHRLSTVRE-ADLVIFMDQGRV 547
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
33-299 |
1.04e-10 |
|
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: 62.93 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 33 AITIAEPILFGRIIDAISSQKDVAPM--LLLW---------AGFGVFNTIAFVLVSREADRlahgrraSLLTEAFGRIVS 101
Cdd:cd18583 10 VLNVLVPRQLGIIVDSLSGGSGKSPWkeIGLYvllrflqsgGGLGLLRSWLWIPVEQYSYR-------ALSTAAFNHVMN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 102 MPLSWHSQRGTSNALHTLLRA------CETLFglwLEFMRQHLATAVALMLLiptAFAMDVRLSLILVVLGAAYVMIS-K 174
Cdd:cd18583 83 LSMDFHDSKKSGEVLKAIEQGssindlLEQIL---FQIVPMIIDLVIAIVYL---YYLFDPYMGLIVAVVMVLYVWSTiK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 175 VVMSRTKEGQAAVEGhYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISM 254
Cdd:cd18583 157 LTSWRTKLRRDMIDA-DREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLILTLGL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 503610856 255 MAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQI 299
Cdd:cd18583 236 LAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSI 280
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
21-307 |
1.58e-10 |
|
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: 62.11 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIAnIVLAAITIAEPILFGRIID---AISSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFG 97
Cdd:cd18543 2 ILALLAA-LLATLAGLAIPLLTRRAIDgpiAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 98 RIVSMPLSWHSQ--------RGTSNalhtlLRACETLFGlWLEFMRQHLAT---AVALMLLIPTAFAMDVRLSLILVVLg 166
Cdd:cd18543 81 HLQRLDGAFHDRwqsgqllsRATSD-----LSLVQRFLA-FGPFLLGNLLTlvvGLVVMLVLSPPLALVALASLPPLVL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 167 AAYVMISKV-VMSRTKEGQAAveghyhTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLD----WWAL 241
Cdd:cd18543 154 VARRFRRRYfPASRRAQDQAG------DLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARlrarFWPL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 242 ASGLnriaSTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18543 228 LEAL----PELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAE 289
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
319-518 |
1.63e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 319 REEPADAGElkgVVGEVEfrDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVD 398
Cdd:COG3845 247 EKAPAEPGE---VVLEVE--NLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGED 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 399 IATVTRKSLRRS-IATVFQD---AGL-MNRSIGENIRLGREDAS-------LDevmAAAEAAAASDFIED---RLNGYDT 463
Cdd:COG3845 322 ITGLSPRERRRLgVAYIPEDrlgRGLvPDMSVAENLILGRYRRPpfsrggfLD---RKAIRAFAEELIEEfdvRTPGPDT 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 464 VVGergnRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALR 518
Cdd:COG3845 399 PAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR 449
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
353-516 |
2.32e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILI-DGVDIATV--TRKSLRRSiATVFQD--AGLmnrsigE 427
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVdqSRDALDPN-KTVWEEisGGL------D 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 NIRLG-REDASLDEVmaaaeaaaasdfieDRLN--GYDT--VVGErgnrLSGGERQRVAIARAILKNAPILVLDEATSAL 502
Cdd:PRK11819 415 IIKVGnREIPSRAYV--------------GRFNfkGGDQqkKVGV----LSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
170
....*....|....
gi 503610856 503 DVETEARVKDAIDA 516
Cdd:PRK11819 477 DVETLRALEEALLE 490
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
25-277 |
2.82e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 61.72 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAISS-----------QKDVAP----MLLLWAGFGVFNTIAFVLVSREADRLAHgrra 89
Cdd:cd18577 5 LLAAIAAGAALPLMTIVFGDLFDAFTDfgsgesspdefLDDVNKyalyFVYLGIGSFVLSYIQTACWTITGERQAR---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 90 SLLTEAFGRIVSMPLSWHSQRGTSNALHTLLRACETL-------FGLWLefmrQHLATAVALMLLiptAFAMDVRLSLIL 162
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIqdgigekLGLLI----QSLSTFIAGFII---AFIYSWKLTLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 163 ----VVLGAAYVMISKVVMSRTKEGQAAveghYHTVFSHVSDSISNVSVVHSYNrieAETRELKKFTQRLLSAQYPVLdW 238
Cdd:cd18577 154 latlPLIAIVGGIMGKLLSKYTKKEQEA----YAKAGSIAEEALSSIRTVKAFG---GEEKEIKRYSKALEKARKAGI-K 225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 503610856 239 WALASGLNRIASTISMMAILVI----GTVLVQRGELGVGEVIA 277
Cdd:cd18577 226 KGLVSGLGLGLLFFIIFAMYALafwyGSRLVRDGEISPGDVLT 268
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-556 |
2.87e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQgVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRkSLRRSIATV 414
Cdd:PRK13536 42 IDLAGVSKSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-LARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 415 FQDAGL-MNRSIGENI-----RLGREDASLDEVMAAAEaaaasDFIedRL-NGYDTVVGErgnrLSGGERQRVAIARAIL 487
Cdd:PRK13536 120 PQFDNLdLEFTVRENLlvfgrYFGMSTREIEAVIPSLL-----EFA--RLeSKADARVSD----LSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 488 KNAPILVLDEATSALDVETEARVKDAIDA-LRKDRTTFIIAHRLSTV-READLVIFMDQGRVVEMGGFHEL 556
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-532 |
3.30e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 359 KAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQIlIDGVDIATVtrksLRRSIATVFQD--AGLMNRSIG--------EN 428
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-DEEPSWDEV----LKRFRGTELQDyfKKLANGEIKvahkpqyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IR----------LGRED--ASLDEVMaaaeaaaasdfieDRLNgYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLD 496
Cdd:COG1245 172 IPkvfkgtvrelLEKVDerGKLDELA-------------EKLG-LENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*..
gi 503610856 497 EATSALDVETEARVKDAI-DALRKDRTTFIIAHRLST 532
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
344-563 |
3.74e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 344 FANSAQGV-----RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGvdiatvtrkslrrSIATVFQDA 418
Cdd:PRK13545 28 FFRSKDGEyhyalNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------------SAALIAISS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 GLMNRSIG-ENIRL-----GREDASLDEVM-AAAEAAAASDFIEDRLNGYdtvvgergnrlSGGERQRVAIARAILKNAP 491
Cdd:PRK13545 95 GLNGQLTGiENIELkglmmGLTKEKIKEIIpEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 492 ILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMGGFHELSQSNGRF 563
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
18-304 |
3.83e-10 |
|
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: 61.31 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 18 KFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAP----------MLLLWAGFGVFNTIAFVLVSREADRlahgr 87
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLlniisiglilLYLFQSLLSYIRSYLLLKLSQKLDI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 88 raSLLTEAFGRIVSMPLSWHSQRGT---------SNALHTLLraCETLFGLWLEFmrqhLATAVALMLLiptaFAMDVRL 158
Cdd:cd18570 76 --RLILGYFKHLLKLPLSFFETRKTgeiisrfndANKIREAI--SSTTISLFLDL----LMVIISGIIL----FFYNWKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 159 SLILVVLGAAYVMIS-------KVVMSRTKEGQAAVEghyhtvfSHVSDSISNVSVVHSYNrieAETRELKKFTQRL--- 228
Cdd:cd18570 144 FLITLLIIPLYILIIllfnkpfKKKNREVMESNAELN-------SYLIESLKGIETIKSLN---AEEQFLKKIEKKFskl 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 229 --LSAQYPVLDwwALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARA 304
Cdd:cd18570 214 lkKSFKLGKLS--NLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKV 289
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-291 |
5.67e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 60.63 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAH--GRR--ASLLTEAFGRIV 100
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHvaEQKvvADLRSDLYDKLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 101 SMPLSWHSQRGT----------SNALHTLL-RACETLFglwlefmrqhlaTAVaLMLLIPTA--FAMDVRLSLI----LV 163
Cdd:cd18778 85 RLSLRYFDDRQTgdlmsrvindVANVERLIaDGIPQGI------------TNV-LTLVGVAIilFSINPKLALLtlipIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 164 VLGAAYVMISKVVMSRTKEGQAAVeGHYHTVfshVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALAS 243
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREAL-GELNAL---LQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFH 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 503610856 244 GLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLL---IGRLDQ 291
Cdd:cd18778 228 PLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFyepITSLHG 278
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-551 |
5.71e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 354 VSFKAKAGQTIAIVGPTGAGKTTLV----NLLqrvhePKHGQILIDGVDIATVTRKSLRRSIA------------TVFQd 417
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLarmaGLL-----PGSGSIQFAGQPLEAWSAAELARHRAylsqqqtppfamPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 agLMNRSIGENIRLGREDASLDEVMAAAEaaaasdfIEDRLngydtvvGERGNRLSGGERQRVAIARAILK-------NA 490
Cdd:PRK03695 89 --YLTLHQPDKTRTEAVASALNEVAEALG-------LDDKL-------GRSVNQLSGGEWQRVRLAAVVLQvwpdinpAG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 491 PILVLDEATSALDVETEARVKDAIDAL-RKDRTTFIIAHRLS-TVREADLVIFMDQGRVVEMG 551
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASG 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
351-548 |
6.27e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.20 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPK---HGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSIGE 427
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 428 NIrlgreDASLdevmaaaeaaaasdfiedRLNGYDTVvgeRGnrLSGGERQRVAIARAILKNAPILVLDEATSALDVETE 507
Cdd:cd03233 103 TL-----DFAL------------------RCKGNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503610856 508 ----ARVKDAIDALRKdrTTFIIAHRLS--TVREADLVIFMDQGRVV 548
Cdd:cd03233 155 leilKCIRTMADVLKT--TTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
358-555 |
8.76e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 358 AKAGQTIAIVGPTGAGKTTLVNLLQ-RVHEPKH-GQILIDGVDIatvTRKSLRRsIATVFQDAGL--------------- 420
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAgRIQGNNFtGTILANNRKP---TKQILKR-TGFVTQDDILyphltvretlvfcsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 421 --MNRSIGENIRLGREDASLDEVMAAAEAaaasdfiedrlngyDTVVGERGNR-LSGGERQRVAIARAILKNAPILVLDE 497
Cdd:PLN03211 167 lrLPKSLTKQEKILVAESVISELGLTKCE--------------NTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 498 ATSALDVETEARVKDAIDAL-RKDRTTFIIAHRLST--VREADLVIFMDQGRVVEMGGFHE 555
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLaQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-292 |
9.10e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 60.22 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIANIVLAAITIAEPILFGRIID--AISSQKDVAPMLLLWAGFGvfntIAFVLVSREADRLAHGRRASLL------ 92
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdvLIQLGPGGNTSLLLLLVLG----LAGAYVLSALLGILRGRLLARLgerita 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 93 ---TEAFGRIVSMPLSWHSQRGT----------SNALHTLLracetLFGLwlefmrQHLATAVALMLLIPTA-FAMDVRL 158
Cdd:cd18563 77 dlrRDLYEHLQRLSLSFFDKRQTgslmsrvtsdTDRLQDFL-----SDGL------PDFLTNILMIIGIGVVlFSLNWKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 159 SLILVVLGAAYVMISKVVMSRTKegqaaveGHYHTVF-------SHVSDSISNVSVVHSYNRieaETRELKKFT---QRL 228
Cdd:cd18563 146 ALLVLIPVPLVVWGSYFFWKKIR-------RLFHRQWrrwsrlnSVLNDTLPGIRVVKAFGQ---EKREIKRFDeanQEL 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 229 LSAQYPVLDWWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQM 292
Cdd:cd18563 216 LDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWL 279
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-543 |
1.77e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 361 GQTIAIVGPTGAGKTTLVNLL-QRVHEPKHGQILIDGVDIATVTRKSLRrsiatvfqdaglmnrsigenirlgredasld 439
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 440 evmaaaeaaaasdfiedrlngyDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAID---- 515
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190
....*....|....*....|....*....|.
gi 503610856 516 ---ALRKDRTTFIIAHRLSTVREADLVIFMD 543
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
24-307 |
2.26e-09 |
|
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: 58.76 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 24 IVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGF-------GVFNTIAFVLVSREADRLAhgrrASLLTEAF 96
Cdd:cd18782 7 VLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMlvaalleAVLTALRTYLFTDTANRID----LELGGTII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 97 GRIVSMPLSWHSQR---GTSNALHTLLRACETLFGlwlefmrQHLATAVALMLLIPTAFAM---DVRLSLI-LVVL---G 166
Cdd:cd18782 83 DHLLRLPLGFFDKRpvgELSTRISELDTIRGFLTG-------TALTTLLDVLFSVIYIAVLfsySPLLTLVvLATVplqL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 167 AAYVMISKVV---MSRTKEGQAAVEghyhtvfSHVSDSISNVSVVHSYNrieAETRELKKFTQRL---LSAQYPVLDWWA 240
Cdd:cd18782 156 LLTFLFGPILrrqIRRRAEASAKTQ-------SYLVESLTGIQTVKAQN---AELKARWRWQNRYarsLGEGFKLTVLGT 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 241 LASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18782 226 TSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLE 292
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
352-516 |
3.71e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVtRKSLRRSIATVFQDAGLMNR-SIGENIR 430
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYLGHQPGIKTElTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 -LGREDASLDEvmaaaeaaaasDFIEDRLNGydtvVGERG------NRLSGGERQRVAIARAILKNAPILVLDEATSALD 503
Cdd:PRK13538 97 fYQRLHGPGDD-----------EALWEALAQ----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170
....*....|...
gi 503610856 504 VETEARVKDAIDA 516
Cdd:PRK13538 162 KQGVARLEALLAQ 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
353-519 |
3.73e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIA-TVTRKSLRRSIATVFQDAGLM-NRSIGENIR 430
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 LGR---------EDASLDEVMAaaeaaaasdfIEDRLnGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSA 501
Cdd:PRK10982 96 LGRyptkgmfvdQDKMYRDTKA----------IFDEL-DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170
....*....|....*...
gi 503610856 502 LdveTEARVKDAIDALRK 519
Cdd:PRK10982 165 L---TEKEVNHLFTIIRK 179
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
359-530 |
5.54e-09 |
|
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: 55.66 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 359 KAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSlrrsiatvfqdaglmnrsigenirlgredasl 438
Cdd:cd03222 23 KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI-------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 439 devmaaaeaaaasdfiedrlngydtvvgergnRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDAL- 517
Cdd:cd03222 71 --------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLs 118
|
170
....*....|....
gi 503610856 518 -RKDRTTFIIAHRL 530
Cdd:cd03222 119 eEGKKTALVVEHDL 132
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
23-307 |
5.66e-09 |
|
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: 57.50 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 23 AIVIANIVLAAIT-IAEPILFGRIIDAISSQKDVAPML---LLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFGR 98
Cdd:cd18546 2 ALALLLVVVDTAAsLAGPLLVRYGIDSGVRAGDLGVLLlaaAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 99 IVSMPLSWHsQRGTSNALHTLLRA-CETLfglwLEFMRQHLATA-VALMLLIPTA---FAMDVRLSLILVVLGAAYVMIS 173
Cdd:cd18546 82 LQRLSLDFH-ERETSGRIMTRMTSdIDAL----SELLQTGLVQLvVSLLTLVGIAvvlLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 174 KVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRieaETRELKKF-------------TQRLLSAQYPVLDWwa 240
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRR---ERRNAERFaelsddyrdarlrAQRLVAIYFPGVEL-- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 241 lasglnriASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18546 232 --------LGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALE 290
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
351-553 |
6.16e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLL--QRVHEPKHGQILIDGVDIATVT-RKSLRRSIATVFQDA----GLMNR 423
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPveipGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 424 SIGEN----IRLGREDASLDEVmaaaeaaAASDFIEDR---LNGYDTVVGERGNR-LSGGERQRVAIARAILKNAPILVL 495
Cdd:PRK09580 97 FFLQTalnaVRSYRGQEPLDRF-------DFQDLMEEKialLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 496 DEATSALDVETEARVKDAIDALRKDRTTFIIA---HRLSTVREADLVIFMDQGRVVEMGGF 553
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
335-551 |
7.14e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTL---VNLLQRVHEpkhGQILIDGVDIATVTRKSlrRSI 411
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERITS---GEIWIGGRVVNELEPAD--RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQDAGL---MnrSIGENIRLGREDASL--DEVMAAAEAAAASDFIEDRLngydtvvgERGNR-LSGGERQRVAIARA 485
Cdd:PRK11650 79 AMVFQNYALyphM--SVRENMAYGLKIRGMpkAEIEERVAEAARILELEPLL--------DRKPReLSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 486 ILKNAPILVLDEATSALDVETEARVKDAIDAL-RKDRTTFI-IAH-RLSTVREADLVIFMDQGRVVEMG 551
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLhRRLKTTSLyVTHdQVEAMTLADRVVVMNGGVAEQIG 217
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
20-283 |
8.26e-09 |
|
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: 57.09 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 20 RVGAIVIANIVLAAITIAEPILFGRIIDAISSQKDV---APMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAF 96
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLsglLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 97 GRIVSMPLSWHSQR----------GTSNALHTLLRacETLFGLWLEFMrqHLATAVALMlliptaFAMDVRLSLI-LVVL 165
Cdd:cd18545 81 SHLQKLSFSFFDSRpvgkilsrviNDVNSLSDLLS--NGLINLIPDLL--TLVGIVIIM------FSLNVRLALVtLAVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 166 GAAYVMI------SKVVMSRTKEGQAAVEGHYHtvfshvsDSISNVSVVHSYNRiEAETRE---------LKKFTQ--RL 228
Cdd:cd18545 151 PLLVLVVfllrrrARKAWQRVRKKISNLNAYLH-------ESISGIRVIQSFAR-EDENEEifdelnrenRKANMRavRL 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 229 LSAQYPVLDwwalasglnrIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFAN 283
Cdd:cd18545 223 NALFWPLVE----------LISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVG 267
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
23-281 |
1.02e-08 |
|
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: 56.74 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 23 AIVIANIVLAAITiaePILFGRIIDAISSQKDVAPM--LLLWAGFGVFNTIA----------FVLVSREAdrlahGRRAS 90
Cdd:cd18582 3 LLLVLAKLLNVAV---PFLLKYAVDALSAPASALLAvpLLLLLAYGLARILSslfnelrdalFARVSQRA-----VRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 91 LltEAFGRIVSMPLSWHSQR---GTSNALHTLLRACETLFGlwlefmrqhlataVALMLLIPTAFAM-----------DV 156
Cdd:cd18582 75 L--RVFRHLHSLSLRFHLSRktgALSRAIERGTRGIEFLLR-------------FLLFNILPTILELllvcgilwylyGW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 157 RLSLILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNrieAETRELKKFTQRLLSAQYPVL 236
Cdd:cd18582 140 SYALITLVTVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFN---NEEYEAERYDKALAKYEKAAV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 503610856 237 DWWALASGLNRIASTI---SMMAILVIGTVLVQRGELGVGEVIAFIGF 281
Cdd:cd18582 217 KSQTSLALLNIGQALIislGLTAIMLLAAQGVVAGTLTVGDFVLVNTY 264
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
18-307 |
1.09e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 56.75 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 18 KFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAG-------FGVFNTI-AFVLVSREA--DRlahgr 87
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGililfllYGLFSFLrGYIIIKLQTklDK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 88 raSLLTEAFGRIVSMPLSWHSQRgTSNALhtLLRACEtlfglwLEFMRQHLATAVA-----LMLLIPTAFAM---DVRLS 159
Cdd:cd18555 76 --SLMSDFFEHLLKLPYSFFENR-SSGDL--LFRANS------NVYIRQILSNQVIsliidLLLLVIYLIYMlyySPLLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 160 LILVVLGAAYVMISKVVMSRTKEG---QAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKftqRLLSAQYPVL 236
Cdd:cd18555 145 LIVLLLGLLIVLLLLLTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFK---KQLKAFKKKE 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 237 DWWALasgLNRIASTISMMA---ILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18555 222 RLSNI---LNSISSSIQFIApllILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLE 292
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-559 |
1.15e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRSIATVFQD---AGLM-NRSI 425
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrsTGIYaYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 GENIRLGREDASLDEVMAAAEAAAASD--FIEDRLN----GYDTVVGErgnrLSGGERQRVAIARAILKNAPILVLDEAT 499
Cdd:PRK10982 344 GFNSLISNIRNYKNKVGLLDNSRMKSDtqWVIDSMRvktpGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 500 SALDVETEARVKDAIDAL-RKDRTTFIIAhrlSTVRE----ADLVIFMDQGRVVEMGGFHELSQS 559
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELaKKDKGIIIIS---SEMPEllgiTDRILVMSNGLVAGIVDTKTTTQN 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
331-566 |
1.15e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 331 VVGEVEfrDISFDFANSaQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQIlidgvdiatvtRKSLRRS 410
Cdd:PRK11147 318 IVFEME--NVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------HCGTKLE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQDAGLMN--RSIGENIRLGREdasldEVMAAAEAAAASDFIEDRL---NGYDTVVgergNRLSGGERQRVAIARA 485
Cdd:PRK11147 384 VAYFDQHRAELDpeKTVMDNLAEGKQ-----EVMVNGRPRHVLGYLQDFLfhpKRAMTPV----KALSGGERNRLLLARL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 486 ILKNAPILVLDEATSALDVETEARVKDAIDALRKdrTTFIIAH-RL---STVREAdlVIFMDQGRVVE-MGGFHELSQSN 560
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSHdRQfvdNTVTEC--WIFEGNGKIGRyVGGYHDARQQQ 530
|
....*.
gi 503610856 561 GRFAAL 566
Cdd:PRK11147 531 AQYLAL 536
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
25-316 |
3.12e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 55.54 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAISSQKDVAPM--LLLWAGF--------GVFNTIAFVLVSREADRLAHgrraSLLTE 94
Cdd:cd18578 15 LIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRseANFWALMflvlaivaGIAYFLQGYLFGIAGERLTR----RLRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 95 AFGRIVSMPLSWHSQRG-TSNALHTLL----RACETLFGLWLEFMRQHLATAVALMLLiptAFAMDVRLSL-------IL 162
Cdd:cd18578 91 AFRAILRQDIAWFDDPEnSTGALTSRLstdaSDVRGLVGDRLGLILQAIVTLVAGLII---AFVYGWKLALvglatvpLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 163 VVLGAAYVMISKVVMSRTKEGQAAVEghyhtvfSHVSDSISNVSVVHSYNRieaETRELKKFTQrLLSAQYPVLDWWALA 242
Cdd:cd18578 168 LLAGYLRMRLLSGFEEKNKKAYEESS-------KIASEAVSNIRTVASLTL---EDYFLEKYEE-ALEEPLKKGLRRALI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 243 SGLNrIASTISMM-----AILVIGTVLVQRGELGVGEV-IAFIG--FANLLIGrldQMKAFATQIFEARAKLEDFFQLED 314
Cdd:cd18578 237 SGLG-FGLSQSLTffayaLAFWYGGRLVANGEYTFEQFfIVFMAliFGAQSAG---QAFSFAPDIAKAKAAAARIFRLLD 312
|
..
gi 503610856 315 SV 316
Cdd:cd18578 313 RK 314
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-510 |
3.12e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTR-KSLRRSIATVFQ---DAGLM-NRSI 425
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 GENIRLGR--EDASLDEVMAAAEAAAASDFIEDR---LNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEATS 500
Cdd:PRK09700 359 AQNMAISRslKDGGYKGAMGLFHEVDEQRTAENQrelLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170
....*....|
gi 503610856 501 ALDVETEARV 510
Cdd:PRK09700 439 GIDVGAKAEI 448
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
337-519 |
3.30e-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: 53.79 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 337 FRDISFDFANSAQGVR---NVSFKAKAGQTIAIVGPTGAGKTTLVNLL-QRVHEPK-HGQILIDGVDIatvtRKSLRRSI 411
Cdd:cd03232 6 WKNLNYTVPVKGGKRQllnNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPL----DKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 412 ATVFQ-DAGLMNRSIGENIRLgreDASLdevmaaaeaaaasdfiedrlngydtvvgeRGnrLSGGERQRVAIARAILKNA 490
Cdd:cd03232 82 GYVEQqDVHSPNLTVREALRF---SALL-----------------------------RG--LSVEQRKRLTIGVELAAKP 127
|
170 180
....*....|....*....|....*....
gi 503610856 491 PILVLDEATSALDVETEARVkdaIDALRK 519
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNI---VRFLKK 153
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-307 |
3.43e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 55.21 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 24 IVIANIVLAAITIAEPILFGRIIDAISSQKDVAPML-------------------------LLWAGFGVFNTIAFVLVsr 78
Cdd:cd18564 4 ALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLglapllgpdplallllaaaalvgiaLLRGLASYAGTYLTALV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 79 eADRLAHGRRASLlteaFGRIVSMPLSWHSQRGT------------------SNALHTLLRACETLFGLwlefmrqhlat 140
Cdd:cd18564 82 -GQRVVLDLRRDL----FAHLQRLSLSFHDRRRTgdllsrltgdvgaiqdllVSGVLPLLTNLLTLVGM----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 141 aVALMlliptaFAMDVRLSLILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRE 220
Cdd:cd18564 146 -LGVM------FWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 221 LKKFTQRLLSAQypvLDWWALASGLNRIAS---TISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFAT 297
Cdd:cd18564 219 FARENRKSLRAG---LRAARLQALLSPVVDvlvAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTG 295
|
330
....*....|
gi 503610856 298 QIFEARAKLE 307
Cdd:cd18564 296 RIAKASASAE 305
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
346-552 |
3.61e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 346 NSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLqrVHEPKH----GQILIDGVDI--ATVTRKSlRRSIATVFQD-- 417
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAYkileGDILFKGESIldLEPEERA-HLGIFLAFQYpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 418 --AGLMN----RSIGENIRLGREDASLDEVMAAaeaaaasDFIEDRLN--GYDTVVGERG-NR-LSGGERQRVAIARAIL 487
Cdd:CHL00131 95 eiPGVSNadflRLAYNSKRKFQGLPELDPLEFL-------EIINEKLKlvGMDPSFLSRNvNEgFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 488 KNAPILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAH--RLSTVREADLVIFMDQGRVVEMGG 552
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
356-505 |
6.51e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 356 FKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKslrRSIATVFQDAGL-MNRSIGENIRL--- 431
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLkADLSTLENLHFlcg 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 432 --GREDASLDEVMAAAEAaaasdfiedrLNGY-DTVVgergNRLSGGERQRVAIARAILKNAPILVLDEATSALDVE 505
Cdd:PRK13543 109 lhGRRAKQMPGSALAIVG----------LAGYeDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-519 |
7.36e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 339 DISFDFANSAQgVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDgvdiatvtRKSLRRSIATVFQDA 418
Cdd:PRK13540 6 ELDFDYHDQPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFE--------RQSIKKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 GLMNRSIGENIRLGREDASLDEVMAAAEAAAASDFIedRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDEA 498
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELC--RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180
....*....|....*....|.
gi 503610856 499 TSALDVETEARVKDAIDALRK 519
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRA 175
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-531 |
8.61e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 359 KAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHG-------------------------QILIDGVDiatVTRKSlrrsiat 413
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyftKLLEGDVK---VIVKP------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 vfQDAGLMNRS----IGENIRLGREDASLDEVMaaaeaaaasdfieDRLnGYDTVVGERGNRLSGGERQRVAIARAILKN 489
Cdd:cd03236 94 --QYVDLIPKAvkgkVGELLKKKDERGKLDELV-------------DQL-ELRHVLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503610856 490 APILVLDEATSALDVETEARVKDAIDALRKD-RTTFIIAHRLS 531
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDdNYVLVVEHDLA 200
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
330-561 |
1.52e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 330 GVVGEVEFRDISFDFAnSAQGVRNVSFKAKAGQTIAIVGPTGAGKTtlvnllqRVHEPKHgqilIDGVDIA--------- 400
Cdd:NF000106 9 GARNAVEVRGLVKHFG-EVKAVDGVDLDVREGTVLGVLGP*GAA**-------RGALPAH----V*GPDAGrrpwrf*tw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 401 TVTRKSLRRSIAT-----VFQDAGLMNRS----IGENIRLGREDASldevmaaaeaaAASDFIEDRLNgYDTVVGERGNR 471
Cdd:NF000106 77 CANRRALRRTIG*hrpvr*GRRESFSGREnlymIGR*LDLSRKDAR-----------ARADELLERFS-LTEAAGRAAAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 472 LSGGERQRVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVRE--ADLVIFMDQGRVVE 549
Cdd:NF000106 145 YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVIDRGRVIA 224
|
250
....*....|..
gi 503610856 550 MGGFHELSQSNG 561
Cdd:NF000106 225 DGKVDELKTKVG 236
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
33-289 |
1.58e-07 |
|
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: 53.00 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 33 AITIAEPILFGRIIDAISSQKDVAP----MLLLWAGFGVFN--------TIAFVLVSREADRlahgrraSLLTEAFGRIV 100
Cdd:cd18560 10 ACNVLAPLFLGRAVNALTLAKVKDLesavTLILLYALLRFSskllkelrSLLYRRVQQNAYR-------ELSLKTFAHLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 101 SMPLSWHSQRGTSNALHTLLRACETLFGLwLEFMRQHLATAVALMLLIPTAFAM--DVRLSLILVVLGAAYVMIS-KVVM 177
Cdd:cd18560 83 SLSLDWHLSKKTGEVVRIMDRGTESANTL-LSYLVFYLVPTLLELIVVSVVFAFhfGAWLALIVFLSVLLYGVFTiKVTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 178 SRTKEGQAAVE--GHYHTVfshVSDSISNVSVVHSYNrieAETRELKKFTQRLLsaQYPVLDWWALAS--GLNRIASTI- 252
Cdd:cd18560 162 WRTKFRRAANKkdNEAHDI---AVDSLLNFETVKYFT---NEKYEVDRYGEAVK--EYQKSSVKVQASlsLLNVGQQLIi 233
|
250 260 270
....*....|....*....|....*....|....*....
gi 503610856 253 --SMMAILVIGTVLVQRGELGVGEVIAFigfaNLLIGRL 289
Cdd:cd18560 234 qlGLTLGLLLAGYRVVDGGLSVGDFVAV----NTYIFQL 268
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
351-551 |
1.81e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTL-----VNLLQrVHEPKHGQILIDGVDIATVTRKSLRRSIATVFQDAGLMNRSI 425
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLlktiaSNTDG-FHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 426 GEN----IRLGREDASLDEVMAAAEAAAASDFIEdRLNG----YDTVVGE---RGnrLSGGERQRVAIARAILKNAPILV 494
Cdd:TIGR00956 156 GETldfaARCKTPQNRPDGVSREEYAKHIADVYM-ATYGlshtRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 495 LDEATSALDVETEARVkdaIDALRK-----DRTTFIIAHRLS--TVREADLVIFMDQGRVVEMG 551
Cdd:TIGR00956 233 WDNATRGLDSATALEF---IRALKTsanilDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
353-551 |
2.53e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGvdiatvtrkslrrSIATVFQDAGLMNRSIG-ENIR- 430
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVIAISAGLSGQLTGiENIEf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 431 ----LGREDASLDEVM-AAAEAAAASDFIEDRLNGYdtvvgergnrlSGGERQRVAIARAILKNAPILVLDEATSALDVE 505
Cdd:PRK13546 109 kmlcMGFKRKEIKAMTpKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503610856 506 TEARVKDAIDALR-KDRTTFIIAHRLSTVRE-ADLVIFMDQGRVVEMG 551
Cdd:PRK13546 178 FAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYG 225
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
23-286 |
2.56e-07 |
|
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: 52.40 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 23 AIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPML---LLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFGRI 99
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILrtgLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 100 VSMPLSWHSQRGTS--------------NALHTLLRAcetlfglwleFMRqhlatavALMLLIPT---AFAMDVRLSLIL 162
Cdd:cd18548 83 QSFSFAEIDKFGTSslitrltndvtqvqNFVMMLLRM----------LVR-------APIMLIGAiimAFRINPKLALIL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 163 VV----LGAAYVMISKVVMSRTKEGQAAVEGhyhtVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDW 238
Cdd:cd18548 146 LVaipiLALVVFLIMKKAIPLFKKVQKKLDR----LNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 503610856 239 WALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLI 286
Cdd:cd18548 222 MALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQIL 269
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
25-299 |
3.25e-07 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 52.13 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLL------WAGFGVF------NTIAFVLVSREADRLAhgrrASLL 92
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLslktfaLALLGVFvvgaaaNFGRVYLLRIAGERIV----ARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 93 TEAFGRIVSMPLSWHSQRGTSNALHTL------------------LRAceTLFGlwlefmrqhlATAVALMLLIPTAFAM 154
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGELVSRLssdtsvvgksltqnlsdgLRS--LVSG----------VGGIGMMLYISPKLTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 155 dVRLSLILVVLGAAYVMiSKVVMSRTKEGQAAVEGhyhtvFSHVSD-SISNVSVVHSYNrieAETRELKKFTQRL---LS 230
Cdd:cd18573 146 -VMLLVVPPIAVGAVFY-GRYVRKLSKQVQDALAD-----ATKVAEeRLSNIRTVRAFA---AERKEVERYAKKVdevFD 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503610856 231 AQYPVLDWWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQI 299
Cdd:cd18573 216 LAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSEL 284
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-504 |
3.77e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTL-VNLLQRVHEPKH-GQILIDG--VDIATVtRKSLRRSIATVFQD---AGL-MN 422
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNIsGTVFKDGkeVDVSTV-SDAIDAGLAYVTEDrkgYGLnLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSIGENIRLgredASLDE-----VMAAAEAAAASDFIEDRLNGYDTVVGERGNRLSGGERQRVAIARAILKNAPILVLDE 497
Cdd:NF040905 355 DDIKRNITL----ANLGKvsrrgVIDENEEIKVAEEYRKKMNIKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
....*..
gi 503610856 498 ATSALDV 504
Cdd:NF040905 431 PTRGIDV 437
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
460-551 |
4.77e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 460 GYDTVvGERGNRLSGGERQRVAIARAILKNAP--ILVLDEATSALDVETEARVKDAIDALRKDRTTFI-IAHRLSTVREA 536
Cdd:cd03238 77 GYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVIlIEHNLDVLSSA 155
|
90 100
....*....|....*....|.
gi 503610856 537 DLVIFM------DQGRVVEMG 551
Cdd:cd03238 156 DWIIDFgpgsgkSGGKVVFSG 176
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
353-510 |
6.19e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 353 NVSFKAKAGQTIAIVGPTGAGKTTLVNLL-QRVHEP--KHGQILIDGVDIatvtRKSLRRSIATVFQ-DAGLMNRSIGEN 428
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGviTGGDRLVNGRPL----DSSFQRSIGYVQQqDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 429 IRLG---REDASL---------DEVMaaaeaaaasDFIEdrLNGY-DTVVGERGNRLSGGERQRVAIARAILKNAPILV- 494
Cdd:TIGR00956 857 LRFSaylRQPKSVsksekmeyvEEVI---------KLLE--MESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170
....*....|....*.
gi 503610856 495 LDEATSALDVETEARV 510
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSI 941
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
30-279 |
7.27e-07 |
|
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: 51.00 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 30 VLAAIT-IAEPILFGRIIDAISSQKD-------VAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLlteaFGRIVS 101
Cdd:cd18572 6 VVAALSeLAIPHYTGAVIDAVVADGSreafyraVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDL----FRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 102 MPLSWHSQRGT------------------SNALHTLLRACETLFGLwLEFMrqhlatavalmlliptaFAMDVRLSLILV 163
Cdd:cd18572 82 QDIAFFDATKTgeltsrltsdcqkvsdplSTNLNVFLRNLVQLVGG-LAFM-----------------FSLSWRLTLLAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 164 VLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNrieAETRELKKFTQRLLSAqypvLDWW---A 240
Cdd:cd18572 144 ITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA---TEEREARRYERALDKA----LKLSvrqA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 503610856 241 LASGLNRIASTISMMAILVI----GTVLVQRGELGVGEVIAFI 279
Cdd:cd18572 217 LAYAGYVAVNTLLQNGTQVLvlfyGGHLVLSGRMSAGQLVTFM 259
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
24-307 |
1.39e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 50.25 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 24 IVIANIVLAAITIAEPILFGRIIDAISSQKDV---APMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFGRIV 100
Cdd:cd18568 7 ILLASLLLQLLGLALPLFTQIILDRVLVHKNIsllNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 101 SMPLSWHSQRGTSNALHtllRACETLfgLWLEFMRQHLATAV--ALMLLIPTA--FAMDVRLSLILVVLGAAYVMISKVV 176
Cdd:cd18568 87 SLPLSFFASRKVGDIIT---RFQENQ--KIRRFLTRSALTTIldLLMVFIYLGlmFYYNLQLTLIVLAFIPLYVLLTLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 177 MSRTKEG-----QAAVEGHyhtvfSHVSDSISNVSVVHSYNrIEAETR-ELKKFTQRLLSAQYPVLDWWALASGLNRIAS 250
Cdd:cd18568 162 SPKLKRNsreifQANAEQQ-----SFLVEALTGIATIKALA-AERPIRwRWENKFAKALNTRFRGQKLSIVLQLISSLIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 251 TISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18568 236 HLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVE 292
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
351-558 |
3.63e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 351 VRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQ------------RVhepkHGQILIDGVDIATVTRKSLRRSIATVFQDA 418
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggaprgaRV----TGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 419 G-LMNRSIGENIRLGRedasLDEVMAAAEAAAASDFIEDR---LNGYDTVVGERGNRLSGGERQRVAIARAILKNAP--- 491
Cdd:PRK13547 93 QpAFAFSAREIVLLGR----YPHARRAGALTHRDGEIAWQalaLAGATALVGRDVTTLSGGELARVQFARVLAQLWPphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503610856 492 ------ILVLDEATSALDVETEARVKDAIDALRKDRT--TFIIAHRLS-TVREADLVIFMDQGRVVEMGGFHELSQ 558
Cdd:PRK13547 169 aaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
25-304 |
4.34e-06 |
|
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: 48.72 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAISSQKD----------------------VAPMLLLWAGFGVFNTIAFVLVSREADR 82
Cdd:cd18565 5 LLASILNRLFDLAPPLLIGVAIDAVFNGEAsflplvpaslgpadprgqlwllGGLTVAAFLLESLFQYLSGVLWRRFAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 83 LAHGRRasllTEAFGRIVSMPLSWHSQRGTSNALHTL---LRACETLFGlwlEFMRQHLATAVALMLLIPTAFAMDVRLS 159
Cdd:cd18565 85 VQHDLR----TDTYDHVQRLDMAFFEDRQTGDLMSVLnndVNQLERFLD---DGANSIIRVVVTVLGIGAILFYLNWQLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 160 LILV----VLGAAYVMISKVVMSRTKEGQAAVEGhyhtVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPV 235
Cdd:cd18565 158 LVALlpvpLIIAGTYWFQRRIEPRYRAVREAVGD----LNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 236 LDWWALASGLNRIASTISMMAILVIGTVLVQ------RGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARA 304
Cdd:cd18565 234 IRLRAAFFPVIRLVAGAGFVATFVVGGYWVLdgpplfTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMA 308
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
472-547 |
4.58e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 472 LSGGERQRVAIA--RAILKN--APILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHRLSTVREAD-LV-IFMDQG 545
Cdd:pfam02463 1078 LSGGEKTLVALAliFAIQKYkpAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADkLVgVTMVEN 1157
|
..
gi 503610856 546 RV 547
Cdd:pfam02463 1158 GV 1159
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
470-508 |
4.99e-06 |
|
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: 49.55 E-value: 4.99e-06
10 20 30
....*....|....*....|....*....|....*....
gi 503610856 470 NRLSGGERQRVAIARAILKNAPILVLDEATSALDVETEA 508
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA 198
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
18-288 |
8.15e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 47.96 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 18 KFRVGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAH-GRRAS--LLTE 94
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWiGARFDhrLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 95 AFGRIVSMPLSWHSQRGTSnALHTLLRACETLfglwlefmRQHLaTAVALMLLIPTAFA---------MDVRLSLILVVL 165
Cdd:cd18566 81 AFEHLLSLPLSFFEREPSG-AHLERLNSLEQI--------REFL-TGQALLALLDLPFVliflgliwyLGGKLVLVPLVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 166 GAAYVMISKVVMSRTKegQAAVEGHYHTV--FSHVSDSISNVSVVHSYNrieAETRELKKFtQRLLS----AQYPVLDWW 239
Cdd:cd18566 151 LGLFVLVAILLGPILR--RALKERSRADErrQNFLIETLTGIHTIKAMA---MEPQMLRRY-ERLQAnaayAGFKVAKIN 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 503610856 240 ALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFigfaNLLIGR 288
Cdd:cd18566 225 AVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIAC----TMLSGR 269
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
472-540 |
8.50e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 8.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 472 LSGGERQRVAIARAILKNAP---ILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAHRLSTVREADLVI 540
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWII 242
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
21-291 |
1.11e-05 |
|
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: 47.49 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFGVFNTIAFVL-------VSREADRLahgrRASLLT 93
Cdd:cd18588 4 LGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLsglrtylFSHTTNRI----DAELGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 94 EAFGRIVSMPLSWHSQRGTSNalhTLLRACEtlfglwLEFMRQHLaTAVALMLLIPTAFA------M---DVRLSLILVV 164
Cdd:cd18588 80 RLFRHLLRLPLSYFESRQVGD---TVARVRE------LESIRQFL-TGSALTLVLDLVFSvvflavMfyySPTLTLIVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 165 LGAAYVMISKVVM----SRTKEG-QAAVEGHyhtvfSHVSDSISNVSVVHSynrIEAETRELKKFTQRL---LSAQYPVL 236
Cdd:cd18588 150 SLPLYALLSLLVTpilrRRLEEKfQRGAENQ-----SFLVETVTGIETVKS---LAVEPQFQRRWEELLaryVKASFKTA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 237 DWWALASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFigfaNLLIGRLDQ 291
Cdd:cd18588 222 NLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF----NMLAGQVSQ 272
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-289 |
1.13e-05 |
|
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: 47.48 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 21 VGAIVIANIVLAAITIAEPILFGRIIDAISSQKDVApmLLLW-----AGFGVFNTIAFVLVSREADRLAHGRRASLLTEA 95
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLG--LLVLlalgmVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 96 FGRIVSMPLSWHSQRGTS---NALHTLLRACETLFGLWLEFMRQHLATAVALMLlipTAFAMDVRLSLILVVLGAAYVMI 172
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGeiqSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLV---AMLALDWRLALLSLVLLPLFVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 173 SKVVMSRTKEGQAAVEGHYHTVFSHVSD--SISNVSVVHSYNRIEAETRELKKFTQRLLSAQY--PVLDWWALASGlnRI 248
Cdd:cd18550 156 TRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVrqALAGRWFFAAL--GL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 503610856 249 ASTISMMAILVIGTVLVQRGELGVGEVIAFIGfanlLIGRL 289
Cdd:cd18550 234 FTAIGPALVYWVGGLLVIGGGLTIGTLVAFTA----LLGRL 270
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
472-540 |
1.44e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 45.92 E-value: 1.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 472 LSGGERQRVAIAR--AIL--KNAPILVLDEATSALDVETEARVKDAIDALRKDrTTFI-IAHRLSTVREADLVI 540
Cdd:cd03278 114 LSGGEKALTALALlfAIFrvRPSPFCVLDEVDAALDDANVERFARLLKEFSKE-TQFIvITHRKGTMEAADRLY 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
276-530 |
1.51e-05 |
|
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: 48.09 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 276 IAFIGFANLLIGRLDQMKAFATQIFEARAKLEDFFQLEDSVQDREEPADAGELKGVVGEVEFRDISFdfANSAQGVRNVS 355
Cdd:TIGR01257 1882 MAVEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYS--GTSSPAVDRLC 1959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 356 FKAKAGQTIAIVGPTGAGKTTLVNLLQrvhepkhGQILIDGVDiATVTRKSLRRSIATVFQDAGLMNRSIG-ENIRLGRE 434
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLT-------GDTTVTSGD-ATVAGKSILTNISDVHQNMGYCPQFDAiDDLLTGRE 2031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 435 DASL------------DEVMAAAEAAAASDFIEDRLNGydtvvgergnRLSGGERQRVAIARAILKNAPILVLDEATSAL 502
Cdd:TIGR01257 2032 HLYLyarlrgvpaeeiEKVANWSIQSLGLSLYADRLAG----------TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
250 260
....*....|....*....|....*....
gi 503610856 503 DVETEARVKDAI-DALRKDRTTFIIAHRL 530
Cdd:TIGR01257 2102 DPQARRMLWNTIvSIIREGRAVVLTSHSM 2130
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
335-517 |
1.57e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 335 VEFRDISFDFANSAQGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGqilidgvdiaTVTRKS-LRRSIAT 413
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG----------TVFRSAkVRMAVFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 414 VFQDAGLmnrsigenirlgreDASLDEVMAAAEAAaaSDFIEDRLNGYDTVVGERGN-------RLSGGERQRVAIARAI 486
Cdd:PLN03073 579 QHHVDGL--------------DLSSNPLLYMMRCF--PGVPEQKLRAHLGSFGVTGNlalqpmyTLSGGQKSRVAFAKIT 642
|
170 180 190
....*....|....*....|....*....|.
gi 503610856 487 LKNAPILVLDEATSALDVetearvkDAIDAL 517
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDL-------DAVEAL 666
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
352-517 |
1.91e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 352 RNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQIlidgvdiatvtRKSLRRSIATVFQD-----AGLMN---- 422
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIGYYAQDhaydfENDLTlfdw 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 ----RSIGEN---IR--LGREDASLDEvmaaaeaaaasdfiedrlngydtvVGERGNRLSGGERQRVAIARAILKNAPIL 493
Cdd:PRK15064 405 msqwRQEGDDeqaVRgtLGRLLFSQDD------------------------IKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180
....*....|....*....|....
gi 503610856 494 VLDEATSALDVEtearvkdAIDAL 517
Cdd:PRK15064 461 VMDEPTNHMDME-------SIESL 477
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
347-548 |
2.08e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 347 SAQGVRN-VSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDG--VDIATvTRKSLRRSIATVFQD---AGL 420
Cdd:PRK11288 264 KGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIRAGIMLCPEDrkaEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 421 MN-RSIGENIRL---------------GREDASLDEvmaaaeaaaasdFIEdRLN----GYDTVVGErgnrLSGGERQRV 480
Cdd:PRK11288 343 IPvHSVADNINIsarrhhlragclinnRWEAENADR------------FIR-SLNiktpSREQLIMN----LSGGNQQKA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 481 AIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIAHrlSTVRE----ADLVIFMDQGRVV 548
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVS--SDLPEvlgvADRIVVMREGRIA 475
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
472-506 |
2.44e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 2.44e-05
10 20 30
....*....|....*....|....*....|....*
gi 503610856 472 LSGGERQRVAIARAILKNAPILVLDEATSALDVET 506
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
471-542 |
2.61e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 2.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 471 RLSGGERQRVAIARAI----LKNAPILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVREADLVIFM 542
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELADKLIHI 153
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
365-540 |
3.72e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.91 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 365 AIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVTRKSLRR-SIATVFQDAglmnrsIGENIRLGREDASLDEVMA 443
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREGEVRaQVKLAFENA------NGKKYTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 444 AAEAAAASdFIEDrlngydtvvgERGnRLSGGERQ------RVAIARAILKNAPILVLDEATSALDVET-EARVKDAIDA 516
Cdd:cd03240 100 CHQGESNW-PLLD----------MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEE 167
|
170 180
....*....|....*....|....*.
gi 503610856 517 LRKD--RTTFIIAHRLSTVREADLVI 540
Cdd:cd03240 168 RKSQknFQLIVITHDEELVDAADHIY 193
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
364-528 |
4.12e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 364 IAIVGPTGAGKTTLVNLL-------QRVHEPKHGQILIDGVDIATVT--------------------------RKSLRRS 410
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalygkARSRSKLRSDLINVGSEEASVElefehggkryrierrqgefaefleakPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 411 IATVFQDAGLmnRSIGENIRlGREDASLDEVMAAAEAAAASDFIEDRLNGYDTVvgergNRLSGGERQRVAIARAILkna 490
Cdd:COG0419 106 LKRLLGLEIY--EELKERLK-ELEEALESALEELAELQKLKQEILAQLSGLDPI-----ETLSGGERLRLALADLLS--- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 503610856 491 piLVLDeaTSALDVETEARVKDAIDALRkdrttfIIAH 528
Cdd:COG0419 175 --LILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
29-279 |
4.49e-05 |
|
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: 45.73 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 29 IVLAAIT---IAEPILFGRIIDAISSQKDVAPMLLLWAGF-GVFNTIAFVLVSRE--ADRLAHGRRASLLTEAFGRIVSM 102
Cdd:cd18561 3 LLGLLITalyIAQAWLLARALARIFAGGPWEDIMPPLAGIaGVIVLRAALLWLRErvAHRAAQRVKQHLRRRLFAKLLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 103 PLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVALMLLIPTAFAMDVRLSLILVVLGAAYVMISKVVMSRTKE 182
Cdd:cd18561 83 GPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 183 GQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALASGLNRIASTISMMAILVIGT 262
Cdd:cd18561 163 TGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGA 242
|
250
....*....|....*..
gi 503610856 263 VLVQRGELGVGEVIAFI 279
Cdd:cd18561 243 LRVLGGQLTLSSLLLIL 259
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
472-537 |
6.35e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 6.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 472 LSGGERQRVAIAR--AIL--KNAPILVLDEATSALDvetEARVKDAIDALRK--DRTTFI-IAHRLSTVREAD 537
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIFkvKPAPFCILDEVDAPLD---DANVERFANLLKEfsKNTQFIvITHNKGTMEVAD 1159
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
350-526 |
6.52e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 43.84 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 350 GVRNVSFKAKAGQTI--------AIVGPTGAGKTTLVNllqrvhepkhgqilidgvdiatvtrkslrrSIATVFQdaglm 421
Cdd:cd03239 3 QITLKNFKSYRDETVvggsnsfnAIVGPNGSGKSNIVD------------------------------AICFVLG----- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 422 nrsiGENIRLGREDaSLDEVMAAAEAAAASDFIEDRL-NGYDTVVGERGNR-LSGGERQRVAIAR--AI--LKNAPILVL 495
Cdd:cd03239 48 ----GKAAKLRRGS-LLFLAGGGVKAGINSASVEITFdKSYFLVLQGKVEQiLSGGEKSLSALALifALqeIKPSPFYVL 122
|
170 180 190
....*....|....*....|....*....|.
gi 503610856 496 DEATSALDVETEARVKDAIDALRKDRTTFII 526
Cdd:cd03239 123 DEIDAALDPTNRRRVSDMIKEMAKHTSQFIV 153
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
125-307 |
6.72e-05 |
|
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: 45.10 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 125 TLFGLWLEFMRqhLATAVALMLLiptafaMDVRLSLILVVLGAAYVMISKVVMSR----TKEGQAAVEghyhTVFSHVSD 200
Cdd:cd18554 123 GLMNIWLDMIT--IIIAICIMLV------LNPKLTFVSLVIFPFYILAVKYFFGRlrklTKERSQALA----EVQGFLHE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 201 SISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWALAsgLNRIASTISMMAILVI--GTVLVQRGELGVGEVIAF 278
Cdd:cd18554 191 RIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKT--FSAVNTITDLAPLLVIgfAAYLVIEGNLTVGTLVAF 268
|
170 180
....*....|....*....|....*....
gi 503610856 279 IGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18554 269 VGYMERMYSPLRRLVNSFTTLTQSFASMD 297
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
472-548 |
1.96e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 472 LSGGERQRVAIARAILKNAPILVLDEATSALDVET----EARVKD---AIDALRKDRtTFIiaHRLSTvREADLvifmDQ 544
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiewlEGFLKTfqgSIIFISHDR-SFI--RNMAT-RIVDL----DR 228
|
....
gi 503610856 545 GRVV 548
Cdd:PRK11147 229 GKLV 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
472-540 |
2.63e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 2.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503610856 472 LSGGERQRVAIARAILKNA---PILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAHRLSTVREADLVI 540
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYII 902
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
472-544 |
2.96e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 472 LSGGERQ------RVAIARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRT----TFIIAHRLSTVREADLVIF 541
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISHHRELLSVADVAYE 881
|
...
gi 503610856 542 MDQ 544
Cdd:PRK01156 882 VKK 884
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
24-307 |
3.51e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 42.89 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 24 IVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAGFG---VFNTIafvlvsreadrLAHGRRASLL-------- 92
Cdd:cd18783 7 VAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVialLFEGI-----------LGYLRRYLLLvattrida 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 93 ---TEAFGRIVSMPLSWHSQRGTSNALHTL-----LRacetlfglwlEFMRQHLAT----AVALMLLIPTAFAMDVRLSL 160
Cdd:cd18783 76 rlaLRTFDRLLSLPIDFFERTPAGVLTKHMqqierIR----------QFLTGQLFGtlldATSLLVFLPVLFFYSPTLAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 161 ILVVLGAAYVMISKVVMSRTKEGQAAVEGHYHTVFSHVSDSISNVSVVHSYNRIEAETRELKKFTQRLLSAQYPVLDWWA 240
Cdd:cd18783 146 VVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSN 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503610856 241 LASGLNRIASTISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18783 226 WPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVR 292
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
349-567 |
3.63e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 349 QGVRNVSFKAKAGQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQILIDGVDIATVT-RKSLRRSIATVFQdaGL-----MN 422
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhRRAVCPRIAYMPQ--GLgknlyPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 423 RSIGENIrlgredasldevmaaaeaaaasDFIeDRLNGYDTvvGERGNR--------------------LSGGERQRVAI 482
Cdd:NF033858 93 LSVFENL----------------------DFF-GRLFGQDA--AERRRRidellratglapfadrpagkLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 483 ARAILKNAPILVLDEATSALDVETEARVKDAIDALRKDRT--TFIIAhrlsT--VREA---DLVIFMDQGRVVEMGGFHE 555
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA----TayMEEAerfDWLVAMDAGRVLATGTPAE 223
|
250
....*....|....*...
gi 503610856 556 LSQSNGR------FAALL 567
Cdd:NF033858 224 LLARTGAdtleaaFIALL 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
472-556 |
4.22e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 472 LSGGERQRVAIARAiLKNAP-ILVLDEATSALDVETEARVKDAIDALRKDRTTFI--IAHRLSTVRE-ADLVIFMDQGRV 547
Cdd:PRK15093 159 LTEGECQKVMIAIA-LANQPrLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQT 237
|
....*....
gi 503610856 548 VEMGGFHEL 556
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
472-540 |
8.00e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.09 E-value: 8.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503610856 472 LSGGERQRVAIARAILKN--APILVLDEATSALDVETEARVKDAIDALR-KDRTTFIIAHRLSTVREADLVI 540
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVI 209
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
25-164 |
8.22e-04 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 41.63 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 25 VIANIVLAAITIAEPILFGRIIDAI----SSQKDVAPMLLLWAGFGVFNTIAFVLVSREADRLAHGRRASLLTEAFGRIV 100
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVflegAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503610856 101 SMPLSWHSQRGTSNALHTLLRACETLFGLWLEFMRQHLATAVA-LMLLIpTAFAMDVRLSLILVV 164
Cdd:cd18584 82 ALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVpLLILV-AVFPLDWVSALILLV 145
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
22-307 |
8.51e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 41.76 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 22 GAIVIANIVLAAITIAEPILFGRIIDAISSQKDVAPMLLLWAG---FGVFNTIAFVLVSREADRLAHGRRASLLTEAFGR 98
Cdd:cd18779 5 GQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGlaaLVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 99 IVSMPLSWHSQRGTSNAL-----HTLLRacetlfglwlEFMRQHLATAV--ALMLLIPTA--FAMDVRLSLILVVLGAAY 169
Cdd:cd18779 85 LLRLPYRFFQQRSTGDLLmrlssNATIR----------ELLTSQTLSALldGTLVLGYLAllFAQSPLLGLVVLGLAALQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 170 VMI-------SKVVMSRTKEGQAAVEGHyhtvfshvsdsisnvsVVHSYNRIE------AETRELKKFTQRLLSAQYPVL 236
Cdd:cd18779 155 VALllatrrrVRELMARELAAQAEAQSY----------------LVEALSGIEtlkasgAEDRALDRWSNLFVDQLNASL 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503610856 237 DWWALASGLNRIASTISM---MAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18779 219 RRGRLDALVDALLATLRLaapLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLE 292
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
360-382 |
1.72e-03 |
|
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: 40.07 E-value: 1.72e-03
10 20
....*....|....*....|...
gi 503610856 360 AGQTIAIVGPTGAGKTTLVNLLQ 382
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALL 106
|
|
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
364-381 |
3.44e-03 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 39.00 E-value: 3.44e-03
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
364-413 |
4.04e-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: 37.90 E-value: 4.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503610856 364 IAIVGPTGAGKTTLVNLLQRVHEPKHGQIL-----------IDGVDIATVTRKSLRRSIAT 413
Cdd:cd00071 2 IVLSGPSGVGKSTLLKRLLEEFDPNFGFSVshttrkprpgeVDGVDYHFVSKEEFERLIEN 62
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
364-382 |
4.75e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.86 E-value: 4.75e-03
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
464-551 |
5.24e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 464 VVGERGNRLSGGERQRVAIARAILKNAPILVLDEATSALD-VeteARvkDA-----IDALRKDRTT-FIIAHRLStvrEA 536
Cdd:NF033858 390 VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpV---AR--DMfwrllIELSREDGVTiFISTHFMN---EA 461
|
90
....*....|....*...
gi 503610856 537 ---DLVIFMDQGRVVEMG 551
Cdd:NF033858 462 ercDRISLMHAGRVLASD 479
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
361-392 |
7.94e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 7.94e-03
10 20 30
....*....|....*....|....*....|..
gi 503610856 361 GQTIAIVGPTGAGKTTLVNLLQRVHEPKHGQI 392
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
392-560 |
9.23e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 392 ILIDGVDIATVTRKSLRRSIAtVFQDAGLMnrsigenirlGREDASLDEVMAAaeaaaasdfIEDRLN-----GYDTVVG 466
Cdd:TIGR00630 423 VTVGGKSIADVSELSIREAHE-FFNQLTLT----------PEEKKIAEEVLKE---------IRERLGflidvGLDYLSL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503610856 467 ER-GNRLSGGERQRVAIARAI---LKNApILVLDEATSALDVETEARVKDAIDALRKDRTTFIIA-HRLSTVREADLVIF 541
Cdd:TIGR00630 483 SRaAGTLSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVeHDEDTIRAADYVID 561
|
170 180
....*....|....*....|....*
gi 503610856 542 MDQ------GRVVEMGGFHELSQSN 560
Cdd:TIGR00630 562 IGPgagehgGEVVASGTPEEILANP 586
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
250-307 |
9.67e-03 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 38.23 E-value: 9.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503610856 250 STISMMAILVIGTVLVQRGELGVGEVIAFIGFANLLIGRLDQMKAFATQIFEARAKLE 307
Cdd:cd18569 235 SALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDME 292
|
|
| |
