|
Name |
Accession |
Description |
Interval |
E-value |
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-270 |
6.53e-129 |
|
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: 365.58 E-value: 6.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 27 WPQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERL 106
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 RNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSkvglieecdelsliseqeqpnfsshklrnrfidlntvVKSGG 186
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR-------------------------------------VSEGG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKE 266
Cdd:cd03369 124 LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
....
gi 767157600 267 YDHP 270
Cdd:cd03369 204 YDHP 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-270 |
6.52e-122 |
|
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: 348.33 E-value: 6.52e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSI 110
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGLIEECDELSliseqeqpnfsshklrnrfIDLNTVVKSGGSNLS 190
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLP-------------------GGLDTVVEEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 191 QGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHP 270
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-289 |
1.71e-81 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 268.53 E-value: 1.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTDIPSESNGYIS---PPANWPQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSII 77
Cdd:PLN03130 1203 LNAVERVGTYIDLPSEAPLVIEnnrPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSML 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 78 AAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGLIEecdelsl 157
Cdd:PLN03130 1283 NALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKD------- 1355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 158 iseqeqpnfsshKLRNRFIDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN 237
Cdd:PLN03130 1356 ------------VIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS 1423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767157600 238 TTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLISDRNTIFYRLCRQSG 289
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-305 |
5.62e-77 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 255.67 E-value: 5.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTDIPSESNGYIS---PPANWPQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSII 77
Cdd:PLN03232 1200 LNSVERVGNYIDLPSEATAIIEnnrPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 78 AAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGLIEECDelsl 157
Cdd:PLN03232 1280 NALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVID---- 1355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 158 iseqeqpnfsshklRNRFiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN 237
Cdd:PLN03232 1356 --------------RNPF-GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767157600 238 TTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLISDRNTIFYRLCRQSGEfENLFELAKVSFDNK 305
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP-ANAQYLSNLVFERR 1487
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-290 |
7.05e-76 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 242.38 E-value: 7.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTDIPSESNGYISPPANWPQTGDVELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI 80
Cdd:COG1132 308 LASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 81 YRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLdpfdRY-----SDVQIYGVLSKVGlieeCDEl 155
Cdd:COG1132 387 LRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI----RYgrpdaTDEEVEEAAKAAQ----AHE- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 156 sliseqeqpnfsshklrnrFID-----LNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKT 230
Cdd:COG1132 458 -------------------FIEalpdgYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 231 IRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLIsDRNTIFYRLCR-QSGE 290
Cdd:COG1132 519 LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL-ARGGLYARLYRlQFGE 578
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-289 |
1.23e-75 |
|
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: 251.79 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 3 SVERIKEYTDIPSESNGYI---SPPANWPQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAA 79
Cdd:TIGR00957 1252 AVERLKEYSETEKEAPWQIqetAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLG 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 80 IYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLskvglieecdELSLIS 159
Cdd:TIGR00957 1332 LFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWAL----------ELAHLK 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 160 E--QEQPNfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN 237
Cdd:TIGR00957 1402 TfvSALPD-----------KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED 1470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767157600 238 TTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLISDRNtIFYRLCRQSG 289
Cdd:TIGR00957 1471 CTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG-IFYSMAKDAG 1521
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-287 |
1.72e-71 |
|
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: 233.96 E-value: 1.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 3 SVERIKEYTDIPSESNGYISPPANWPQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYR 82
Cdd:COG2274 444 ALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 83 LSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNL---DPfdRYSDVQIYGVLSKVGLIEEcdelslIs 159
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDF------I- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 160 eQEQPNfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTT 239
Cdd:COG2274 595 -EALPM-----------GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT 662
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767157600 240 ILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLISdRNTIFYRLCRQ 287
Cdd:COG2274 663 VIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQQ 709
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-275 |
4.98e-64 |
|
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: 211.16 E-value: 4.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTDIPSESNGYISPPANWPQTGDVELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI 80
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 81 YRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNL---DPfdRYSDVQIYGVLSKVGLieecdeLSL 157
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEAALEAAGL------DEF 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 158 ISEQEQpnfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN 237
Cdd:COG4988 456 VAALPD-------------GLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG 522
|
250 260 270
....*....|....*....|....*....|....*...
gi 767157600 238 TTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLIS 275
Cdd:COG4988 523 RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
33-263 |
5.36e-64 |
|
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: 199.15 E-value: 5.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGTVRSNLdpfdrysdvqiygvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksggsnLSQG 192
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------------------------LSGG 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 193 QRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGR 263
Cdd:cd03228 101 QRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
31-277 |
3.86e-63 |
|
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: 198.99 E-value: 3.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYSpHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSI 110
Cdd:cd03254 1 GEIEFENVNFSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLDPFDRYSDVQIygvlskvgLIEECDELSLiseqeqpnfsshklrNRFI-----DLNTVVKSG 185
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEE--------VIEAAKEAGA---------------HDFImklpnGYDTVLGEN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 186 GSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVK 265
Cdd:cd03254 137 GGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
250
....*....|..
gi 767157600 266 EYDHPYTLISDR 277
Cdd:cd03254 217 EEGTHDELLAKK 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-284 |
2.67e-62 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 213.49 E-value: 2.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTD-IPSES---------------------NGYI-----SPPANWP---QTGDVELKNLSLRYSPHSSKAL 50
Cdd:PTZ00243 1247 MNSVERLLYYTDeVPHEDmpeldeevdalerrtgmaadvTGTVviepaSPTSAAPhpvQAGSLVFEGVQMRYREGLPLVL 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 51 DNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDP 130
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDP 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 131 FDRYSDVQIYGVLSKVGLIEEcdelsLISEQEQpnfsshklrnrfIDlnTVVKSGGSNLSQGQRQLLCLARSMLG-ARNI 209
Cdd:PTZ00243 1407 FLEASSAEVWAALELVGLRER-----VASESEG------------ID--SRVLEGGSNYSVGQRQLMCMARALLKkGSGF 1467
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 210 MLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLISDRNTIFYRL 284
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSM 1542
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
31-286 |
2.81e-57 |
|
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: 185.11 E-value: 2.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSI 110
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLskvglieECDELSLISeQEQPNfsshklrnrfiDLNTVVKSGGSNLS 190
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEAL-------EIAQLKNMV-KSLPG-----------GLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 191 QGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHP 270
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTP 238
|
250
....*....|....*.
gi 767157600 271 YTLISDRNTIFYRLCR 286
Cdd:cd03288 239 ENLLAQEDGVFASLVR 254
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
33-266 |
1.81e-54 |
|
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: 177.04 E-value: 1.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSsKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:cd03253 1 IEFENVTFAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGTVRSNLdpfdRY-----SDVQIYGVlSKVGLIeecdelsliseqeqpnfssHKLRNRFID-LNTVVKSGG 186
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEA-AKAAQI-------------------HDKIMRFPDgYDTIVGERG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKE 266
Cdd:cd03253 136 LKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-266 |
1.96e-52 |
|
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: 180.68 E-value: 1.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTDIPSESN-GYISPPAnwpQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAA 79
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEKDtGTRAIER---ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 80 IYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNL---DPfDRYSDVQIYGVLSKVGLIEECDELS 156
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDFVDKLP 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 157 LiseqeqpnfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK 236
Cdd:TIGR02203 457 L-------------------GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ 517
|
250 260 270
....*....|....*....|....*....|
gi 767157600 237 NTTILTIAHRLRSVIDYDKILVMEMGRVKE 266
Cdd:TIGR02203 518 GRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
33-266 |
3.69e-52 |
|
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: 171.18 E-value: 3.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY-SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSIS 111
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPTLFDGTVRSNLdpfdRYSDVQiygvlSKVGLIEECDELSLISEqeqpnFSShKLRNRFidlNTVVKSGGSNLSQ 191
Cdd:cd03249 81 LVSQEPVLFDGTIAENI----RYGKPD-----ATDEEVEEAAKKANIHD-----FIM-SLPDGY---DTLVGERGSQLSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 192 GQRQLLCLARSMLgaRN--IMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKE 266
Cdd:cd03249 143 GQKQRIAIARALL--RNpkILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-266 |
3.29e-51 |
|
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: 168.56 E-value: 3.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGTVRSNLdpfdRYSDvqiygvlskvgliEECDELSLISEQEQPNfsSHKLRNRFID-LNTVVKSGGSNLSQ 191
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYGR-------------PGATREEVEEAARAAN--AHEFIMELPEgYDTVIGERGVKLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKE 266
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-278 |
3.97e-50 |
|
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: 178.18 E-value: 3.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTDIPSESngyiSPPAN---------------------WPQTGDVELKNLSLRYSPHSSKALDNVSFKVKA 59
Cdd:TIGR01271 1169 MRSVSRVFKFIDLPQEE----PRPSGgggkyqlstvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEG 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 60 GTKVGIVGRTGAGKSSIIAAIYRLSDWEnGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQI 139
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEI 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 140 YGVLSKVGLieecdeLSLIseqEQpnfsshklrnrFID-LNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATAS 218
Cdd:TIGR01271 1324 WKVAEEVGL------KSVI---EQ-----------FPDkLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 219 IDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLISDRN 278
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
31-264 |
4.77e-50 |
|
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: 165.07 E-value: 4.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSI 110
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLDPFDRYSDVQiygvlskvgLIEECDELSLISE--QEQPNfsshklrnrfiDLNTVVKSGGSN 188
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDE---------RILRAAELAGVTDfvNKHPN-----------GLDLQIGERGRG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRV 264
Cdd:cd03245 141 LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
31-278 |
2.27e-48 |
|
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: 162.72 E-value: 2.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEnGTIIIDNKDIKHIPLERLRNSI 110
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGLieecdelSLISEQeqpnfsshklrnrFID-LNTVVKSGGSNL 189
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGL-------KSVIEQ-------------FPGqLDFVLVDGGCVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 190 SQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDH 269
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 219
|
....*....
gi 767157600 270 PYTLISDRN 278
Cdd:cd03289 220 IQKLLNEKS 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
31-289 |
2.11e-47 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 167.45 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSI 110
Cdd:PRK13657 333 GAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLDpfdrysdvqiygvLSKVGLIEEcdELSLISEQEQPnfsshklrNRFID-----LNTVVKSG 185
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIR-------------VGRPDATDE--EMRAAAERAQA--------HDFIErkpdgYDTVVGER 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 186 GSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVK 265
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
250 260
....*....|....*....|....*..
gi 767157600 266 E---YDHpytlISDRNTIFYRLCRQSG 289
Cdd:PRK13657 549 EsgsFDE----LVARGGRFAALLRAQG 571
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
31-266 |
1.30e-45 |
|
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: 162.68 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYSPHSsKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSI 110
Cdd:COG5265 356 GEVRFENVSFGYDPER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLdpfdRY-----SDVQiygvlskvglIEECDELSLISEqeqpnfsshklrnrFID-----LNT 180
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNI----AYgrpdaSEEE----------VEAAARAAQIHD--------------FIEslpdgYDT 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 181 VVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVME 260
Cdd:COG5265 487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLE 566
|
....*.
gi 767157600 261 MGRVKE 266
Cdd:COG5265 567 AGRIVE 572
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
33-284 |
2.07e-45 |
|
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: 153.80 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGTVRSNLDPFDRYSDVQiygvlskvgLIEECDELSLISEqeqpnFSShKLRNRFidlNTVVKSGGSNLSQG 192
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSME---------RVIEAAKLAGAHD-----FIS-ELPEGY---DTIVGEQGAGLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 193 QRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYT 272
Cdd:cd03252 143 QRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDE 222
|
250
....*....|..
gi 767157600 273 LIsDRNTIFYRL 284
Cdd:cd03252 223 LL-AENGLYAYL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-259 |
5.06e-44 |
|
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: 157.45 E-value: 5.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 24 PANWPQTGDVELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPL 103
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 104 ERLRNSISCIPQDPTLFDGTVRSNLDPFDRY-SDVQIYGVLSKVGLIEecdelsLISEQEQpnfsshklrnrfiDLNTVV 182
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDE------FVAALPQ-------------GLDTPI 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 183 KSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVM 259
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
31-267 |
2.48e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 153.64 E-value: 2.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSI 110
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNL--DPFDRYSDVQIygvlskvgliEECDELSLISEqeqpnfsshklrnrFID-----LNTVVK 183
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIayARTEQYSREQI----------EEAARMAYAMD--------------FINkmdngLDTVIG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 SGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGR 263
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
....
gi 767157600 264 VKEY 267
Cdd:PRK11176 556 IVER 559
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-287 |
1.21e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 148.82 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSVERIKEYTDIPSEsngyISPPAN---WPQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSII 77
Cdd:PRK11160 308 IASARRINEITEQKPE----VTFPTTstaAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 78 AAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNL---DPfdRYSDVQIYGVLSKVGlieecde 154
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVG------- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 155 LSLISEQEQPnfsshklrnrfidLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRET 234
Cdd:PRK11160 455 LEKLLEDDKG-------------LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH 521
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767157600 235 MKNTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHPYTLISDRNTiFYRLCRQ 287
Cdd:PRK11160 522 AQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR-YYQLKQR 573
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-290 |
2.87e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 147.68 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 5 ERIKEYTDIPSESNGYISPPANWPQTGDVELKNLSLrYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI---- 80
Cdd:PRK11174 322 ESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgfl 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 81 -YRlsdwenGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNL---DPfdRYSDVQIYGVLSKVGLIEECDELS 156
Cdd:PRK11174 401 pYQ------GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWVSEFLPLLP 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 157 LiseqeqpnfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK 236
Cdd:PRK11174 473 Q-------------------GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767157600 237 NTTILTIAHRLRSVIDYDKILVMEMGRVKEYDHpYTLISDRNTIFYRLCRQSGE 290
Cdd:PRK11174 534 RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD-YAELSQAGGLFATLLAHRQE 586
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
50-217 |
2.68e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 135.08 E-value: 2.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 50 LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDG-TVRSNL 128
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 129 -------DPFDRYSDVQIYGVLSKVGLIEecdelsliseqeqpnfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLAR 201
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGD--------------------------LADRPVGERPGTLSGGQRQRVAIAR 134
|
170
....*....|....*.
gi 767157600 202 SMLGARNIMLIDEATA 217
Cdd:pfam00005 135 ALLTKPKLLLLDEPTA 150
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-290 |
3.90e-38 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 142.16 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 5 ERIKEYTDIPSESNGYISPPAnwpQTGDVELKNLSLRYSpHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLS 84
Cdd:PRK10790 316 ERVFELMDGPRQQYGNDDRPL---QSGRIDIDNVSFAYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 85 DWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGLIEecdelsliseqeqp 164
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAE-------------- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 165 nfsshkLRNRFID-LNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTI 243
Cdd:PRK10790 458 ------LARSLPDgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI 531
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767157600 244 AHRLRSVIDYDKILVMEMGRVKEYDHPYTLISDRNTIF--YRLcRQSGE 290
Cdd:PRK10790 532 AHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWqmYQL-QLAGE 579
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-286 |
7.70e-37 |
|
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: 138.94 E-value: 7.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 5 ERIKEYTDIPSESNGYISPPAnwPQTGDVELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLS 84
Cdd:TIGR03797 426 ERAKPILEALPEVDEAKTDPG--KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFE 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 85 DWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGLIEECDELSLiseqeqp 164
Cdd:TIGR03797 504 TPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPM------- 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 165 nfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIrETMKNTTILtIA 244
Cdd:TIGR03797 577 ------------GMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL-ERLKVTRIV-IA 642
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767157600 245 HRLRSVIDYDKILVMEMGRVKEYDHPYTLISdRNTIFYRLCR 286
Cdd:TIGR03797 643 HRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQLAR 683
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
33-266 |
3.39e-35 |
|
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: 125.50 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIkHIPLERLRNSISC 112
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGTVRSNLdpfdrysdvqiygvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksgGSNLSQG 192
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------------------------GRRFSGG 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767157600 193 QRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKE 266
Cdd:cd03247 103 ERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
34-263 |
2.54e-34 |
|
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: 122.35 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYspHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCI 113
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 114 PQdptlfdgtvrsnldpfdrysdvqiygvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksggsnLSQGQ 193
Cdd:cd00267 79 PQ-------------------------------------------------------------------------LSGGQ 85
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767157600 194 RQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKILVMEMGR 263
Cdd:cd00267 86 RQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-247 |
1.63e-33 |
|
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: 128.63 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 3 SVERIKEYTDIPSESNGYISPPAN--WPQTGDVELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI 80
Cdd:TIGR02868 303 AAERIVEVLDAAGPVAEGSAPAAGavGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 81 YRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLdpfdRY-----SDVQIYGVLSKVGLIEECDEL 155
Cdd:TIGR02868 382 AGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL----RLarpdaTDEELWAALERVGLADWLRAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 156 sliseqeqPNfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM 235
Cdd:TIGR02868 458 --------PD-----------GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
250
....*....|..
gi 767157600 236 KNTTILTIAHRL 247
Cdd:TIGR02868 519 SGRTVVLITHHL 530
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-267 |
1.65e-33 |
|
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: 122.61 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSS--KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERL---R 107
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDPtlfdgtvRSNLDPfdRYSdV--QIYGVLSKVGLIEECDELSLISEQEQPNFS-SHKLRNRFIdlntvvks 184
Cdd:cd03257 82 KEIQMVFQDP-------MSSLNP--RMT-IgeQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlPEEVLNRYP-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 185 ggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHRLrSVIDY--DKILVME 260
Cdd:cd03257 144 --HELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDL-GVVAKiaDRVAVMY 220
|
....*..
gi 767157600 261 MGRVKEY 267
Cdd:cd03257 221 AGKIVEE 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
34-264 |
2.39e-33 |
|
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: 120.40 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCI 113
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 114 PQDPTLFDGTVRSNLdpfdrysdvqiygvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksggsnLSQGQ 193
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------------------------LSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767157600 194 RQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRET-MKNTTILTIAHRLRSVIDYDKILVMEMGRV 264
Cdd:cd03246 102 RQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-264 |
2.45e-33 |
|
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: 122.19 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRY--SPHSsKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRN 108
Cdd:cd03248 10 GIVKFQNVTFAYptRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 109 SISCIPQDPTLFDGTVRSNLDpfdrysdvqiYGVLSKVglIEECDEL-------SLISEQEQpnfsshklrnrfiDLNTV 181
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIA----------YGLQSCS--FECVKEAaqkahahSFISELAS-------------GYDTE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 182 VKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEM 261
Cdd:cd03248 144 VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDG 223
|
...
gi 767157600 262 GRV 264
Cdd:cd03248 224 GRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-267 |
3.08e-33 |
|
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: 127.94 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 30 TGDVELKNLSLRYsPHSSKA-LDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSdweNGTIIIDNKDIKHIPLER 105
Cdd:COG4618 328 KGRLSVENLTVVP-PGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTlarLLVGVWPPT---AGSVRLDGADLSQWDREE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGlieeCDELSLiseqeqpnfsshKLRNRFidlNTVVKSG 185
Cdd:COG4618 404 LGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAG----VHEMIL------------RLPDGY---DTRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 186 GSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIREtMK--NTTILTIAHR---LRSVidyDKILVME 260
Cdd:COG4618 465 GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKarGATVVVITHRpslLAAV---DKLLVLR 540
|
....*..
gi 767157600 261 MGRVKEY 267
Cdd:COG4618 541 DGRVQAF 547
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-266 |
3.12e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.07 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 1 MSSV---ERIKEYTDIP--SESNGYISPPanwPQTGDVELKNLSLRYSPHSSK-ALDNVSFKVKAGTKVGIVGRTGAGKS 74
Cdd:TIGR00958 445 MQAVgasEKVFEYLDRKpnIPLTGTLAPL---NLEGLIEFQDVSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKS 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 75 SIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLD-PFDRYSDVQIYGVlskvglIEECD 153
Cdd:TIGR00958 522 TVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAA------AKAAN 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 154 ELSLISEQEQpnfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRE 233
Cdd:TIGR00958 596 AHDFIMEFPN-------------GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL----DAECEQLLQE 658
|
250 260 270
....*....|....*....|....*....|....*
gi 767157600 234 TM--KNTTILTIAHRLRSVIDYDKILVMEMGRVKE 266
Cdd:TIGR00958 659 SRsrASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
33-267 |
1.06e-31 |
|
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: 117.67 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWE-----NGTIIIDNKDIKHIPLER-- 105
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTLFDGTVRSNLdpfdRYSdVQIYGVLSKVGLiEECDELSLiseqeqpnfsshklrnRFIDLNTVVK-- 183
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNV----AYG-LRLHGIKLKEEL-DERVEEAL----------------RKAALWDEVKdr 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 SGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDY-DKILVMEMG 262
Cdd:cd03260 137 LHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNG 216
|
....*
gi 767157600 263 RVKEY 267
Cdd:cd03260 217 RLVEF 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
34-263 |
1.19e-30 |
|
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: 114.49 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCI 113
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 114 PQDPT--LFDGTVRS---------NLDPFDRYSDVQiyGVLSKVGLIEecdelsliseqeqpnfsshkLRNRFIdlntvv 182
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafglenlGLPEEEIEERVE--EALELVGLEG--------------------LRDRSP------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 ksggSNLSQGQRQLLCLArSMLGAR-NIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKILVM 259
Cdd:cd03225 133 ----FTLSGGQKQRVAIA-GVLAMDpDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVL 207
|
....
gi 767157600 260 EMGR 263
Cdd:cd03225 208 EDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
33-276 |
9.45e-30 |
|
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: 117.70 E-value: 9.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWE---NGTIIIDNKDIKHIPLERLRNS 109
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTlfdgtvrSNLDPfdrysdvqiygvlSKVGL-IEECDELSLISEQEQPNFSSHKLrnRFIDLNTVVKSGGSN 188
Cdd:COG1123 85 IGMVFQDPM-------TQLNP-------------VTVGDqIAEALENLGLSRAEARARVLELL--EAVGLERRLDRYPHQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILVMEMGRVK 265
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIaDRVVVMDDGRIV 222
|
250
....*....|.
gi 767157600 266 EYDHPYTLISD 276
Cdd:COG1123 223 EDGPPEEILAA 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
33-272 |
1.21e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 114.62 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY---SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP---LERL 106
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 RNSISCIPQDPTlfdgtvrSNLDPFDRYSDV-----QIYGVLSKVGLIEECDEL----SLISEqeqpnfsshkLRNRFId 177
Cdd:COG1123 341 RRRVQMVFQDPY-------SSLNPRMTVGDIiaeplRLHGLLSRAERRERVAELlervGLPPD----------LADRYP- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 178 lntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHRLRSVIDY-D 254
Cdd:COG1123 403 ---------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLTYLFISHDLAVVRYIaD 473
|
250 260
....*....|....*....|....*...
gi 767157600 255 KILVMEMGRVKEYD----------HPYT 272
Cdd:COG1123 474 RVAVMYDGRIVEDGpteevfanpqHPYT 501
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-259 |
1.98e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 106.65 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 28 PQTGDVELKNLSLRYSPHSSKAL-DNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIII-DNKDIKHIPLER 105
Cdd:PTZ00265 378 KDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTLFDGTVRSNL-------------------DPFDRYSD--------VQIYGVLSKV-------GLIEE 151
Cdd:PTZ00265 458 WRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQENknkrnscrAKCAGDLNDMsnttdsnELIEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 152 CDELSLISEQEQPNFSSHKLRNRFID-----LNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAK 226
Cdd:PTZ00265 538 RKNYQTIKDSEVVDVSKKVLIHDFVSalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260 270
....*....|....*....|....*....|....*
gi 767157600 227 IQKTIRETMKNTTILT--IAHRLRSVIDYDKILVM 259
Cdd:PTZ00265 618 VQKTINNLKGNENRITiiIAHRLSTIRYANTIFVL 652
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
33-264 |
2.01e-25 |
|
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: 99.39 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKS---SIIAAIYRLSDwenGTIIIDNKDIKHIPlERLRNS 109
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTtliKIILGLLKPDS---GEIKVLGKDIKKEP-EEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLFDG-TVRSNLDpfdrysdvqiygvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksggsn 188
Cdd:cd03230 75 IGYLPEEPSLYENlTVRENLK----------------------------------------------------------- 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
34-264 |
6.31e-25 |
|
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: 98.28 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYspHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCI 113
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 114 PQdptlfdgtvrsnldpfdrysdvqiygVLSKVGLIEecdelsliseqeqpnfsshkLRNRFIDlntvvksggsNLSQGQ 193
Cdd:cd03214 79 PQ--------------------------ALELLGLAH--------------------LADRPFN----------ELSGGE 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767157600 194 RQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03214 103 RQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
33-264 |
1.05e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.78 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI---YRLSdweNGTIIIDNKdikhiPLERLRNS 109
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlglLPPT---SGTVRLFGK-----PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQ----DP----TLFDgTVRSNLDP----FDRYSDVQ---IYGVLSKVGLIEecdelsliseqeqpnfsshkLRNR 174
Cdd:COG1121 77 IGYVPQraevDWdfpiTVRD-VVLMGRYGrrglFRRPSRADreaVDEALERVGLED--------------------LADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 175 FIdlntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY 253
Cdd:COG1121 136 PI----------GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREY 205
|
250
....*....|..
gi 767157600 254 -DKILVMEMGRV 264
Cdd:COG1121 206 fDRVLLLNRGLV 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
33-263 |
2.44e-24 |
|
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: 97.54 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSP---HSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI----YRLSdwenGTIiidnkdikhipleR 105
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgelEKLS----GSV-------------S 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTLFDGTVRSNL---DPFD--RYSDVqiygvlskvglIEEC---DELSLISEQEQpnfsshklrnrfid 177
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENIlfgKPFDeeRYEKV-----------IKACalePDLEILPDGDL-------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 178 lnTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASID-YISDAKIQKTIR-ETMKNTTILTIAHRLRSVIDYDK 255
Cdd:cd03250 119 --TEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDaHVGRHIFENCILgLLLNNKTRILVTHQLQLLPHADQ 196
|
....*...
gi 767157600 256 ILVMEMGR 263
Cdd:cd03250 197 IVVLDNGR 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
34-259 |
1.87e-23 |
|
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: 95.29 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKdikhiPLERLRNSISCI 113
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 114 PQ----DPTlFDGTVR--------SNLDPFDRYSDVQ---IYGVLSKVGLIEecdelsliseqeqpnfsshkLRNRFIdl 178
Cdd:cd03235 74 PQrrsiDRD-FPISVRdvvlmglyGHKGLFRRLSKADkakVDEALERVGLSE--------------------LADRQI-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 179 ntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKI 256
Cdd:cd03235 131 --------GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRV 202
|
...
gi 767157600 257 LVM 259
Cdd:cd03235 203 LLL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
33-263 |
5.49e-23 |
|
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: 93.41 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYspHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI--KHIPLERLRNSI 110
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDG-TVRSNLdpfdrysdvqIYGvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksggsnL 189
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI----------ALG-----------------------------------------------L 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 190 SQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHRLRSVIDY-DKILVMEMGR 263
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
33-267 |
5.61e-23 |
|
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: 94.57 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSK--ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP---LERLR 107
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDPTLFDG-TVRSNLD-PFdrysdvQIYGVlSKVGLIEECDELSliseqeqpnfsshklrnRFIDLNTVVKSG 185
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAlPL------EIAGV-PKAEIEERVLELL-----------------ELVGLEDKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 186 GSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILVMEMG 262
Cdd:cd03258 138 PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRIcDRVAVMEKG 217
|
....*
gi 767157600 263 RVKEY 267
Cdd:cd03258 218 EVVEE 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
34-264 |
1.08e-22 |
|
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: 93.65 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYSPhsSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPL-ERLRNSISC 112
Cdd:cd03224 2 EVENLNAGYGK--SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSNLdpfdrysdvqiygvlsKVGLIEECDElsliSEQEQPNfsshKLRNRFIDLNTVVKSGGSNLSQ 191
Cdd:cd03224 80 VPEGRRIFPElTVEENL----------------LLGAYARRRA----KRKARLE----RVYELFPRLKERRKQLAGTLSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATAS-----IDYISDAkIQKtIRETmkNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03224 136 GEQQMLAIARALMSRPKLLLLDEPSEGlapkiVEEIFEA-IRE-LRDE--GVTILLVEQNARFALEIaDRAYVLERGRV 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
33-264 |
1.75e-22 |
|
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: 92.97 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYspHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERlRNsISC 112
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RN-IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSNLDpfdrysdvqiYGVlskvglieecdELSLISEQEQPNfsSHKLRNRFIDLNTVVKSGGSNLSQ 191
Cdd:cd03259 77 VFQDYALFPHlTVAENIA----------FGL-----------KLRGVPKAEIRA--RVRELLELVGLEGLLNRYPHELSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767157600 192 GQRQLLCLARSMlgARN--IMLIDEATASIDYISDAKIQKTIRETMKNT--TILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03259 134 GQQQRVALARAL--AREpsLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALaDRIAVMNEGRI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
33-264 |
5.80e-22 |
|
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: 91.40 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYS--PHSSKALDNVSFKVKAGTKVGIVGRTGAGKS---SIIAAIYRLSdweNGTIIIDNKDIKHIPLERL- 106
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKStllNILGGLDRPT---SGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 ---RNSISCIPQDPTLFDG-TVRSNLD-------PFDRYSDVQIYGVLSKVGLieecdelsliseqeqpnfsSHKLrNRF 175
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVElplllagVPKKERRERAEELLERVGL-------------------GDRL-NHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 176 IdlntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY 253
Cdd:cd03255 138 P----------SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYA 207
|
250
....*....|.
gi 767157600 254 DKILVMEMGRV 264
Cdd:cd03255 208 DRIIELRDGKI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
33-275 |
7.08e-22 |
|
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: 93.58 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY--SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRL---SDWENGTIIIDNKDIKHIPLERLR 107
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 ----NSISCIPQDPTlfdgtvrSNLDPFDRYSD-----VQIYGVLSKVGLIEECDELsL----ISEQEQ-----PnfssH 169
Cdd:COG0444 82 kirgREIQMIFQDPM-------TSLNPVMTVGDqiaepLRIHGGLSKAEARERAIEL-LervgLPDPERrldryP----H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 170 KLrnrfidlntvvkSGgsnlsqGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETMK------NTTILTI 243
Cdd:COG0444 150 EL------------SG------GMRQRVMIARALALEPKLLIADEPTTAL----DVTIQAQILNLLKdlqrelGLAILFI 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767157600 244 AHRLrSVIDY--DKILVM------EMGRVKE-YD---HPYT--LIS 275
Cdd:COG0444 208 THDL-GVVAEiaDRVAVMyagrivEEGPVEElFEnprHPYTraLLS 252
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
41-264 |
9.69e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 95.16 E-value: 9.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 41 RYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLF 120
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 121 DGTVRSNLdPFDRYSDVQiygvlskvGLIEECDELSLISEqeqpnfsshklrnrfiDL-------NTVVKSGGSNLSQGQ 193
Cdd:PRK10789 402 SDTVANNI-ALGRPDATQ--------QEIEHVARLASVHD----------------DIlrlpqgyDTEVGERGVMLSGGQ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 194 RQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRV 264
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
31-260 |
1.01e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRySPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDnkdikhiPLERlrnsI 110
Cdd:COG4178 361 GALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP-------AGAR----V 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNL---DPFDRYSDVQIYGVLSKVGLieecdelsliseqeqpnfssHKLRNRFidlnTVVKSGGS 187
Cdd:COG4178 429 LFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL--------------------GHLAERL----DEEADWDQ 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767157600 188 NLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRlRSVIDY-DKILVME 260
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFhDRVLELT 557
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-299 |
1.33e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.40 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 31 GDVELKNLSLRY-SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEN--------------------- 88
Cdd:PTZ00265 1164 GKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyq 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 89 ---------------------------------GTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDGTVRSNLDPFDRYS 135
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 136 DVQIYGVLSKVGLIEECDElsliseqeqpnfsshKLRNRFidlNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEA 215
Cdd:PTZ00265 1324 TREDVKRACKFAAIDEFIE---------------SLPNKY---DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEA 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 216 TASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDYDKILVmemgrvkeYDHPytlisDRNTIFYR--------LC 285
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVV--------FNNP-----DRTGSFVQahgtheelLS 1452
|
330
....*....|....
gi 767157600 286 RQSGEFENLFELAK 299
Cdd:PTZ00265 1453 VQDGVYKKYVKLAK 1466
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
33-274 |
1.65e-20 |
|
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: 88.13 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSN--LDPfdrysdvQIYGVlSKVGLIEECDEL-SLISEQEQpnfsshKLRNRFIDlntvvksggsN 188
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVP-------KLLKW-PKEKIRERADELlALVGLDPA------EFADRYPH----------E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILVMEMGRVK 265
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLaDRIAIMKNGEIV 215
|
....*....
gi 767157600 266 EYDHPYTLI 274
Cdd:cd03295 216 QVGTPDEIL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-259 |
3.47e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKS---SIIAAIYRLSDwenGTIIIDNKDIKHI-PLERLRN 108
Cdd:COG1129 5 LEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKStlmKILSGVYQPDS---GEILLDGEPVRFRsPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 109 SISCIPQDPTLFDG-TVRSNLdpF-DRYsdVQIYGVLSKVGLIEECDELsliseqeqpnFSSHKLRnrfIDLNTVVksgg 186
Cdd:COG1129 80 GIAIIHQELNLVPNlSVAENI--FlGRE--PRRGGLIDWRAMRRRAREL----------LARLGLD---IDPDTPV---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSM-LGARniMLI-DEATASidyISDAKIQ---KTIRE-TMKNTTILTIAHRLRSVIDY-DKILVM 259
Cdd:COG1129 139 GDLSVAQQQLVEIARALsRDAR--VLIlDEPTAS---LTEREVErlfRIIRRlKAQGVAIIYISHRLDEVFEIaDRVTVL 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
33-264 |
3.79e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 84.13 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIDNKDIKHIPL-ERLRN 108
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTtfyMIVGLVKPDS---GKILLDGQDITKLPMhKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 109 SISCIPQDPTLFDG-TVRSNLDPFdrysdVQIYGVLSKvgliEECDEL-SLISEqeqpnFSSHKLRNRFidlntvvksgG 186
Cdd:cd03218 76 GIGYLPQEASIFRKlTVEENILAV-----LEIRGLSKK----EREEKLeELLEE-----FHITHLRKSK----------A 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03218 132 SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSItDRAYIIYEGKV 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
33-264 |
4.84e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.66 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIDNKDIKHIPLERLRNS 109
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQS---GEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPtlfdgtvrsnldpfdrysDVQIygvlskVGLIEECD-ELSLiseqEQPNFSSHKLRNRFIDLNTVV------ 182
Cdd:PRK13632 85 IGIIFQNP------------------DNQF------IGATVEDDiAFGL----ENKKVPPKKMKDIIDDLAKKVgmedyl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 KSGGSNLSQGQRQLLCLArSMLgARN--IMLIDEATASIDYISDAKIQKTIRETMKNT--TILTIAHRLRSVIDYDKILV 258
Cdd:PRK13632 137 DKEPQNLSGGQKQRVAIA-SVL-ALNpeIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIV 214
|
....*.
gi 767157600 259 MEMGRV 264
Cdd:PRK13632 215 FSEGKL 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
33-269 |
5.38e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.56 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP---LERLRNS 109
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQD-PTLFDGTVRSNL---------DPFDRYSDVQIygVLSKVGLieecdelsliseqeqpnfsSHKLrNRFIDln 179
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgkSRKEIRRRVRE--VLDLVGL-------------------SDKA-KALPH-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 180 tvvksggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIDyisdakiQKTIRETMK--------NTTILtIA-HRLRSV 250
Cdd:COG2884 137 --------ELSGGEQQRVAIARALVNRPELLLADEPTGNLD-------PETSWEIMElleeinrrGTTVL-IAtHDLELV 200
|
250 260
....*....|....*....|
gi 767157600 251 IDYDK-ILVMEMGRVKEYDH 269
Cdd:COG2884 201 DRMPKrVLELEDGRLVRDEA 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-276 |
3.41e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDP-TLFDGTV---------RSNLDPFDRYSDVqIYGVLSKVGLIEECDelsliseqEQPNfsshklrnrfidlntvv 182
Cdd:PRK13648 88 VFQNPdNQFVGSIvkydvafglENHAVPYDEMHRR-VSEALKQVDMLERAD--------YEPN----------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 ksggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM--KNTTILTIAHRLRSVIDYDKILVME 260
Cdd:PRK13648 142 -----ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMN 216
|
250
....*....|....*.
gi 767157600 261 MGRVKEYDHPYTLISD 276
Cdd:PRK13648 217 KGTVYKEGTPTEIFDH 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-264 |
3.48e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 79.78 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKS---SIIAAIYRLSDwenGTIIIDNKDIK-HIPLERLRN 108
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKStlmKILSGLYKPDS---GEILVDGKEVSfASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 109 SISCIPQdptlfdgtvrsnldpfdrysdvqiygvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksggsn 188
Cdd:cd03216 76 GIAMVYQ------------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASidyISDAKIQ---KTIRE-TMKNTTILTIAHRLRSVIDY-DKILVMEMGR 263
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAA---LTPAEVErlfKVIRRlRAQGVAVIFISHRLDEVFEIaDRVTVLRDGR 159
|
.
gi 767157600 264 V 264
Cdd:cd03216 160 V 160
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
33-264 |
3.59e-18 |
|
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: 81.26 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSS--KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNsI 110
Cdd:cd03266 2 ITADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDG-TVRSNLDPFDRysdvqIYGvLSKVGLIEECDELSLISEQEQpnfsshkLRNRfidlntvvKSGGsnL 189
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAG-----LYG-LKGDELTARLEELADRLGMEE-------LLDR--------RVGG--F 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 190 SQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK-NTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03266 138 STGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLcDRVVVLHRGRV 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
33-264 |
4.29e-18 |
|
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: 80.91 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP---LERLRNS 109
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLF-DGTVRSNLDPFDRYSDV-------QIYGVLSKVGLieecdelsliseqeqpnfsSHKLRnrfidlntv 181
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFALEVTGVppreirkRVPAALELVGL-------------------SHKHR--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 182 vkSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK-NTTILTIAHRLRSVIDYDK-ILVM 259
Cdd:cd03292 132 --ALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIAL 209
|
....*
gi 767157600 260 EMGRV 264
Cdd:cd03292 210 ERGKL 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
33-264 |
7.27e-18 |
|
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: 80.62 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI---KHIPLERLRNS 109
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLFDG-TVRSNLDPFDRYsdvqiYGVLSKvgliEECDELSLiseqeqpnfssHKLrnRFIDLNTVVKSGGSN 188
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPLRE-----HTRLSE----EEIREIVL-----------EKL--EAVGLRGAEDLYPAE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRET--MKNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIaDRIAVLYDGKI 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
34-264 |
7.66e-18 |
|
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: 80.56 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSdweNGTIIIDNKDIKHI-PLERLRNS 109
Cdd:cd03219 2 EVRGLTKRFGGL--VALDDVSFSVRPGEIHGLIGPNGAGKTTlfnLISGFLRPT---SGSVLFDGEDITGLpPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLFDG-TVRSNLD---------------PFDRYSDV--QIYGVLSKVGLIEECDELSliseqeqpnfsshkl 171
Cdd:cd03219 77 IGRTFQIPRLFPElTVLENVMvaaqartgsglllarARREEREAreRAEELLERVGLADLADRPA--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 172 rnrfidlntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASidyISDAKIQKTIR--ETMK--NTTILTIAHRL 247
Cdd:cd03219 142 ---------------GELSYGQQRRLEIARALATDPKLLLLDEPAAG---LNPEETEELAEliRELRerGITVLLVEHDM 203
|
250
....*....|....*...
gi 767157600 248 RSVIDY-DKILVMEMGRV 264
Cdd:cd03219 204 DVVMSLaDRVTVLDQGRV 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-266 |
1.10e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.21 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDnkdikHIPLER-----LR 107
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-----GMVLSEetvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDP-TLFDG-TVRsnldpfdrySDVqIYGvLSKVG-----LIEECDE-LSLISEQEqpnFSSHKlrnrfidln 179
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGaTVQ---------DDV-AFG-LENIGvpreeMVERVDQaLRQVGMED---FLNRE--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 180 tvvksgGSNLSQGQRQLLCLArSMLGAR-NIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHRLRSVIDYDKI 256
Cdd:PRK13635 138 ------PHRLSGGQKQRVAIA-GVLALQpDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRV 210
|
250
....*....|
gi 767157600 257 LVMEMGRVKE 266
Cdd:PRK13635 211 IVMNKGEILE 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-292 |
2.46e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.72 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 3 SVERIKEYtdIPSESNGYISPPANWPQTGDVELKNLSLRYSPHSSK-ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIY 81
Cdd:PLN03232 587 SLQRIEEL--LLSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 82 -RLSDWENGTIIIdnkdikhiplerlRNSISCIPQDPTLFDGTVRSNLDPFDRYSDVQIYGVLSKVGLIEECDElslise 160
Cdd:PLN03232 665 gELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDL------ 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 161 qeqpnFSSHKLrnrfidlnTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASID-YISDAKIQKTIRETMKNTT 239
Cdd:PLN03232 726 -----LPGRDL--------TEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDaHVAHQVFDSCMKDELKGKT 792
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767157600 240 ILTIAHRLRSVIDYDKILVMEMGRVKEyDHPYTLISDRNTIFYRLCRQSGEFE 292
Cdd:PLN03232 793 RVLVTNQLHFLPLMDRIILVSEGMIKE-EGTFAELSKSGSLFKKLMENAGKMD 844
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
33-264 |
2.97e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.09 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY---SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI--KHIPLERLR 107
Cdd:PRK13637 3 IKIENLTHIYmegTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDP--TLFDGTVrsnldpfdrYSDVQiYGvLSKVGLieecdelsliSEQEQPNFSSHKLRNRFIDLNTVVKSG 185
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETI---------EKDIA-FG-PINLGL----------SEEEIENRVKRAMNIVGLDYEDYKDKS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 186 GSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILVMEMG 262
Cdd:PRK13637 142 PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKG 221
|
..
gi 767157600 263 RV 264
Cdd:PRK13637 222 KC 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
36-276 |
3.63e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 36 KNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPL-ERLRNSISCIP 114
Cdd:PRK10895 7 KNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 115 QDPTLFdgtvrSNLDPFDRYsdvqiygvlskVGLIEECDELSliseQEQPNFSSHKLRNRFiDLNTVVKSGGSNLSQGQR 194
Cdd:PRK10895 85 QEASIF-----RRLSVYDNL-----------MAVLQIRDDLS----AEQREDRANELMEEF-HIEHLRDSMGQSLSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 195 QLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIrETMKNT--TILTIAHRLRSVIDY-DKILVMEMGRVKEYDHPY 271
Cdd:PRK10895 144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPT 222
|
....*
gi 767157600 272 TLISD 276
Cdd:PRK10895 223 EILQD 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-278 |
3.92e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.87 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSS---KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIK----HIPLER 105
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDP--TLFDGTVrsnldpfdrYSDVQiYGVLSkVGlieecdelslISEQEQPNFSSHKLRNRFIDLNTVVK 183
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTV---------LKDVE-FGPKN-FG----------FSEDEAKEKALKWLKKVGLSEDLISK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 SgGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK-NTTILTIAHRLRSVIDY-DKILVMEM 261
Cdd:PRK13641 142 S-PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEYaDDVLVLEH 220
|
250
....*....|....*..
gi 767157600 262 GRVKEYDHPYTLISDRN 278
Cdd:PRK13641 221 GKLIKHASPKEIFSDKE 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-264 |
4.39e-17 |
|
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: 77.59 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSL----RYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI--YRLSDWENGTIIIDNKDIkhiPLERL 106
Cdd:cd03213 4 LSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 RNSISCIPQD----PTLfdgTVRSNLDpfdrysdvqiygvlskvglieecdelsliseqeqpnFSShKLRNrfidlntvv 182
Cdd:cd03213 81 RKIIGYVPQDdilhPTL---TVRETLM------------------------------------FAA-KLRG--------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 ksggsnLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK-NTTILTIAHRLRSVI--DYDKILVM 259
Cdd:cd03213 112 ------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLL 185
|
....*
gi 767157600 260 EMGRV 264
Cdd:cd03213 186 SQGRV 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-250 |
5.91e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.93 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEN-----GTIIIDNKDI--KHIPLER 105
Cdd:PRK14258 8 IKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTLFDGTVRSNLdpfdRYSdVQIYGVLSKVglieECDEL--SLISEQEQPNFSSHKLRNRFIDLntvvk 183
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNV----AYG-VKIVGWRPKL----EIDDIveSALKDADLWDEIKHKIHKSALDL----- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 184 sggsnlSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNT--TILTIAHRLRSV 250
Cdd:PRK14258 152 ------SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQV 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
33-278 |
8.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.62 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSK-ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSIS 111
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPtlfdgtvrsnldpfdrysDVQIygvlskVGLIEECD-----ELSLISEQEQPNFSSHKLrnRFIDLNTVVKSGG 186
Cdd:PRK13650 85 MVFQNP------------------DNQF------VGATVEDDvafglENKGIPHEEMKERVNEAL--ELVGMQDFKEREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDYDKILVMEMGRV 264
Cdd:PRK13650 139 ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
250
....*....|....
gi 767157600 265 KEYDHPYTLISDRN 278
Cdd:PRK13650 219 ESTSTPRELFSRGN 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
33-233 |
8.75e-17 |
|
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: 77.13 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYspHSSKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIDNKDIkHIPLERLRNS 109
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLPPSA---GEVLWNGEPI-RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLFDG-TVRSNLDpF------DRYSDVQIYGVLSKVGLieecdelsliseqeqpnfssHKLRNRFIdlntvv 182
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGL--------------------AGLADLPV------ 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767157600 183 ksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE 233
Cdd:COG4133 130 ----RQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
33-266 |
1.21e-16 |
|
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: 77.13 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSS--KALDNVSFKVKAGTKVGIVGRTGAGKS---SIIAAIYRLSDwenGTIIIDNKdikhiPLERLR 107
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKStllRIIAGLERPTS---GEVLVDGE-----PVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDPTLFD-GTVRSN---------LDPFDRYSDVQIYgvLSKVGLieecdelsliSEQEqpnfsshklrNRFId 177
Cdd:cd03293 73 PDRGYVFQQDALLPwLTVLDNvalglelqgVPKAEARERAEEL--LELVGL----------SGFE----------NAYP- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 178 lntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQ----KTIRETmkNTTILTIAHRLRSVIdY 253
Cdd:cd03293 130 ---------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQeellDIWRET--GKTVLLVTHDIDEAV-F 197
|
250
....*....|....*..
gi 767157600 254 --DKILVMEM--GRVKE 266
Cdd:cd03293 198 laDRVVVLSArpGRIVA 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
50-262 |
1.97e-16 |
|
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: 76.60 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 50 LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLE----RLRNSISCIPQDPTLFDGTVR 125
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 126 SNL---DPFD--RYSDVqiygvlskvglIEECdelSLiseqeQPNfsshklrnrfIDL-----NTVVKSGGSNLSQGQRQ 195
Cdd:cd03290 97 ENItfgSPFNkqRYKAV-----------TDAC---SL-----QPD----------IDLlpfgdQTEIGERGINLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 196 LLCLARSMLGARNIMLIDEATASID-YISDAKIQKTIRETMKNT--TILTIAHRLRSVIDYDKILVMEMG 262
Cdd:cd03290 148 RICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDkrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
33-264 |
2.04e-16 |
|
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: 76.41 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI--KHIPLERLRNSI 110
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDG-TVRSNLdpfdRYSDVQIYGV------------LSKVGLIEECDELsliseqeqPnfsshklrnrfid 177
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENI----TLAPIKVKGMskaeaeeralelLEKVGLADKADAY--------P------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 178 lntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDyisdakiQKTIRE---TMKN-----TTILTIAHRL-- 247
Cdd:cd03262 134 ---------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD-------PELVGEvldVMKDlaeegMTMVVVTHEMgf 197
|
250
....*....|....*...
gi 767157600 248 -RSVIdyDKILVMEMGRV 264
Cdd:cd03262 198 aREVA--DRVIFMDDGRI 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
33-264 |
2.26e-16 |
|
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: 76.25 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLErLRNSISC 112
Cdd:cd03265 1 IEVENLVKKYG--DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSNLDPFDRysdvqIYGVLSKVgLIEECDELSliseqeqpnfsshklrnRFIDLNTVVKSGGSNLSQ 191
Cdd:cd03265 78 VFQDLSVDDElTGWENLYIHAR-----LYGVPGAE-RRERIDELL-----------------DFVGLLEAADRLVKTYSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03265 135 GMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRI 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
33-272 |
2.63e-16 |
|
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: 76.61 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERlRNsISC 112
Cdd:cd03296 3 IEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSNLdpfdrysdvqIYGvlskvglieecdeLSLISEQEQPnfSSHKLRNRFIDLNTVVKSGG----- 186
Cdd:cd03296 79 VFQHYALFRHmTVFDNV----------AFG-------------LRVKPRSERP--PEAEIRAKVHELLKLVQLDWladry 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 -SNLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIR-------ETMKNTTILtIAHRLRSVIDY-DKIL 257
Cdd:cd03296 134 pAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL----DAKVRKELRrwlrrlhDELHVTTVF-VTHDQEEALEVaDRVV 208
|
250 260
....*....|....*....|..
gi 767157600 258 VMEMGRVKE-------YDHPYT 272
Cdd:cd03296 209 VMNKGRIEQvgtpdevYDHPAS 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-264 |
7.60e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKS---SIIAAIYRLSDwenGTIIIDNK--DIKHiPLERLR 107
Cdd:COG3845 6 LELRGITKRFGGV--VANDDVSLTVRPGEIHALLGENGAGKStlmKILYGLYQPDS---GEILIDGKpvRIRS-PRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDPTLFDG-TVRSNL----DPFDRysdvqiyGVLSKVGLIEECDELSliseqEQPNFSshklrnrfIDLNTVV 182
Cdd:COG3845 80 LGIGMVHQHFMLVPNlTVAENIvlglEPTKG-------GRLDRKAARARIRELS-----ERYGLD--------VDPDAKV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 ksggSNLSQGQRQ----LLCLARsmlGARnIMLIDEATAsidYISDAKIQ---KTIREtMKN--TTILTIAHRLRSVIDY 253
Cdd:COG3845 140 ----EDLSVGEQQrveiLKALYR---GAR-ILILDEPTA---VLTPQEADelfEILRR-LAAegKSIIFITHKLREVMAI 207
|
250
....*....|..
gi 767157600 254 -DKILVMEMGRV 264
Cdd:COG3845 208 aDRVTVLRRGKV 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
48-275 |
9.09e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.31 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP---LERLRNSISCIPQDPtlfdgtv 124
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 125 RSNLDPFDRYSDV-----QIYGVLSKVGLIEECDELsliseqeqpnfsshklrnrfidLNTVvksgGSN----------L 189
Cdd:COG4608 105 YASLNPRMTVGDIiaeplRIHGLASKAERRERVAEL----------------------LELV----GLRpehadrypheF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 190 SQGQRQLLCLARS-MLGARNIMLiDEATASIDYiSdakIQKTI-------RETMkNTTILTIAHRLrSVIDY--DKILVM 259
Cdd:COG4608 159 SGGQRQRIGIARAlALNPKLIVC-DEPVSALDV-S---IQAQVlnlledlQDEL-GLTYLFISHDL-SVVRHisDRVAVM 231
|
250 260
....*....|....*....|....*...
gi 767157600 260 EMGRVKE-------YD---HPYT--LIS 275
Cdd:COG4608 232 YLGKIVEiaprdelYArplHPYTqaLLS 259
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
33-275 |
1.17e-15 |
|
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: 74.68 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSskaLDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERlRNsISC 112
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-RD-ISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLF-DGTVRSNLDpfdrysdvqiYGV----LSKVGLIEECDELSliseqeqpnfsshklrnRFIDLNTVVKSGGS 187
Cdd:cd03299 76 VPQNYALFpHMTVYKNIA----------YGLkkrkVDKKEIERKVLEIA-----------------EMLGIDHLLNRKPE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 188 NLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETMK------NTTILTIAHRLRSV-IDYDKILVME 260
Cdd:cd03299 129 TLSGGEQQRVAIARALVVNPKILLLDEPFSAL----DVRTKEKLREELKkirkefGVTVLHVTHDFEEAwALADKVAIML 204
|
250
....*....|....*
gi 767157600 261 MGRVKEYDHPYTLIS 275
Cdd:cd03299 205 NGKLIQVGKPEEVFK 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-264 |
1.40e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYsPHSSKALDnvsFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHI-PLERlrnSISC 112
Cdd:COG3840 3 RLDDLTYRY-GDFPLRFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALpPAER---PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSN----LDPFDRYSDVQ---IYGVLSKVGLiEECdelslisEQEQPnfsshklrnrfidlntvvks 184
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGL-AGL-------LDRLP-------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 185 ggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDyisDAK-------IQKTIRETmkNTTILTIAHRLRSVIDY-DKI 256
Cdd:COG3840 128 --GQLSGGQRQRVALARCLVRKRPILLLDEPFSALD---PALrqemldlVDELCRER--GLTVLMVTHDPEDAARIaDRV 200
|
....*...
gi 767157600 257 LVMEMGRV 264
Cdd:COG3840 201 LLVADGRI 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
33-265 |
1.95e-15 |
|
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: 73.38 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTkVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLErLRNSISC 112
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSNLDPF-------DRYSDVQIYGVLSKVGLIEECDELsliseqeqpnfsshklrnrfidlntvVKS 184
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYIawlkgipSKEVKARVDEVLELVNLGDRAKKK--------------------------IGS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 185 ggsnLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSVID-YDKILVMEMGR 263
Cdd:cd03264 131 ----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGK 206
|
..
gi 767157600 264 VK 265
Cdd:cd03264 207 LV 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
48-272 |
5.10e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 75.11 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEnGTIIIDNKDI---KHIPLERLRNSISCIPQDPtlFdgtv 124
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLdglSRRALRPLRRRMQVVFQDP--F---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 125 rSNLDPfdRYSDVQIYG---------------------VLSKVGLIEECdelsliseqeqpnfsshklRNRFIdlntvvk 183
Cdd:COG4172 373 -GSLSP--RMTVGQIIAeglrvhgpglsaaerrarvaeALEEVGLDPAA-------------------RHRYP------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 sggSNLSQGQRQLLCLARSM-LGARNIMLiDEATASIdyisDAKIQKTIRETMK------NTTILTIAHRLRsVIDY--D 254
Cdd:COG4172 424 ---HEFSGGQRQRIAIARALiLEPKLLVL-DEPTSAL----DVSVQAQILDLLRdlqrehGLAYLFISHDLA-VVRAlaH 494
|
250 260
....*....|....*....|....*...
gi 767157600 255 KILVMEMGRVKEY----------DHPYT 272
Cdd:COG4172 495 RVMVMKDGKVVEQgpteqvfdapQHPYT 522
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-266 |
2.02e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.48 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWE-----NGTIIIDNKDIKHIPLERLR 107
Cdd:PRK14247 4 IEIRDLKVSFG--QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDP------TLFDGT---------VRSNLDPFDRysdvqIYGVLSKVGLIEEcdelsliseqeqpnfsshkLR 172
Cdd:PRK14247 82 RRVQMVFQIPnpipnlSIFENValglklnrlVKSKKELQER-----VRWALEKAQLWDE-------------------VK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 173 NRfidlntvVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAH---RLRS 249
Cdd:PRK14247 138 DR-------LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAAR 210
|
250 260
....*....|....*....|.
gi 767157600 250 VIDYDKIL----VMEMGRVKE 266
Cdd:PRK14247 211 ISDYVAFLykgqIVEWGPTRE 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-262 |
2.83e-14 |
|
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: 73.41 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 42 YSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYrlsdwenGTIIIDNKDIKHiplerlRNSISCIPQDPTLFD 121
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------GELEPSEGKIKH------SGRISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 122 GTVRSNLD---PFDRYSdvqiYGVLSKVGLIEEcdELSLISEQEqpnfsshklrnrfidlNTVVKSGGSNLSQGQRQLLC 198
Cdd:TIGR01271 501 GTIKDNIIfglSYDEYR----YTSVIKACQLEE--DIALFPEKD----------------KTVLGEGGITLSGGQRARIS 558
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 199 LARSMLGARNIMLIDEATASIDYISDAKI-QKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMG 262
Cdd:TIGR01271 559 LARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
34-273 |
2.88e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYSPHSS--KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDwENGTI----IIDNKDIKHIP---LE 104
Cdd:PRK09473 14 DVKDLRVTFSTPDGdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREILNLPekeLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 105 RLR-NSISCIPQDPTlfdgtvrSNLDPFDRYSDvQIYGVL------SKVGLIEEC----DELSLISEQEQPNFSSHKLrn 173
Cdd:PRK09473 93 KLRaEQISMIFQDPM-------TSLNPYMRVGE-QLMEVLmlhkgmSKAEAFEESvrmlDAVKMPEARKRMKMYPHEF-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 174 rfidlntvvksggsnlSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVI 251
Cdd:PRK09473 163 ----------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVA 226
|
250 260 270
....*....|....*....|....*....|...
gi 767157600 252 DY-DKILVMEMGRVKEY----------DHPYTL 273
Cdd:PRK09473 227 GIcDKVLVMYAGRTMEYgnardvfyqpSHPYSI 259
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-264 |
3.88e-14 |
|
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: 69.38 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRysphssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKH-IPLERLRNSIS 111
Cdd:cd03215 5 LEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPtlfdgtvrsnldpfdrysdvqiygvlSKVGLIeecdelsliseqeqPNFSshklrnrfIDLNTVVksgGSNLSQ 191
Cdd:cd03215 79 YVPEDR--------------------------KREGLV--------------LDLS--------VAENIAL---SSLLSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRElADAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
33-276 |
4.97e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP-LERLRNSIS 111
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDP-TLFDG-TVRSNLdpfdrysdvqIYGVlskvglieecDELSLiseqeqPNFSSHKLRNRF---IDLNTVVKSGG 186
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL----------AFGP----------ENLCL------PPIEIRKRVDRAlaeIGLEKYRHRSP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM-KNTTILTIAHRLRSVIDYDKILVMEMGRVK 265
Cdd:PRK13644 135 KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
250
....*....|.
gi 767157600 266 EYDHPYTLISD 276
Cdd:PRK13644 215 LEGEPENVLSD 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
33-248 |
5.58e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.19 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWE-----NGTIIIDNKDI--KHIPLER 105
Cdd:PRK14239 6 LQVSDLSVYYN--KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTLFdgtvrsnldPFDRYSDV----QIYGVLSKvGLIEECDELSLISEQeqpnfSSHKLRNRFIDlntv 181
Cdd:PRK14239 84 LRKEIGMVFQQPNPF---------PMSIYENVvyglRLKGIKDK-QVLDEAVEKSLKGAS-----IWDEVKDRLHD---- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 182 vksGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLR 248
Cdd:PRK14239 145 ---SALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
50-296 |
6.21e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.46 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 50 LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIY-RLSDWENGTIIIdnkdikhiplerlRNSISCIPQDPTLFDGTVRSNL 128
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLgELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 129 ---DPFD--RYSD-VQIYGVLSKVGLIEECDeLSLISEQeqpnfsshklrnrfidlntvvksgGSNLSQGQRQLLCLARS 202
Cdd:PLN03130 700 lfgSPFDpeRYERaIDVTALQHDLDLLPGGD-LTEIGER------------------------GVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 203 MLGARNIMLIDEATASID-YISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVKEyDHPYTLISDRNTIF 281
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDaHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE-EGTYEELSNNGPLF 833
|
250
....*....|....*
gi 767157600 282 YRLCRQSGEFENLFE 296
Cdd:PLN03130 834 QKLMENAGKMEEYVE 848
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
33-268 |
6.87e-14 |
|
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: 69.48 E-value: 6.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY----SPHSSK----------------ALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSdweNG 89
Cdd:cd03220 1 IELENVSKSYptykGGSSSLkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTllrLLAGIYPPD---SG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 90 TIIIDNKdikhiplerlrnsISCIPQ-----DPTLfdgTVRSNLdpfdrYSDVQIYGVLSKV--GLIEECDELSLISEqe 162
Cdd:cd03220 78 TVTVRGR-------------VSSLLGlgggfNPEL---TGRENI-----YLNGRLLGLSRKEidEKIDEIIEFSELGD-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 163 qpnfsshklrnrFIDLNtvVKsggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILT 242
Cdd:cd03220 135 ------------FIDLP--VK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVI 196
|
250 260
....*....|....*....|....*...
gi 767157600 243 IA-HRLRSVIDY-DKILVMEMGRVKEYD 268
Cdd:cd03220 197 LVsHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
33-270 |
8.37e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:PRK09536 4 IDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTL-FDGTVRSNLDpFDRYSDvqiygvLSKVGLIEECDELSLISEQEQPNFSshklrnRFIDLNTvvksggSNLSQ 191
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVE-MGRTPH------RSRFDTWTETDRAAVERAMERTGVA------QFADRPV------TSLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-TTILTIAHRLRSVIDY-DKILVMEMGRVKEYDH 269
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYcDELVLLADGRVRAAGP 222
|
.
gi 767157600 270 P 270
Cdd:PRK09536 223 P 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
33-266 |
8.47e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSK--ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP---LERLR 107
Cdd:PRK11153 2 IELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQ------DPTLFD---------GTVRSNLDPfdrysdvQIYGVLSKVGLieecdelsliseqeqpnfsSHKlR 172
Cdd:PRK11153 82 RQIGMIFQhfnllsSRTVFDnvalplelaGTPKAEIKA-------RVTELLELVGL-------------------SDK-A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 173 NRFidlntvvksgGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLrSV 250
Cdd:PRK11153 135 DRY----------PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEM-DV 203
|
250
....*....|....*...
gi 767157600 251 IDY--DKILVMEMGRVKE 266
Cdd:PRK11153 204 VKRicDRVAVIDAGRLVE 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
33-266 |
1.20e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.11 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSK--ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLsdwE---NGTIIIDNKDIKHIPLERLR 107
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL---ErptSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 N---SISCIPQDPTLFDG-TVRSN---------LDPFDRysDVQIYGVLSKVGLieecdelsliseqeqpnfsSHKlRNR 174
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENvalpleiagVPKAEI--RKRVAELLELVGL-------------------SDK-ADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 175 FIdlntvvksggSNLSQGQRQLLCLARSMlgARN--IMLIDEATASIDyisdakiQKT----------IRETMkNTTILT 242
Cdd:COG1135 137 YP----------SQLSGGQKQRVGIARAL--ANNpkVLLCDEATSALD-------PETtrsildllkdINREL-GLTIVL 196
|
250 260
....*....|....*....|....*.
gi 767157600 243 IAHRLrSVIDY--DKILVMEMGRVKE 266
Cdd:COG1135 197 ITHEM-DVVRRicDRVAVLENGRIVE 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
42-269 |
4.17e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 42 YSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFD 121
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 122 GTVRSNLD-PFdrysdvQIYGvlskvglieecdelslisEQEQPNFSSHKLrNRFIDLNTVVKSGGSNLSQGQRQLLCLA 200
Cdd:PRK10247 95 DTVYDNLIfPW------QIRN------------------QQPDPAIFLDDL-ERFALPDTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767157600 201 RSMLGARNIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHRLRSVIDYDKILVME--MGRVKEYDH 269
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITLQphAGEMQEARY 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
32-264 |
6.89e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.35 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 32 DVELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSIS 111
Cdd:PRK11231 2 TLRTENLTVGYG--TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPTLFDG-TVRsNLDPFDRYSDVQIYGVLSkvglieECDELSLISEQEQPNFSShkLRNRFIdlntvvksggSNLS 190
Cdd:PRK11231 80 LLPQHHLTPEGiTVR-ELVAYGRSPWLSLWGRLS------AEDNARVNQAMEQTRINH--LADRRL----------TDLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 191 QGQRQLLCLArsMLGARN--IMLIDEATASIDYISDAKIQKTIREtMKNT--TILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:PRK11231 141 GGQRQRAFLA--MVLAQDtpVVLLDEPTTYLDINHQVELMRLMRE-LNTQgkTVVTVLHDLNQASRYcDHLVVLANGHV 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-246 |
7.05e-13 |
|
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: 65.25 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLrYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIiidnkdikHIPlerLRNSISC 112
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMP---EGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGTVRSNLD-PFDrysdvqiygvlskvglieecDELSLiseqeqpnfsshklrnrfidlntvvksggsnlsq 191
Cdd:cd03223 69 LPQRPYLPLGTLREQLIyPWD--------------------DVLSG---------------------------------- 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIREtmKNTTILTIAHR 246
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-253 |
9.40e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 37 NLSLRYSPHSSKA-LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNK------DIKHIPLERLRNS 109
Cdd:PRK14246 12 NISRLYLYINDKAiLKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPtlfdgtvrsnlDPFDRYSDVQIYGVLSKVGLIEECDELSLISEQEQPNFSSHKlrnrfiDLNTVVKSGGSNL 189
Cdd:PRK14246 92 VGMVFQQP-----------NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWK------EVYDRLNSPASQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 190 SQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAH---RLRSVIDY 253
Cdd:PRK14246 155 SGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-276 |
9.66e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.13 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSI---IAAIYRLSDWENGTIIIDNKDIKHIPLERLRNS 109
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPtlfdgtvrsnldpfdrysDVQIYGvlSKVGlieecDELSLISEQEQ-PNFSSHKLRNRF---IDLNTVVKSG 185
Cdd:PRK13640 86 VGIVFQNP------------------DNQFVG--ATVG-----DDVAFGLENRAvPRPEMIKIVRDVladVGMLDYIDSE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 186 GSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM--KNTTILTIAHRLRSVIDYDKILVMEMGR 263
Cdd:PRK13640 141 PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGK 220
|
250
....*....|...
gi 767157600 264 VKEYDHPYTLISD 276
Cdd:PRK13640 221 LLAQGSPVEIFSK 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-264 |
1.67e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 28 PQTGDV--ELKNLSLRysphssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNK--DIKHiPL 103
Cdd:COG1129 250 AAPGEVvlEVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRS-PR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 104 ERLRNSISCIPQDPT---LF-DGTVRSN--LDPFDRYSDvqiYGVLSKVGLIEECDELsliseqeqpnfsSHKLRNRFID 177
Cdd:COG1129 323 DAIRAGIAYVPEDRKgegLVlDLSIRENitLASLDRLSR---GGLLDRRRERALAEEY------------IKRLRIKTPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 178 LNTVVksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDyISdAK--IQKTIRE-TMKNTTI----------LTIA 244
Cdd:COG1129 388 PEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VG-AKaeIYRLIRElAAEGKAVivisselpelLGLS 461
|
250 260
....*....|....*....|
gi 767157600 245 HRlrsvidydkILVMEMGRV 264
Cdd:COG1129 462 DR---------ILVMREGRI 472
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
33-268 |
1.95e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEN-----GTIIIDNKDI--KHIPLER 105
Cdd:PRK14243 11 LRTENLNVYYG--SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTLFDGTVRSNLdpfdrysdvqIYG--VLSKVGLIEECDELSLiseqeqpnfsshKLRNRFIDLNTVVK 183
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNI----------AYGarINGYKGDMDELVERSL------------RQAALWDEVKDKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 SGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRS---VIDYDKILVME 260
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMTAFFNVE 226
|
250
....*....|....*
gi 767157600 261 -------MGRVKEYD 268
Cdd:PRK14243 227 ltegggrYGYLVEFD 241
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
42-262 |
4.30e-12 |
|
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: 65.26 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 42 YSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYrlsdwenGTIIIDNKDIKHiplerlRNSISCIPQDPTLFD 121
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL-------GELEPSEGKIKH------SGRISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 122 GTVRSNL---DPFDRYSdvqiYGVLSKVGLIEEcdELSLISEQEqpnfsshklrnrfidlNTVVKSGGSNLSQGQRQLLC 198
Cdd:cd03291 112 GTIKENIifgVSYDEYR----YKSVVKACQLEE--DITKFPEKD----------------NTVLGEGGITLSGGQRARIS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 199 LARSMLGARNIMLIDEATASIDYISDAKI-QKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMG 262
Cdd:cd03291 170 LARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
33-265 |
4.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY----SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDN---KDIKHipLER 105
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEEN--LWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPtlfdgtvrsnldpfdrysDVQIygvlskVGLIEECDelsLISEQEQPNFSSHKLRNRF------IDLN 179
Cdd:PRK13633 83 IRNKAGMVFQNP------------------DNQI------VATIVEED---VAFGPENLGIPPEEIRERVdeslkkVGMY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 180 TVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNT--TILTIAHRLRSVIDYDKIL 257
Cdd:PRK13633 136 EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRII 215
|
....*...
gi 767157600 258 VMEMGRVK 265
Cdd:PRK13633 216 VMDSGKVV 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-276 |
7.18e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 30 TGDVELKNLSLRYS---PHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDN-------KDIK 99
Cdd:PRK13645 4 SKDIILDNVSYTYAkktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 100 HIplERLRNSISCIPQDP--TLFDGTVRSNL--DPFDRYSDVQ-IYGVLSKVglieecdeLSLISEQEQpnfsshklrnr 174
Cdd:PRK13645 84 EV--KRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQeAYKKVPEL--------LKLVQLPED----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 175 fidlntVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN--TTILTIAHRLRSVID 252
Cdd:PRK13645 143 ------YVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLR 216
|
250 260
....*....|....*....|....*
gi 767157600 253 Y-DKILVMEMGRVKEYDHPYTLISD 276
Cdd:PRK13645 217 IaDEVIVMHEGKVISIGSPFEIFSN 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
34-272 |
7.72e-12 |
|
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: 65.48 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRY--SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRL----SDWENGTIIIDNKDIKHIPLERLR 107
Cdd:COG4172 8 SVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 ----NSISCIPQDPTlfdgtvrSNLDPFDRYSDvQIYGVL------SKVGLIEECDELsL----ISEQEQPnFSS--HKL 171
Cdd:COG4172 88 rirgNRIAMIFQEPM-------TSLNPLHTIGK-QIAEVLrlhrglSGAAARARALEL-LervgIPDPERR-LDAypHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 172 rnrfidlntvvkSGgsnlsqGQRQllclaRSM----LGARNIMLI-DEATASIdyisDAKIQKTIRETMK------NTTI 240
Cdd:COG4172 158 ------------SG------GQRQ-----RVMiamaLANEPDLLIaDEPTTAL----DVTVQAQILDLLKdlqrelGMAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767157600 241 LTIAHRLRSVIDY-DKILVMEMGRVKEY----------DHPYT 272
Cdd:COG4172 211 LLITHDLGVVRRFaDRVAVMRQGEIVEQgptaelfaapQHPYT 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
49-272 |
9.66e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP---LERLRNSISCIPQDPTlfdgtvr 125
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 126 SNLDPFDRYSD-----VQIYG-------------VLSKVGLIEEcdelsliseqeqpnfssHKLRNRfidlntvvksggS 187
Cdd:PRK10261 412 ASLDPRQTVGDsimepLRVHGllpgkaaaarvawLLERVGLLPE-----------------HAWRYP------------H 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 188 NLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTI--LTIAHRLRSV--IDYdKILVMEMGR 263
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVerISH-RVAVMYLGQ 541
|
250
....*....|....*....
gi 767157600 264 VKEY----------DHPYT 272
Cdd:PRK10261 542 IVEIgprravfenpQHPYT 560
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-265 |
1.09e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 29 QTGDV--ELKNLSLrYSPHSS--KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIY-----RlsdWEnGTIIIDNKDIK 99
Cdd:PRK13549 254 TIGEVilEVRNLTA-WDPVNPhiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgaypgR---WE-GEIFIDGKPVK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 100 -HIPLERLRNSISCIPQDptlfdgtvRSnldpfdRYSDVQIYGV-----------LSKVGLIEECDELSLISEQEQpnfs 167
Cdd:PRK13549 329 iRNPQQAIAQGIAMVPED--------RK------RDGIVPVMGVgknitlaaldrFTGGSRIDDAAELKTILESIQ---- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 168 shKLRnrfidlntvVKSGG-----SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-TTIL 241
Cdd:PRK13549 391 --RLK---------VKTASpelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQgVAII 459
|
250 260
....*....|....*....|....*
gi 767157600 242 TIAHRLRSVIDY-DKILVMEMGRVK 265
Cdd:PRK13549 460 VISSELPEVLGLsDRVLVMHEGKLK 484
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
33-275 |
1.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSS-KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSIS 111
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPtlfdgtvrsnldpfdrysDVQIYGVLSKVGLIEECDELSLISEQEQPNFSSHKLRNRFIDLNTvvkSGGSNLSQ 191
Cdd:PRK13642 85 MVFQNP------------------DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKT---REPARLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDYDKILVMEMGRVKEYDH 269
Cdd:PRK13642 144 GQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
....*.
gi 767157600 270 PYTLIS 275
Cdd:PRK13642 224 PSELFA 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
48-263 |
1.13e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDWEnGTIIIDNKDIK--HIPlERLRNSISCIPQDPTLFDG 122
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTlmkVLSGVYPHGTYE-GEIIFEGEELQasNIR-DTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 123 -TVRSN------LDPFDRYSDVQIYgvlskvgliEECDELsliseqeqpnfsshkLRNRFIDLNTVVKSGgsNLSQGQRQ 195
Cdd:PRK13549 97 lSVLENiflgneITPGGIMDYDAMY---------LRAQKL---------------LAQLKLDINPATPVG--NLGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 196 LLCLARSMLGARNIMLIDEATASIDYiSDAKIQKTIRETMKN--TTILTIAHRLRSVIDY-DKILVMEMGR 263
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTE-SETAVLLDIIRDLKAhgIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
33-280 |
1.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.71 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNK--DIKHIPLERLRNSI 110
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDP--TLFDGTVrsnldpfdrYSDVQiYGVLSkVGLIEecDELSLISEQEQPNFSSHKLRNRFIDLntvvksggsn 188
Cdd:PRK13636 85 GMVFQDPdnQLFSASV---------YQDVS-FGAVN-LKLPE--DEVRKRVDNALKRTGIEHLKDKPTHC---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILVMEMGRVK 265
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYcDNVFVMKEGRVI 221
|
250
....*....|....*
gi 767157600 266 EYDHPYTLISDRNTI 280
Cdd:PRK13636 222 LQGNPKEVFAEKEML 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-286 |
1.41e-11 |
|
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: 65.35 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIiidnkdikhipleRLRNSISC 112
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGTVRSN------LDPfDRYSDVqiygvlskvglIEEC---DELSLISEQEQpnfsshklrnrfidlnTVVK 183
Cdd:TIGR00957 704 VPQQAWIQNDSLRENilfgkaLNE-KYYQQV-----------LEACallPDLEILPSGDR----------------TEIG 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 SGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRE-------TMKNTTILTIAHRLRSVIDYDKI 256
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV----DAHVGKHIFEhvigpegVLKNKTRILVTHGISYLPQVDVI 831
|
250 260 270
....*....|....*....|....*....|
gi 767157600 257 LVMEMGRVKEYDhPYTLISDRNTIFYRLCR 286
Cdd:TIGR00957 832 IVMSGGKISEMG-SYQELLQRDGAFAEFLR 860
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
33-267 |
1.76e-11 |
|
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: 62.30 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPlerlRNSISC 112
Cdd:cd03269 1 LEVENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLF-DGTVRSNLDPFDRYSDV-------QIYGVLSKVGLIEecdelsliseqeqpnfsshkLRNRFIDlntvvks 184
Cdd:cd03269 75 LPEERGLYpKMKVIDQLVYLAQLKGLkkeearrRIDEWLERLELSE--------------------YANKRVE------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 185 ggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM-KNTTILTIAHRLRSVIDY-DKILVMEMG 262
Cdd:cd03269 128 ---ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELcDRVLLLNKG 204
|
....*
gi 767157600 263 RVKEY 267
Cdd:cd03269 205 RAVLY 209
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-270 |
2.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWE-----NGTIIIDNKDIKHIPLE--R 105
Cdd:PRK14267 5 IETVNLRVYYG--SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPtlfdgtvrsnlDPFDR---YSDVQIYGVLSkvGLIEECDELSLISEQEQPNFSS-HKLRNRFIDLntv 181
Cdd:PRK14267 83 VRREVGMVFQYP-----------NPFPHltiYDNVAIGVKLN--GLVKSKKELDERVEWALKKAALwDEVKDRLNDY--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 182 vksgGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAH---RLRSVIDYDKILV 258
Cdd:PRK14267 147 ----PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLY 222
|
250
....*....|....*..
gi 767157600 259 M----EMGRVKE-YDHP 270
Cdd:PRK14267 223 LgkliEVGPTRKvFENP 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
33-264 |
2.61e-11 |
|
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: 62.41 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKS---SIIAAiyRLSDWENGTIIIDNKDIKHIPLERLRNS 109
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKStllSLITG--DLPPTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 I--------SCIPQDPTLFDgTVRS----NLDPFDRYSDVQIY---GVLSKVGLieecdelsliseqeqpnfsSHKLRNR 174
Cdd:COG1119 80 IglvspalqLRFPRDETVLD-VVLSgffdSIGLYREPTDEQRErarELLELLGL-------------------AHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 175 FidlntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN--TTILTIAHRLRSVID 252
Cdd:COG1119 140 F-----------GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPP 208
|
250
....*....|...
gi 767157600 253 -YDKILVMEMGRV 264
Cdd:COG1119 209 gITHVLLLKDGRV 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
35-272 |
2.69e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 35 LKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDnKDIKhiplerlrnsISCIP 114
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR----------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 115 QDPTLFDG-TVRSN-LDPFDRYSDvqiygvlskvgLIEECDELS-LISEQEQPNFSSHKLRNRFIDLN---------TVV 182
Cdd:COG0488 68 QEPPLDDDlTVLDTvLDGDAELRA-----------LEAELEELEaKLAEPDEDLERLAELQEEFEALGgweaearaeEIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 KSGG----------SNLSQGQRQLLCLARSMLGARNIMLIDEAT-----ASI----DYISDAKiqktiretmknTTILTI 243
Cdd:COG0488 137 SGLGfpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTnhldlESIewleEFLKNYP-----------GTVLVV 205
|
250 260 270
....*....|....*....|....*....|..
gi 767157600 244 AH-R--LRSVIdyDKILVMEMGRVKEYDHPYT 272
Cdd:COG0488 206 SHdRyfLDRVA--TRILELDRGKLTLYPGNYS 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-265 |
2.77e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 29 QTGDV--ELKNLSLRY--SPHSsKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRL--SDWEnGTIIIDNK--DIKH 100
Cdd:TIGR02633 252 EIGDVilEARNLTCWDviNPHR-KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAypGKFE-GNVFINGKpvDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 101 iPLERLRNSISCIPQD-------PTLFDGTvRSNLDPFDRYsdvqiygvlSKVGLIEECDELSLISEQeqpnFSSHKLRN 173
Cdd:TIGR02633 330 -PAQAIRAGIAMVPEDrkrhgivPILGVGK-NITLSVLKSF---------CFKMRIDAAAELQIIGSA----IQRLKVKT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 174 RFIDLNTvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVID 252
Cdd:TIGR02633 395 ASPFLPI------GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLG 468
|
250
....*....|....
gi 767157600 253 Y-DKILVMEMGRVK 265
Cdd:TIGR02633 469 LsDRVLVIGEGKLK 482
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
34-272 |
2.82e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSL--RYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRL-----SDWENGTIIIDNKDIKHIPLERL 106
Cdd:PRK15134 7 AIENLSVafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 R----NSISCIPQDPTLfdgtvrsNLDPFDRYsDVQIYGVLS-KVGLIEECDELSLISEQEQPNFssHKLRNRFIDLNtv 181
Cdd:PRK15134 87 RgvrgNKIAMIFQEPMV-------SLNPLHTL-EKQLYEVLSlHRGMRREAARGEILNCLDRVGI--RQAAKRLTDYP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 182 vksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILV 258
Cdd:PRK15134 155 -----HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLaDRVAV 229
|
250 260
....*....|....*....|....
gi 767157600 259 MEMGRVKEYD----------HPYT 272
Cdd:PRK15134 230 MQNGRCVEQNraatlfsaptHPYT 253
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
49-274 |
3.99e-11 |
|
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: 62.28 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRN----SISCIPQDPTLF-DGT 123
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 124 VRSNLdpfdrysdvqIYGVlskvglieecdELSLISEQEQPNFSSHKLRNrfIDLNTVVKSGGSNLSQGQRQLLCLARSM 203
Cdd:cd03294 119 VLENV----------AFGL-----------EVQGVPRAEREERAAEALEL--VGLEGWEHKYPDELSGGMQQRVGLARAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 204 LGARNIMLIDEATASIDyisdakiqKTIRETMKNT----------TILTIAHRLRSVIDY-DKILVMEMGRVKEYDHPYT 272
Cdd:cd03294 176 AVDPDILLMDEAFSALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEE 247
|
..
gi 767157600 273 LI 274
Cdd:cd03294 248 IL 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
44-272 |
4.85e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 44 PHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI---KHIPLERLRNSISCIPQDPtLF 120
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDP-LA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 121 DGTVRSNL-----DPFDRY------SDV--QIYGVLSKVGLIeecdelsliseqeqPNfsshkLRNRFidlntvvksgGS 187
Cdd:PRK15079 110 SLNPRMTIgeiiaEPLRTYhpklsrQEVkdRVKAMMLKVGLL--------------PN-----LINRY----------PH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 188 NLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNT--TILTIAHRLrSVIDY--DKILVMEMGR 263
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDL-AVVKHisDRVLVMYLGH 239
|
250
....*....|....*....
gi 767157600 264 VKE---YD-------HPYT 272
Cdd:PRK15079 240 AVElgtYDevyhnplHPYT 258
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
33-280 |
8.60e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.25 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKH--IPLERLRNSI 110
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDP--TLFDGTVRsnldpfdrySDVQiYGVLSkVGLIEEcdelsliseqeqpnfsshKLRNRFID-LNTVVKSGGS 187
Cdd:PRK13639 81 GIVFQNPddQLFAPTVE---------EDVA-FGPLN-LGLSKE------------------EVEKRVKEaLKAVGMEGFE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 188 N-----LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-TTILTIAHRLRSVIDY-DKILVME 260
Cdd:PRK13639 132 NkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYaDKVYVMS 211
|
250 260
....*....|....*....|
gi 767157600 261 MGRVKEYDHPYTLISDRNTI 280
Cdd:PRK13639 212 DGKIIKEGTPKEVFSDIETI 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
33-273 |
9.35e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.70 E-value: 9.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKD--IKHIPLERlrnSI 110
Cdd:COG1118 3 IEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPRER---RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLF-DGTVRSN-------LDPFDRYSDVQIYGVLSKVGLieecDELSliseqeqpnfsshklrNRFIdlntvv 182
Cdd:COG1118 78 GFVFQHYALFpHMTVAENiafglrvRPPSKAEIRARVEELLELVQL----EGLA----------------DRYP------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 ksggSNLSQGQRQLLCLARsMLGAR-NIMLIDEATASIdyisDAKIQKTIR-------ETMKNTTI---------LTIAh 245
Cdd:COG1118 132 ----SQLSGGQRQRVALAR-ALAVEpEVLLLDEPFGAL----DAKVRKELRrwlrrlhDELGGTTVfvthdqeeaLELA- 201
|
250 260 270
....*....|....*....|....*....|....*
gi 767157600 246 rlrsvidyDKILVMEMGRVKE-------YDHPYTL 273
Cdd:COG1118 202 --------DRVVVMNQGRIEQvgtpdevYDRPATP 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-124 |
9.47e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 28 PQTGDV--ELKNLSLRySPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHI-PLE 104
Cdd:COG3845 251 AEPGEVvlEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLsPRE 329
|
90 100
....*....|....*....|
gi 767157600 105 RLRNSISCIPQDPtLFDGTV 124
Cdd:COG3845 330 RRRLGVAYIPEDR-LGRGLV 348
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
33-264 |
1.59e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 60.53 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY---SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIID---------NKDIKH 100
Cdd:PRK13649 3 INLQNVSYTYqagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstskNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 101 IplerlRNSISCIPQDP--TLFDGTVrsnldpfdrYSDV----QIYGVlskvglieecdelsliSEQEQPNFSSHKLRNR 174
Cdd:PRK13649 83 I-----RKKVGLVFQFPesQLFEETV---------LKDVafgpQNFGV----------------SQEEAEALAREKLALV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 175 FIDLNTVVKSgGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETMKN-----TTILTIAHRLRS 249
Cdd:PRK13649 133 GISESLFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL----DPKGRKELMTLFKKlhqsgMTIVLVTHLMDD 207
|
250
....*....|....*.
gi 767157600 250 VIDY-DKILVMEMGRV 264
Cdd:PRK13649 208 VANYaDFVYVLEKGKL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
49-250 |
1.81e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEnGTIIIDNKdikhiPLERL--------RNSISCIPQDPTlf 120
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQ-----PLHNLnrrqllpvRHRIQVVFQDPN-- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 121 dgtvrSNLDPfdRYSDVQIygvlskvglIEECDELsliseqEQPNFSSHKLRNRFIDlntVVKSGG----------SNLS 190
Cdd:PRK15134 373 -----SSLNP--RLNVLQI---------IEEGLRV------HQPTLSAAQREQQVIA---VMEEVGldpetrhrypAEFS 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767157600 191 QGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKI---QKTIRETMKNTTILtIAHRLRSV 250
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIlalLKSLQQKHQLAYLF-ISHDLHVV 489
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
33-273 |
2.22e-10 |
|
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: 59.56 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERlRNsISC 112
Cdd:cd03300 1 IELENVSKFYG--GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK-RP-VNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFdgtvrSNLDPFDRYSdvqiYGV----LSKVGLIEECDE-LSLISEQEqpnfsshkLRNRFIDlntvvksggs 187
Cdd:cd03300 77 VFQNYALF-----PHLTVFENIA----FGLrlkkLPKAEIKERVAEaLDLVQLEG--------YANRKPS---------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 188 NLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETMKN------TTILTIAHRLRSVIDY-DKILVME 260
Cdd:cd03300 130 QLSGGQQQRVAIARALVNEPKVLLLDEPLGAL----DLKLRKDMQLELKRlqkelgITFVFVTHDQEEALTMsDRIAVMN 205
|
250 260
....*....|....*....|
gi 767157600 261 MGRVKE-------YDHPYTL 273
Cdd:cd03300 206 KGKIQQigtpeeiYEEPANR 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
49-233 |
2.91e-10 |
|
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: 58.52 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISCIPQD---PTLfdgTVR 125
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPglkPEL---SAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 126 SNLD---PFDRYSDVQIYGVLSKVGLIEECDelsLISEQeqpnfsshklrnrfidlntvvksggsnLSQGQRQLLCLARS 202
Cdd:TIGR01189 92 ENLHfwaAIHGGAQRTIEDALAAVGLTGFED---LPAAQ---------------------------LSAGQQRRLALARL 141
|
170 180 190
....*....|....*....|....*....|.
gi 767157600 203 MLGARNIMLIDEATASIDYISDAKIQKTIRE 233
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-260 |
3.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 37 NLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSD-----WENGTIIIDNKDI-KHIPLERLRNSI 110
Cdd:PRK14271 26 NLTLGFA--GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIfNYRDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDGTVRSNLdpfdrysdvqIYGVLSKvglieecdelSLISEQEQPNFSSHKLRNrfIDLNTVVKSGGSN-- 188
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNV----------LAGVRAH----------KLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDsp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 189 --LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRL--------RSVIDYDKILV 258
Cdd:PRK14271 162 frLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaqaarisdRAALFFDGRLV 241
|
..
gi 767157600 259 ME 260
Cdd:PRK14271 242 EE 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
33-276 |
3.37e-10 |
|
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: 60.59 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSS---KALDNVSFKVKAGTKVGIVGRTGAGK---SSIIAAI---------YRLSD-WENGTiiidnk 96
Cdd:TIGR03269 280 IKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKttlSKIIAGVleptsgevnVRVGDeWVDMT------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 97 diKHIPLERLRNS--ISCIPQDPTLFdgTVRSNLDPfdrysdvqiygvLSKVGLIEECDELSL---ISEQEQPNFSSHKL 171
Cdd:TIGR03269 354 --KPGPDGRGRAKryIGILHQEYDLY--PHRTVLDN------------LTEAIGLELPDELARmkaVITLKMVGFDEEKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 172 RNrfidlntVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTI---RETMkNTTILTIAHRLR 248
Cdd:TIGR03269 418 EE-------ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEM-EQTFIIVSHDMD 489
|
250 260
....*....|....*....|....*....
gi 767157600 249 SVIDY-DKILVMEMGRVKEYDHPYTLISD 276
Cdd:TIGR03269 490 FVLDVcDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-274 |
3.75e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.82 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 30 TGDVELKNLSLRYSPHSskALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI-KHIPLERLRn 108
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 109 sISCIPQ----DPtlfDGTVRSNLDPFDRYsdvqiygvlskVGLieecdelsliseqeqpnfSSHKLRNR------FIDL 178
Cdd:PRK13537 82 -VGVVPQfdnlDP---DFTVRENLLVFGRY-----------FGL------------------SAAAARALvpplleFAKL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 179 NTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM-KNTTILTIAH------RLrsvi 251
Cdd:PRK13537 129 ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL---- 204
|
250 260
....*....|....*....|...
gi 767157600 252 dYDKILVMEMGRVKEYDHPYTLI 274
Cdd:PRK13537 205 -CDRLCVIEEGRKIAEGAPHALI 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
33-270 |
5.42e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSK--------------------ALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSdweNG 89
Cdd:COG1134 5 IEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTllkLIAGILEPT---SG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 90 TIIIDNKdikhI--PLErlrnsiscipqdptL---FDG--TVRSNLdpfdrYSDVQIYGvLSKV---GLIEECDELSLIS 159
Cdd:COG1134 82 RVEVNGR----VsaLLE--------------LgagFHPelTGRENI-----YLNGRLLG-LSRKeidEKFDEIVEFAELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 160 EqeqpnfsshklrnrFIDlnTVVKsggsNLSQGQRQLLCLARSMlgARN--IMLIDEATAsidyISDA----KIQKTIRE 233
Cdd:COG1134 138 D--------------FID--QPVK----TYSSGMRARLAFAVAT--AVDpdILLVDEVLA----VGDAafqkKCLARIRE 191
|
250 260 270
....*....|....*....|....*....|....*....
gi 767157600 234 TMKN-TTILTIAHRLRSVIDY-DKILVMEMGRVKEYDHP 270
Cdd:COG1134 192 LRESgRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDP 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
57-264 |
5.65e-10 |
|
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: 58.27 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 57 VKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERlrNSISCIPQDPTLFDG-TVRSNLD----PF 131
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGlglsPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 132 DRYSDVQ---IYGVLSKVGLieecDELslisEQEQPNfsshklrnrfidlntvvksggsNLSQGQRQLLCLARSMLGARN 208
Cdd:cd03298 99 LKLTAEDrqaIEVALARVGL----AGL----EKRLPG----------------------ELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 209 IMLIDEATASIDYISDAKIQK---TIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRV 264
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDlvlDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
33-264 |
7.89e-10 |
|
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: 57.65 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIDNKDIKHIPLERlRNs 109
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTtlrMIAGLEEPTS---GRIYIGGRDVTDLPPKD-RD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLF-DGTVRSNLDpfdrysdvqiYGVLSKVGLIEECDElsliseqeqpnfsshKLRN--RFIDLNTVVKSGG 186
Cdd:cd03301 74 IAMVFQNYALYpHMTVYDNIA----------FGLKLRKVPKDEIDE---------------RVREvaELLQIEHLLDRKP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETMKN------TTILTIAHrlrsviDY------- 253
Cdd:cd03301 129 KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL----DAKLRVQMRAELKRlqqrlgTTTIYVTH------DQveamtma 198
|
250
....*....|.
gi 767157600 254 DKILVMEMGRV 264
Cdd:cd03301 199 DRIAVMNDGQI 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
33-275 |
1.59e-09 |
|
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: 58.66 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENgtiiIDNKDIKHIPLerlrnSISC 112
Cdd:TIGR03269 1 IEVKNLTKKFD--GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP----TSGRIIYHVAL-----CEKC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDGT----VRSNLDPFD----RYSDVQIYGVLSKVGLI---------EECDELSLISEQEQPNFSSHKLRNRF 175
Cdd:TIGR03269 70 GYVERPSKVGEpcpvCGGTLEPEEvdfwNLSDKLRRRIRKRIAIMlqrtfalygDDTVLDNVLEALEEIGYEGKEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 176 IDLNTVVKSG------GSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTI-LTIAHRLR 248
Cdd:TIGR03269 150 VDLIEMVQLShrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 767157600 249 SVID--YDKILVMEMGRVKEYDHPYTLIS 275
Cdd:TIGR03269 230 EVIEdlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-276 |
1.61e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.92 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 15 SESNGYISPPANWPQTGdVELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTI-II 93
Cdd:PRK13536 25 GISEAKASIPGSMSTVA-IDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 94 DNKDIKHIPLERLRnsISCIPQDPTL-FDGTVRSNLDPFDRY---SDVQIYGVLSKvgLIEecdelsliseqeqpnfssh 169
Cdd:PRK13536 102 GVPVPARARLARAR--IGVVPQFDNLdLEFTVRENLLVFGRYfgmSTREIEAVIPS--LLE------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 170 klrnrFIDLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM-KNTTILTIAH--- 245
Cdd:PRK13536 159 -----FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfme 233
|
250 260 270
....*....|....*....|....*....|....
gi 767157600 246 ---RLrsvidYDKILVMEMGRVKEYDHPYTLISD 276
Cdd:PRK13536 234 eaeRL-----CDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
33-276 |
1.70e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIK--HIPLERLRNSI 110
Cdd:PRK09493 2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 111 SCIPQDPTLFDG-TVRSNLdpfdRYSDVQIYG------------VLSKVGLIEECDELSliseqeqpnfsshklrnrfid 177
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENV----MFGPLRVRGaskeeaekqareLLAKVGLAERAHHYP--------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 178 lntvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIR----ETMkntTILTIAHRL---RSV 250
Cdd:PRK09493 135 ---------SELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlaeEGM---TMVIVTHEIgfaEKV 202
|
250 260
....*....|....*....|....*.
gi 767157600 251 IdyDKILVMEMGRVKEYDHPYTLISD 276
Cdd:PRK09493 203 A--SRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
49-264 |
1.88e-09 |
|
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: 56.96 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIyrlsdweNGTIIIDNKDIK---HIPLERLRNSISCIP----QDPTLFd 121
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL-------SGLLQPTSGEVRvagLVPWKRRKKFLRRIGvvfgQKTQLW- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 122 gtvrSNLDPFDRYSDVQ-IYGvLSKVGLIEECDELSliseqeqpnfsshklrnRFIDLNTVVKSGGSNLSQGQRQLLCLA 200
Cdd:cd03267 108 ----WDLPVIDSFYLLAaIYD-LPPARFKKRLDELS-----------------ELLDLEELLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 201 RSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN--TTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-105 |
1.94e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.43 E-value: 1.94e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLER 105
Cdd:COG4152 2 LELKGLTKRFGDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR 72
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-266 |
2.07e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 23 PPANWpQTgdVELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIDNKDIK 99
Cdd:PRK10522 316 AFPDW-QT--LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTlamLLTGLYQPQS---GEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 100 HIPLERLRNSISCIPQDPTLFDGTvrsnLDPFDRYSDVQIYGV-LSKVGLieecdelsliseqeqpnfsSHKLR---NRF 175
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKM-------------------AHKLEledGRI 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 176 IDLntvvksggsNLSQGQRQLLCLARSMLGARNIMLIDEATASID-------YisdAKIQKTIRETMKntTILTIAHRLR 248
Cdd:PRK10522 446 SNL---------KLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrrefY---QVLLPLLQEMGK--TIFAISHDDH 511
|
250
....*....|....*...
gi 767157600 249 SVIDYDKILVMEMGRVKE 266
Cdd:PRK10522 512 YFIHADRLLEMRNGQLSE 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
43-264 |
2.51e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 43 SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTI----IIDNKDIKHIPLERLRNSISCIPQDP- 117
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRKKVGVVFQFPe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 118 -TLFDGTVRSnldpfDRYSDVQIYGvlskvglieecdelslISEQEQPNFSSHKLRNRFIDLNTVVKSgGSNLSQGQRQL 196
Cdd:PRK13643 95 sQLFEETVLK-----DVAFGPQNFG----------------IPKEKAEKIAAEKLEMVGLADEFWEKS-PFELSGGQMRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767157600 197 LCLARSMLGARNIMLIDEATASID---YISDAKIQKTIRETmkNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDpkaRIEMMQLFESIHQS--GQTVVLVTHLMDDVADYaDYVYLLEKGHI 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
37-276 |
3.07e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.52 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 37 NLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHI-------------PL 103
Cdd:PRK10619 10 DLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 104 ERLRNSISCIPQDPTLFDG-TVRSNLdpfdRYSDVQIYGV------------LSKVGlieecdelslISEQEQPNFSSHk 170
Cdd:PRK10619 88 RLLRTRLTMVFQHFNLWSHmTVLENV----MEAPIQVLGLskqeareravkyLAKVG----------IDERAQGKYPVH- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 171 lrnrfidlntvvksggsnLSQGQRQLLCLARSMLGARNIMLIDEATASID--YISDA-KIQKTIRETMKntTILTIAHRL 247
Cdd:PRK10619 153 ------------------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpeLVGEVlRIMQQLAEEGK--TMVVVTHEM 212
|
250 260 270
....*....|....*....|....*....|..
gi 767157600 248 ---RSVIDYdkILVMEMGRVKEYDHPYTLISD 276
Cdd:PRK10619 213 gfaRHVSSH--VIFLHQGKIEEEGAPEQLFGN 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
28-266 |
3.64e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 28 PQTGDVeLKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLsdwENGTIIIDNKDIKHIPLERLR 107
Cdd:COG2401 25 ERVAIV-LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA---LKGTPVAGCVDVPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDPTLFDGTvrsnldpfdrysdvqiyGVLSKVGLieecdelsliseQEQPNFsshklRNRFidlntvvksggS 187
Cdd:COG2401 101 SLIDAIGRKGDFKDAV-----------------ELLNAVGL------------SDAVLW-----LRRF-----------K 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 188 NLSQGQRQLLCLARSMLGARNIMLIDEATASID----YISDAKIQKTIREtmKNTTILTIAHR--LRSVIDYDKILVMEM 261
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARR--AGITLVVATHHydVIDDLQPDLLIFVGY 213
|
....*
gi 767157600 262 GRVKE 266
Cdd:COG2401 214 GGVPE 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
34-263 |
3.75e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.15 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSI---IAAIYRLSdweNGTIIIDNKDIKHIPLERL-RNS 109
Cdd:PRK11300 7 SVSGLMMRFG--GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVfncLTGFYKPT---GGTILLRGQHIEGLPGHQIaRMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLF-DGTVRSNL-DPFDRYSDVQIYGVLSKVGLIEEcdelsliSEQEQPNFSSHKLRnrFIDLNTVVKSGGS 187
Cdd:PRK11300 82 VVRTFQHVRLFrEMTVIENLlVAQHQQLKTGLFSGLLKTPAFRR-------AESEALDRAATWLE--RVGLLEHANRQAG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 188 NLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILVMEMGR 263
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGIsDRIYVVNQGT 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
50-233 |
4.09e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 50 LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDikhIPLERLRNSISCI-PQD---PTLfdgTVR 125
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNamkPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 126 SNLDpFDRysdvQIYGvlSKVGLIEECDElsliseqeqpnfsshklrnrFIDLNTVVKSGGSNLSQGQRQLLCLARSMLG 205
Cdd:PRK13539 92 ENLE-FWA----AFLG--GEELDIAAALE--------------------AVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180
....*....|....*....|....*...
gi 767157600 206 ARNIMLIDEATASIDYISDAKIQKTIRE 233
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-296 |
4.13e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.77 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 18 NGYISPPANWPQ---TGDVELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIID 94
Cdd:PRK11607 2 NDAIPRPQAKTRkalTPLLEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 95 NKDIKHIPleRLRNSISCIPQDPTLFDG-TVRSNLdPFDRYSDVqiygvLSKVGLIEECDE-LSLISEQEQPNFSSHKLr 172
Cdd:PRK11607 80 GVDLSHVP--PYQRPINMMFQSYALFPHmTVEQNI-AFGLKQDK-----LPKAEIASRVNEmLGLVHMQEFAKRKPHQL- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 173 nrfidlntvvksggsnlSQGQRQLLCLARSMLGARNIMLIDEATASIDyisdakiqKTIRETMKnTTILTIAHRLRS--- 249
Cdd:PRK11607 151 -----------------SGGQRQRVALARSLAKRPKLLLLDEPMGALD--------KKLRDRMQ-LEVVDILERVGVtcv 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767157600 250 VIDYDKILVMEM-GRVKEYDH-PYTLISDRNTIF-YRLCRQSGEF---ENLFE 296
Cdd:PRK11607 205 MVTHDQEEAMTMaGRIAIMNRgKFVQIGEPEEIYeHPTTRYSAEFigsVNVFE 257
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-266 |
7.83e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 24 PANWPQTGDV------ELKNLSLRysphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKD 97
Cdd:PRK09700 251 NAMKENVSNLahetvfEVRNVTSR----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 98 IK-HIPLERLRNSISCIPQ---DPTLFDG-TVRSNLDPFDRYSDVQIYGVLskvGLIEECDELSlISEQEQPNFSshkLR 172
Cdd:PRK09700 327 ISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIAQNMAISRSLKDGGYKGAM---GLFHEVDEQR-TAENQRELLA---LK 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 173 NRFIDLNTvvksggSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-TTILTIAHRLRSVI 251
Cdd:PRK09700 400 CHSVNQNI------TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEII 473
|
250
....*....|....*.
gi 767157600 252 DY-DKILVMEMGRVKE 266
Cdd:PRK09700 474 TVcDRIAVFCEGRLTQ 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
48-263 |
9.18e-09 |
|
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: 55.99 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDWEnGTIIIDNKDIK--HIPlERLRNSISCIPQDPTLF-D 121
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTlmkILSGVYPHGTWD-GEIYWSGSPLKasNIR-DTERAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 122 GTVRSNLdpFDRYSDVQIYGVLSKVGLIEECDELsliseqeqpnfsshkLRNRFIDLNTVVKSGGsNLSQGQRQLLCLAR 201
Cdd:TIGR02633 93 LSVAENI--FLGNEITLPGGRMAYNAMYLRAKNL---------------LRELQLDADNVTRPVG-DYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767157600 202 SMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKILVMEMGR 263
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAVcDTICVIRDGQ 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
33-280 |
1.31e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY---SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIP----LER 105
Cdd:PRK13646 3 IRFDNVSYTYqkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDP--TLFDGTVRSNLdpfdrysdvqIYGVLSKVGLIEECDElsliseqeqpnfSSHKLRNRFIDLNTVVK 183
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVEREI----------IFGPKNFKMNLDEVKN------------YAHRLLMDLGFSRDVMS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 SGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHRLRSVIDY-DKILVME 260
Cdd:PRK13646 141 QSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARYaDEVIVMK 220
|
250 260
....*....|....*....|
gi 767157600 261 MGRVKEYDHPYTLISDRNTI 280
Cdd:PRK13646 221 EGSIVSQTSPKELFKDKKKL 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
49-245 |
1.41e-08 |
|
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: 54.36 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYR--LSDweNGTIIIDNK----DIKHIP----LERLRNSI-------S 111
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPD--SGSILVRHDggwvDLAQASpreiLALRRRTIgyvsqflR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQ--------DPTLFDGTVRSnlDPFDRYSDvqiygVLSKVGLIEECDELSliseqeqPN-Fsshklrnrfidlntvv 182
Cdd:COG4778 104 VIPRvsaldvvaEPLLERGVDRE--EARARARE-----LLARLNLPERLWDLP-------PAtF---------------- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767157600 183 kSGgsnlsqGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-TTILTIAH 245
Cdd:COG4778 154 -SG------GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFH 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
34-278 |
1.56e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.39 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 34 ELKNLSLRYspHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAI--YRLSDweNGTIIIDNKDIKHIPLERLRNSIS 111
Cdd:PRK13548 4 EARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgELSPD--SGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPTL-FDGTVR-----------SNLDPFDRYSDvqiyGVLSKVGLIEecdelsliseqeqpnfsshkLRNRFIdln 179
Cdd:PRK13548 80 VLPQHSSLsFPFTVEevvamgraphgLSRAEDDALVA----AALAQVDLAH--------------------LAGRDY--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 180 tvvksggSNLSQGQRQLLCLARSML------GARNIMLIDEATASIDyisdakiqktIRETMkntTILTIAHRL-----R 248
Cdd:PRK13548 133 -------PQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD----------LAHQH---HVLRLARQLahergL 192
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767157600 249 SVI----D------Y-DKILVMEMGRVKEYDHPYTLISDRN 278
Cdd:PRK13548 193 AVIvvlhDlnlaarYaDRIVLLHQGRLVADGTPAEVLTPET 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
33-281 |
1.79e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.73 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHiplerlrNSIS- 111
Cdd:PRK11432 7 VVLKNITKRFG--SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-------RSIQq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 ---CIP-QDPTLFdgtvrsnldPFDRYSDVQIYGV----LSKVGLIEECDE-LSLIseqEQPNFSshklrNRFIDlntvv 182
Cdd:PRK11432 78 rdiCMVfQSYALF---------PHMSLGENVGYGLkmlgVPKEERKQRVKEaLELV---DLAGFE-----DRYVD----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 183 ksggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETMK------NTTILTIAH-RLRSVIDYDK 255
Cdd:PRK11432 136 -----QISGGQQQRVALARALILKPKVLLFDEPLSNL----DANLRRSMREKIRelqqqfNITSLYVTHdQSEAFAVSDT 206
|
250 260
....*....|....*....|....*.
gi 767157600 256 ILVMEMGRVKEYDHPYTLISDRNTIF 281
Cdd:PRK11432 207 VIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
33-264 |
2.22e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLER-LRNSIS 111
Cdd:PRK11614 6 LSFDKVSAHYG--KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPTLFDG-TVRSNLDPFDRYSDVQIYgvlskVGLIEECDELsliseqeqpnFSshKLRNRFIDlntvvKSGgsNLS 190
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQF-----QERIKWVYEL----------FP--RLHERRIQ-----RAG--TMS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767157600 191 QGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-TTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:PRK11614 140 GGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLaDRGYVLENGHV 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-264 |
2.42e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 23 PPANWPQTGDVELKNLSLRYSPhsskALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIK-HI 101
Cdd:PRK10982 241 DKENKPGEVILEVRNLTSLRQP----SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 102 PLERLRNSISCIPQdptlfdgtvrsnldpfDRYSdVQIYGVLSkvglieeCDELSLISEQEQPNFSSHKLRNRFIDLNTV 181
Cdd:PRK10982 317 ANEAINHGFALVTE----------------ERRS-TGIYAYLD-------IGFNSLISNIRNYKNKVGLLDNSRMKSDTQ 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 182 -------VKSGG-----SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLR 248
Cdd:PRK10982 373 wvidsmrVKTPGhrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMP 452
|
250
....*....|....*..
gi 767157600 249 SVIDY-DKILVMEMGRV 264
Cdd:PRK10982 453 ELLGItDRILVMSNGLV 469
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
33-278 |
2.60e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYsPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:PRK13647 5 IEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDP--TLFDGTVrsnldpfdrYSDVQiYGVLSkVGLIEecDELSLISEQEQPNFSSHKLRNRfidlntvvksGGSNLS 190
Cdd:PRK13647 84 VFQDPddQVFSSTV---------WDDVA-FGPVN-MGLDK--DEVERRVEEALKAVRMWDFRDK----------PPYHLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 191 QGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETM-----KNTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYL----DPRGQETLMEILdrlhnQGKTVIVATHDVDLAAEWaDQVIVLKEGRV 216
|
250
....*....|....
gi 767157600 265 KEYDHPyTLISDRN 278
Cdd:PRK13647 217 LAEGDK-SLLTDED 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
54-270 |
3.17e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.43 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 54 SFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLErlRNSISCIPQDPTLFDG-TVRSN----L 128
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNiglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 129 DPFDRYSDVQ---IYGVLSKVGLIEECDELsliseqeqPnfsshklrnrfidlntvvksggSNLSQGQRQLLCLARSMLG 205
Cdd:PRK10771 97 NPGLKLNAAQrekLHAIARQMGIEDLLARL--------P----------------------GQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 206 ARNIMLIDEATASIDYISDAKIQKTIRE--TMKNTTILTIAHrlrSVIDYDKI----LVMEMGRVkEYDHP 270
Cdd:PRK10771 147 EQPILLLDEPFSALDPALRQEMLTLVSQvcQERQLTLLMVSH---SLEDAARIaprsLVVADGRI-AWDGP 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
33-272 |
5.78e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 52.71 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNK--DIKHIPLER----L 106
Cdd:PRK11124 3 IQLNGINCFYG--AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKaireL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 RNSISCIPQD----PTLfdgTVRSNL--DPfdrysdVQIYGvLSKVGLIEECDEL--SLISEQEQPNFSSHklrnrfidl 178
Cdd:PRK11124 81 RRNVGMVFQQynlwPHL---TVQQNLieAP------CRVLG-LSKDQALARAEKLleRLRLKPYADRFPLH--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 179 ntvvksggsnLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIREtMKNTTI--------LTIAHRLRSv 250
Cdd:PRK11124 142 ----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGItqvivtheVEVARKTAS- 209
|
250 260
....*....|....*....|....*...
gi 767157600 251 idydKILVMEMGRVKE------YDHPYT 272
Cdd:PRK11124 210 ----RVVYMENGHIVEqgdascFTQPQT 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
33-266 |
6.51e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.87 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLS--LRYSP-----HSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLER 105
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPT-----------LFDGTVRSN--LDPFDRysDVQIYGVLSKVGLIeecdelsliseQEQPNFSSHKlr 172
Cdd:PRK15112 85 RSQRIRMIFQDPStslnprqrisqILDFPLRLNtdLEPEQR--EKQIIETLRQVGLL-----------PDHASYYPHM-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 173 nrfidlntvvksggsnLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTI---AHRLRS 249
Cdd:PRK15112 150 ----------------LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIyvtQHLGMM 213
|
250
....*....|....*..
gi 767157600 250 VIDYDKILVMEMGRVKE 266
Cdd:PRK15112 214 KHISDQVLVMHQGEVVE 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-282 |
6.59e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKhIPLERLRNSISC 112
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSNLDPFdrysdVQIYGvlskvgliEECDELSLISEQEQPNFSSHKLRNRfidlntvvksGGSNLSQ 191
Cdd:TIGR01257 1008 CPQHNILFHHlTVAEHILFY-----AQLKG--------RSWEEAQLEMEAMLEDTGLHHKRNE----------EAQDLSG 1064
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 192 GQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLRSV-IDYDKILVMEMGRVKEYDHP 270
Cdd:TIGR01257 1065 GMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
250
....*....|..
gi 767157600 271 YTLISDRNTIFY 282
Cdd:TIGR01257 1145 LFLKNCFGTGFY 1156
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-280 |
7.26e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 28 PQTGD--VELKNLSLRY---SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRL------------------S 84
Cdd:PRK13631 15 PLSDDiiLRVKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyigdkK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 85 DWENGTIIIDNKDIKHipLERLRNSISCIPQDP--TLFDGTVRsnldpfdrySDVQIYGVLSKVGLIEEcdelsliSEQE 162
Cdd:PRK13631 95 NNHELITNPYSKKIKN--FKELRRRVSMVFQFPeyQLFKDTIE---------KDIMFGPVALGVKKSEA-------KKLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 163 QPNFSSHKLRNRFIDLNTVvksggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK-NTTIL 241
Cdd:PRK13631 157 KFYLNKMGLDDSYLERSPF------GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVF 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767157600 242 TIAHRLRSVIDY-DKILVMEMGRVKEYDHPYTLISDRNTI 280
Cdd:PRK13631 231 VITHTMEHVLEVaDEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
33-260 |
8.36e-08 |
|
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: 50.52 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYspHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIyrlsdweNGTIIIDNKDIKHIPlerlRNSISC 112
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGELEPDEGIVTWGS----TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQdptlfdgtvrsnldpfdrysdvqiygvlskvglieecdelsliseqeqpnfsshklrnrfidlntvvksggsnLSQG 192
Cdd:cd03221 68 FEQ-------------------------------------------------------------------------LSGG 74
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 193 QRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIREtmKNTTILTIAH-R--LRSVIdyDKILVME 260
Cdd:cd03221 75 EKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQVA--TKIIELE 141
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-278 |
1.09e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 32 DVELKNLSLRY---SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI----KHIPLE 104
Cdd:PRK13634 2 DITFQKVEHRYqykTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 105 RLRNSISCIPQDP--TLFDGTVRSNL--DPfdrysdvQIYGV------------LSKVGLIEECDElsliseqeqpnfss 168
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETVEKDIcfGP-------MNFGVseedakqkaremIELVGLPEELLA-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 169 hklRNRFidlntvvksggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIdyisDAKIQKTIRETM------KNTTILT 242
Cdd:PRK13634 141 ---RSPF------------ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL----DPKGRKEMMEMFyklhkeKGLTTVL 201
|
250 260 270
....*....|....*....|....*....|....*..
gi 767157600 243 IAHRLRSVIDY-DKILVMEMGRVKEYDHPYTLISDRN 278
Cdd:PRK13634 202 VTHSMEDAARYaDQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
50-264 |
1.38e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.74 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 50 LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSdwENGTIIIDNKDIKHIPLER--LRnSISCIPQDPTLFDG--TVR 125
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLLNGMPIDAkeMR-AISAYVQQDDLFIPtlTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 126 SNLDpF-------DRYSDVQiygvlsKVGLIEEC-DELSLISEQeqpnfsshklrnrfidlNTVVKSGGS--NLSQGQRQ 195
Cdd:TIGR00955 118 EHLM-FqahlrmpRRVTKKE------KRERVDEVlQALGLRKCA-----------------NTRIGVPGRvkGLSGGERK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767157600 196 LLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVI--DYDKILVMEMGRV 264
Cdd:TIGR00955 174 RLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELfeLFDKIILMAEGRV 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
47-283 |
1.46e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 52.34 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 47 SKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLR----NSISCIPQDPTLFdg 122
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALM-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 123 tvrsnldPFDRYSDVQIYGVlskvglieecdELSLISEQEQPNFSSHKLRNrfIDLNTVVKSGGSNLSQGQRQLLCLARS 202
Cdd:PRK10070 119 -------PHMTVLDNTAFGM-----------ELAGINAEERREKALDALRQ--VGLENYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 203 MLGARNIMLIDEATASIDYISDAKIQKTI--RETMKNTTILTIAHRLRSVIDY-DKILVMEMGRVKEYDHPYTLISDRNT 279
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
....
gi 767157600 280 IFYR 283
Cdd:PRK10070 259 DYVR 262
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
36-272 |
1.58e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.83 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 36 KNLSLRY-SPHSS-KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDwENGTIIIDN---KDI---KHIPLER-- 105
Cdd:COG4170 7 RNLTIEIdTPQGRvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRfrwNGIdllKLSPRERrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 -LRNSISCIPQDPtlfdgtvRSNLDPfdrysdvqiygvLSKVG--LIEecdelSLISEQEQPNFSSHKL--RNRFIDL-- 178
Cdd:COG4170 86 iIGREIAMIFQEP-------SSCLDP------------SAKIGdqLIE-----AIPSWTFKGKWWQRFKwrKKRAIELlh 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 179 -------NTVVKSGGSNLSQGQRQLLCLArsM-LGARNIMLI-DEATASIDYISDAKIQKTIRET--MKNTTILTIAHRL 247
Cdd:COG4170 142 rvgikdhKDIMNSYPHELTEGECQKVMIA--MaIANQPRLLIaDEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDL 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 767157600 248 RSVIDY-DKILVM------EMGRVKEY----DHPYT 272
Cdd:COG4170 220 ESISQWaDTITVLycgqtvESGPTEQIlkspHHPYT 255
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
41-265 |
1.92e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 41 RYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIyrLSDWEngtiiidnkdIKH--IPLERlrnSISCIPQDPT 118
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL--LSQFE----------ISEgrVWAER---SIAYVPQQAW 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 119 LFDGTVRSNLDPFDRYSDVQIYGVLSKVGLieECDELSLISeqeqpnfsshklrnrfiDLNTVVKSGGSNLSQGQRQLLC 198
Cdd:PTZ00243 732 IMNATVRGNILFFDEEDAARLADAVRVSQL--EADLAQLGG-----------------GLETEIGEKGVNLSGGQKARVS 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767157600 199 LARSMLGARNIMLIDEATASID-YISDAKIQKTIRETMKNTTILTIAHRLRSVIDYDKILVMEMGRVK 265
Cdd:PTZ00243 793 LARAVYANRDVYLLDDPLSALDaHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
48-272 |
2.17e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLE---RLRNSISCIPQDPtlfdgtv 124
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNP------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 125 rsnldpfdrysdvqiYGVLS---KVGLIEEcdELSLISEqeqpNFSSHKLRNRFIDLNTVVK-------------SGGsn 188
Cdd:PRK11308 102 ---------------YGSLNprkKVGQILE--EPLLINT----SLSAAERREKALAMMAKVGlrpehydryphmfSGG-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 189 lsqgQRQLLCLARSMLGARNIMLIDEATASIDyISdakIQKTIRETMK------NTTILTIAHRLrSVIDY--DKILVME 260
Cdd:PRK11308 159 ----QRQRIAIARALMLDPDVVVADEPVSALD-VS---VQAQVLNLMMdlqqelGLSYVFISHDL-SVVEHiaDEVMVMY 229
|
250 260
....*....|....*....|..
gi 767157600 261 MGRVKE-------YD---HPYT 272
Cdd:PRK11308 230 LGRCVEkgtkeqiFNnprHPYT 251
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
33-276 |
2.44e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.24 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY---SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTI--IIDNKDIKHIPLERLR 107
Cdd:PRK13651 3 IKVKNIVKIFnkkLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 108 NSISCIPQDPT------------------------LFDGTVRSNLdpfdrysdvqIYGVLSkVGlieecdelslISEQEq 163
Cdd:PRK13651 83 VLEKLVIQKTRfkkikkikeirrrvgvvfqfaeyqLFEQTIEKDI----------IFGPVS-MG----------VSKEE- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 164 pnfsSHKLRNRFIDL----NTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-T 238
Cdd:PRK13651 141 ----AKKRAAKYIELvgldESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgK 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 767157600 239 TILTIAHRLRSVIDYDK-ILVMEMGRVKEYDHPYTLISD 276
Cdd:PRK13651 217 TIILVTHDLDNVLEWTKrTIFFKDGKIIKDGDTYDILSD 255
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
48-263 |
2.89e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSdweNGTIIIDNKDIKHI-PLERLRNSISCIPQDPTLF-DG 122
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTllkILSGNYQPD---AGSILIDGQEMRFAsTTAALAAGVAIIYQELHLVpEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 123 TVRSNLD----PfdrysdvQIYGVLSKVGLIEEC-DELSLISEQeqpnfsshklrnrfIDLNTVVKSggsnLSQGQRQLL 197
Cdd:PRK11288 95 TVAENLYlgqlP-------HKGGIVNRRLLNYEArEQLEHLGVD--------------IDPDTPLKY----LSIGQRQMV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 198 CLARS-MLGARNIMLiDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHRLRSVIDY-DKILVMEMGR 263
Cdd:PRK11288 150 EIAKAlARNARVIAF-DEPTSSLSAREIEQLFRVIRElRAEGRVILYVSHRMEEIFALcDAITVFKDGR 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
35-122 |
3.17e-07 |
|
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: 49.83 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 35 LKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWE--NGTIIIDNKDIKHIPL-ERLRNSIS 111
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPeERARLGIF 80
|
90
....*....|.
gi 767157600 112 CIPQDPTLFDG 122
Cdd:cd03217 81 LAFQYPPEIPG 91
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-262 |
3.37e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPhsSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHI-PLERLRNSIS 111
Cdd:PRK09700 6 ISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 112 CIPQDPTLFDG-TVRSNLdPFDRYSDVQIYGVlskvglieECDELSLISEQEQPNFSSHKLRnrfIDLNTVVksggSNLS 190
Cdd:PRK09700 84 IIYQELSVIDElTVLENL-YIGRHLTKKVCGV--------NIIDWREMRVRAAMMLLRVGLK---VDLDEKV----ANLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 191 QGQRQLLCLARSMLGARNIMLIDEATASidyISDAKIQK--TIRETMKN--TTILTIAHRLRSVIDY-DKILVMEMG 262
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSS---LTNKEVDYlfLIMNQLRKegTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-264 |
3.62e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 29 QTGDV--ELKNLSlrysphsSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIK-HIPLER 105
Cdd:PRK10762 252 APGEVrlKVDNLS-------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 106 LRNSISCIPQDPTlFDG-----TVRSN--LDPFDRYSdvqiygvlSKVGLIEECDELSLISEqeqpnfsshklrnrFIDL 178
Cdd:PRK10762 325 LANGIVYISEDRK-RDGlvlgmSVKENmsLTALRYFS--------RAGGSLKHADEQQAVSD--------------FIRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 179 -NTVVKSGGS---NLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN-TTILTIAHRLRSVIDY 253
Cdd:PRK10762 382 fNIKTPSMEQaigLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGM 461
|
250
....*....|..
gi 767157600 254 -DKILVMEMGRV 264
Cdd:PRK10762 462 sDRILVMHEGRI 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-272 |
3.75e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 35 LKNLSLRYSPHSSK--ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTI-------------IIDNKDIK 99
Cdd:PRK10261 15 VENLNIAFMQEQQKiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 100 HIPLERLRNS-ISCIPQDPTlfdgtvrSNLDPfdrysdvqiygVLSKVGLIEECDELSLISEQEQPNFSSHKLRN--RFI 176
Cdd:PRK10261 95 AAQMRHVRGAdMAMIFQEPM-------TSLNP-----------VFTVGEQIAESIRLHQGASREEAMVEAKRMLDqvRIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 177 DLNTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTT--ILTIAHRLRSVIDY- 253
Cdd:PRK10261 157 EAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIa 236
|
250 260
....*....|....*....|....*....
gi 767157600 254 DKILVM------EMGRVKEY----DHPYT 272
Cdd:PRK10261 237 DRVLVMyqgeavETGSVEQIfhapQHPYT 265
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
36-266 |
5.76e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.69 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 36 KNLSLRYSPHSSKA-------LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKdikhiPLERL-- 106
Cdd:PRK10419 7 SGLSHHYAHGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-----PLAKLnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 ------RNSISCIPQDPTlfdgtvrSNLDPfdRYSdvqiygvlskVGLI--EECDELSLISEQEQPNFSSHKLRNRFIDL 178
Cdd:PRK10419 82 aqrkafRRDIQMVFQDSI-------SAVNP--RKT----------VREIirEPLRHLLSLDKAERLARASEMLRAVDLDD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 179 NTVVKSGGSnLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DK 255
Cdd:PRK10419 143 SVLDKRPPQ-LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFcQR 221
|
250
....*....|.
gi 767157600 256 ILVMEMGRVKE 266
Cdd:PRK10419 222 VMVMDNGQIVE 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
48-272 |
6.08e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEnGTII-----IDNKDIKHIPLERLRN----SISCIPQDPT 118
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMaekleFNGQDLQRISEKERRNlvgaEVAMIFQDPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 119 lfdgtvrSNLDPFdrYS-DVQIYGVLsKVglieecdelsliseqeQPNFSSHKLRNRFIDLNTVVK-------------- 183
Cdd:PRK11022 100 -------TSLNPC--YTvGFQIMEAI-KV----------------HQGGNKKTRRQRAIDLLNQVGipdpasrldvyphq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 184 -SGGsnlsQGQRQLLCLArsmLGARNIMLI-DEATASIDYISDAKIQKTIRETMK--NTTILTIAHRLRSVIDY-DKILV 258
Cdd:PRK11022 154 lSGG----MSQRVMIAMA---IACRPKLLIaDEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAaHKIIV 226
|
250 260
....*....|....*....|....
gi 767157600 259 MEMGRVKEYD----------HPYT 272
Cdd:PRK11022 227 MYAGQVVETGkahdifraprHPYT 250
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-133 |
7.26e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLsdwENGTIIIDNKDI---KHipLERL 106
Cdd:NF033858 2 ARLEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSllsLIAGARKI---QQGRVEVLGGDMadaRH--RRAV 74
|
90 100 110
....*....|....*....|....*....|...
gi 767157600 107 RNSISCIPQD------PTLfdgTVRSNLDPFDR 133
Cdd:NF033858 75 CPRIAYMPQGlgknlyPTL---SVFENLDFFGR 104
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-268 |
7.35e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.45 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIdNKDIKhiplerlrns 109
Cdd:COG0488 316 LELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTllkLLAGELEPDS---GTVKL-GETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDptlfdgtvRSNLDPfdrysdvqiygvlskvglieecdELSLISE--QEQPNFSSHKLRN---RFI----DLNT 180
Cdd:COG0488 380 IGYFDQH--------QEELDP-----------------------DKTVLDElrDGAPGGTEQEVRGylgRFLfsgdDAFK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 181 VVKSggsnLSQGQRQLLCLARSMLGARNIMLIDEAT-----ASIDYISDAkiqktiretMKNT--TILTIAH-R--LRSV 250
Cdd:COG0488 429 PVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTnhldiETLEALEEA---------LDDFpgTVLLVSHdRyfLDRV 495
|
250
....*....|....*...
gi 767157600 251 IdyDKILVMEMGRVKEYD 268
Cdd:COG0488 496 A--TRILEFEDGGVREYP 511
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
45-275 |
8.14e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 49.24 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 45 HSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIyrlsdweNGTIIIDNKDIKHIPLerLRNSISC---IPQD---PT 118
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIEL--LGRTVQRegrLARDirkSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 119 LFDGTVRSNLDPFDRYSDVQ--IYGVLSKVGLIEECdeLSLISEQEQPNFSSHKLRnrfIDLNTVVKSGGSNLSQGQRQL 196
Cdd:PRK09984 86 ANTGYIFQQFNLVNRLSVLEnvLIGALGSTPFWRTC--FSWFTREQKQRALQALTR---VGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 197 LCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN--TTILTIAHRLRSVIDY-DKILVMEMGRV--------- 264
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYcERIVALRQGHVfydgssqqf 240
|
250
....*....|...
gi 767157600 265 --KEYDHPYTLIS 275
Cdd:PRK09984 241 dnERFDHLYRSIN 253
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
65-268 |
9.00e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 65 IVGRTGAGKSSIIAAIYRLSDWENGTIIIDN-------KDIkHIPLERLRnsISCIPQDPTLFDG-TVRSNLDpfdrysd 136
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGI-CLPPEKRR--IGYVFQDARLFPHyKVRGNLR------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 137 vqiYGVlskvglieecdelsliSEQEQPNFSS-------HKLRNRFidlntvvksgGSNLSQGQRQLLCLARSMLGARNI 209
Cdd:PRK11144 99 ---YGM----------------AKSMVAQFDKivallgiEPLLDRY----------PGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 210 MLIDEATASID---------YISdaKIQKTIretmkNTTILTIAHRLRSVIDY-DKILVMEMGRVKEYD 268
Cdd:PRK11144 150 LLMDEPLASLDlprkrellpYLE--RLAREI-----NIPILYVSHSLDEILRLaDRVVVLEQGKVKAFG 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-214 |
9.06e-07 |
|
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: 50.18 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 4 VERIKEYTDIPSESNGYISPPANWPQTGDVELKNLSLRYSPHSSK---ALDNVSFKVKAGTKVGIVGRTGAGKSS---II 77
Cdd:COG4615 299 IEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTlakLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 78 AAIYRLSDwenGTIIIDNKDIKHIPLERLRNSISCIPQDPTLFDgtvrSNLDPFDRYSDVQIYGVLSKVGLieecdelsl 157
Cdd:COG4615 379 TGLYRPES---GEILLDGQPVTADNREAYRQLFSAVFSDFHLFD----RLLGLDGEADPARARELLERLEL--------- 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 158 iseqeqpnfsSHKLR---NRFIDLNtvvksggsnLSQGQRQLLCLARSMLGARNIMLIDE 214
Cdd:COG4615 443 ----------DHKVSvedGRFSTTD---------LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
52-264 |
1.55e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 52 NVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHI-PLERLRNSISCIPQD---PTLF-DGTVRS 126
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLARGLVYLPEDrqsSGLYlDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 127 NLdpfdrysdvqiygvlskVGLIEECDELSLISEQEQPNFSS--HKLRNRFIDLNTVVKSggsnLSQGQRQLLCLARSML 204
Cdd:PRK15439 361 NV-----------------CALTHNRRGFWIKPARENAVLERyrRALNIKFNHAEQAART----LSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767157600 205 GARNIMLIDEATASIDYISDAKIQKTIRETMK-NTTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
49-264 |
2.00e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 48.34 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIiidnkDIKHIPLERL--RNSISCIPQD-------PTL 119
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQAlqKNLVAYVPQSeevdwsfPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 120 FDgtvrsnldpfdrysDVQIYGVLSKVGLI---EECDELSLISEQEQPNFSSHklRNRFIdlntvvksggSNLSQGQRQL 196
Cdd:PRK15056 97 VE--------------DVVMMGRYGHMGWLrraKKRDRQIVTAALARVDMVEF--RHRQI----------GELSGGQKKR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 197 LCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETM-KNTTILTIAHRLRSVIDYDKILVMEMGRV 264
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-264 |
2.43e-06 |
|
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: 47.26 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 35 LKNLSLRYSPHSSKA--LDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIY-RLSDWE--NGTIIIDNKDIKHIPLERLRNS 109
Cdd:cd03233 6 WRNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnRTEGNVsvEGDIHYNGIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQD---PTLfdgTVRSNLDpfdrysdvqiygvlskvglieecdelsliseqeqpnFSSHKLRNRFIdlntvvksgg 186
Cdd:cd03233 86 IYVSEEDvhfPTL---TVRETLD------------------------------------FALRCKGNEFV---------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 SNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE---TMKNTTILTIAHRLRSVID-YDKILVMEMG 262
Cdd:cd03233 117 RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTmadVLKTTTFVSLYQASDEIYDlFDKVLVLYEG 196
|
..
gi 767157600 263 RV 264
Cdd:cd03233 197 RQ 198
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
33-272 |
4.09e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRY--SPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDwENGTIIIDNKDIKHIPLERL---- 106
Cdd:PRK15093 4 LDIRNLTIEFktSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLLRLspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 107 -----RNSISCIPQDPtlfdgtvRSNLDPFDRysdvqiygvlskVGlieecdeLSLIseQEQPNFSS--------HKLRN 173
Cdd:PRK15093 83 rrklvGHNVSMIFQEP-------QSCLDPSER------------VG-------RQLM--QNIPGWTYkgrwwqrfGWRKR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 174 RFIDL---------NTVVKSGGSNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN--TTILT 242
Cdd:PRK15093 135 RAIELlhrvgikdhKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767157600 243 IAHRLRSVIDY-DKILVMEMGRVKEY----------DHPYT 272
Cdd:PRK15093 215 ISHDLQMLSQWaDKINVLYCGQTVETapskelvttpHHPYT 255
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
33-98 |
6.07e-06 |
|
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: 46.66 E-value: 6.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 33 VELKNLSLRYSPHSSK--ALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIDNKDI 98
Cdd:COG4181 9 IELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTllgLLAGLDRPTS---GTVRLAGQDL 76
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
44-263 |
6.14e-06 |
|
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: 47.44 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 44 PHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKdikhiplerlrNSISCIPQDPTLFDGT 123
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 124 VRSNLDPFDRYSDVQIYGVLSKVgLIEECDELSL--ISEQEQpNFSShklrnrfidlntvVKSGGSNLSQGQRQLLCLAR 201
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKD-LEQILDNVQLthILEREG-GWSA-------------VQDWMDVLSGGEKQRIAMAR 595
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767157600 202 SMLGARNIMLIDEATASIDYISDAKIQKTIREtmKNTTILTIAHRlRSVIDYDKILvMEMGR 263
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR-KSLWKYHEYL-LYMDG 653
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
32-273 |
6.20e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 32 DVELKNLSLRY-SPHSSKaldNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHI-PLERlrnS 109
Cdd:PRK11000 3 SVTLRNVTKAYgDVVISK---DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVpPAER---G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLFdgtvrSNLDPFDRYSdvqiYGV-LSKVGLIEECDELSLISEQEQpnfSSHKLRNRFIDLntvvksggsn 188
Cdd:PRK11000 77 VGMVFQSYALY-----PHLSVAENMS----FGLkLAGAKKEEINQRVNQVAEVLQ---LAHLLDRKPKAL---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 189 lSQGQRQLLCLARSMLGARNIMLIDEATASID-------YISDAKIQKTIRETMKNTT-----ILTIAhrlrsvidyDKI 256
Cdd:PRK11000 135 -SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmRIEISRLHKRLGRTMIYVThdqveAMTLA---------DKI 204
|
250
....*....|....*..
gi 767157600 257 LVMEMGRVKEYDHPYTL 273
Cdd:PRK11000 205 VVLDAGRVAQVGKPLEL 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
33-270 |
1.48e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.09 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERlRNsISC 112
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDPTLFDG-TVRSNLdpfdrysdvqIYGV-LSKVGL--IEE--CDELSLISEQEqpnFSSHKLRnrfidlntvvksgg 186
Cdd:PRK09452 91 VFQSYALFPHmTVFENV----------AFGLrMQKTPAaeITPrvMEALRMVQLEE---FAQRKPH-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 187 sNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYisdaKIQKTIRETMK------NTTILTIAH-RLRSVIDYDKILVM 259
Cdd:PRK09452 144 -QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY----KLRKQMQNELKalqrklGITFVFVTHdQEEALTMSDRIVVM 218
|
250
....*....|.
gi 767157600 260 EMGRVKEYDHP 270
Cdd:PRK09452 219 RDGRIEQDGTP 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-220 |
8.43e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPHSskALDNVSFKVKAGTKVGIVGRTGAGKSS---IIAAIYRLSDwenGTIIIDnKDIKhiplerlrns 109
Cdd:PRK11147 4 ISIHGAWLSFSDAP--LLDNAELHIEDNERVCLVGRNGAGKSTlmkILNGEVLLDD---GRIIYE-QDLI---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTL-FDGTVrsnldpFDRYSDvqiyGVLSKVGLIEECDELSLISEQEQpnfsSHKLRNRF------ID----- 177
Cdd:PRK11147 68 VARLQQDPPRnVEGTV------YDFVAE----GIEEQAEYLKRYHDISHLVETDP----SEKNLNELaklqeqLDhhnlw 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 178 -----LNTVVKSGG-------SNLSQGQRQLLCLARSMLGARNIMLIDEATASID 220
Cdd:PRK11147 134 qlenrINEVLAQLGldpdaalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
43-264 |
8.60e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.24 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 43 SPHSSKALDNVSFKVK-------------AGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNS 109
Cdd:PRK10575 7 HSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 110 ISCIPQDPTLFDG-TVRSnLDPFDRYSdvqIYGVLSKVGLI--EECDE-LSLISEQeqpnfsshKLRNRFIDlntvvksg 185
Cdd:PRK10575 87 VAYLPQQLPAAEGmTVRE-LVAIGRYP---WHGALGRFGAAdrEKVEEaISLVGLK--------PLAHRLVD-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 186 gsNLSQGQRQLLCLArsMLGARN--IMLIDEATASIDYISD----AKIQKTIREtmKNTTILTIAHRLRSVIDY-DKILV 258
Cdd:PRK10575 147 --SLSGGERQRAWIA--MLVAQDsrCLLLDEPTSALDIAHQvdvlALVHRLSQE--RGLTVIAVLHDINMAARYcDYLVA 220
|
....*.
gi 767157600 259 MEMGRV 264
Cdd:PRK10575 221 LRGGEM 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
36-97 |
1.04e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.99 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767157600 36 KNLSLRYSPHssKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKD 97
Cdd:PRK11701 10 RGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD 69
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
48-77 |
1.23e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.15 E-value: 1.23e-04
10 20 30
....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSSII 77
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTI 65
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
48-116 |
1.31e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.31e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIK-HIPLERLRNSISCIPQD 116
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQE 81
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
48-220 |
1.50e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.17 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDI-----KHIPLerLRNSISCIPQD-PTLFD 121
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlknREVPF--LRRQIGMIFQDhHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 122 GTVRSNLD-PF----DRYSDV--QIYGVLSKVGLIEecdelsliseqeqpnfsshKLRNRFIdlntvvksggsNLSQGQR 194
Cdd:PRK10908 94 RTVYDNVAiPLiiagASGDDIrrRVSAALDKVGLLD-------------------KAKNFPI-----------QLSGGEQ 143
|
170 180
....*....|....*....|....*.
gi 767157600 195 QLLCLARSMLGARNIMLIDEATASID 220
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-93 |
2.32e-04 |
|
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: 42.61 E-value: 2.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767157600 20 YIsPPAnwPQTGD--VELKNLSLRYSphsSKAL-DNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIII 93
Cdd:TIGR03719 311 YI-PPG--PRLGDkvIEAENLTKAFG---DKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
35-246 |
2.86e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.09 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 35 LKNLSLRYSPHSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKhiplerlrnSISCIP 114
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---------KDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 115 QDPTLFDGTvRSNLDPFDRYSDVQIYGVLSKVGLIeECDELSLISEQEQpnfsshklrnrFIDLNTVVksggsnLSQGQR 194
Cdd:PRK13540 73 QKQLCFVGH-RSGINPYLTLRENCLYDIHFSPGAV-GITELCRLFSLEH-----------LIDYPCGL------LSSGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767157600 195 QLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRE-TMKNTTILTIAHR 246
Cdd:PRK13540 134 RQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-264 |
5.98e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 40.94 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSPhSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDNKDIKHIPLERLRNSISC 112
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQDP--TLFDGTVRSNLdpfdrysdvqIYGVLSkVGLIEECDElsliseqeqpnfssHKLRN--RFIDLNTVVKSGGSN 188
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDI----------AFGPIN-LGLDEETVA--------------HRVSSalHMLGLEELRDRVPHH 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKN--TTILTIAHRLRSVIDY-DKILVMEMGRV 264
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMaDYIYVMDKGRI 216
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-259 |
8.49e-04 |
|
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: 40.04 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 41 RYSPHSskaldnvsFK------VKAGTKVGIVGRTGAGKSS---IIAA-----IYRLSDWENGTIIIDN--KDIKHIPLE 104
Cdd:cd03236 9 RYGPNS--------FKlhrlpvPREGQVLGLVGPNGIGKSTalkILAGklkpnLGKFDDPPDWDEILDEfrGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 105 RLRN-SISCI--PQD----PTLFDGTVRSNLDPFDRYsdvqiyGVLSKVglieeCDELSLiseqeqpnfssHKLRNRFID 177
Cdd:cd03236 81 KLLEgDVKVIvkPQYvdliPKAVKGKVGELLKKKDER------GKLDEL-----VDQLEL-----------RHVLDRNID 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 178 lntvvksggsNLSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNT-TILTIAHRLrSVIDY--D 254
Cdd:cd03236 139 ----------QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDnYVLVVEHDL-AVLDYlsD 207
|
....*
gi 767157600 255 KILVM 259
Cdd:cd03236 208 YIHCL 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
48-74 |
9.09e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 9.09e-04
10 20
....*....|....*....|....*..
gi 767157600 48 KALDNVSFKVKAGTKVGIVGRTGAGKS 74
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKS 41
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
53-106 |
2.33e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.76 E-value: 2.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767157600 53 VSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWEnGTIIIDNKDIKHIPLERL 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAEL 67
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
57-253 |
2.73e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.02 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 57 VKAGTKVGIVGRTGAGKSSIIAAiyrLS--------------DWEN------GTIIID------NKDIK--HIPLErlrn 108
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKI---LSgelipnlgdyeeepSWDEvlkrfrGTELQNyfkklyNGEIKvvHKPQY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 109 siscIPQDPTLFDGTVRSNLDPFDRYsdvqiyGVLSKVglieeCDELSLiseqeqpnfssHKLRNRFIDlntvvksggsN 188
Cdd:PRK13409 169 ----VDLIPKVFKGKVRELLKKVDER------GKLDEV-----VERLGL-----------ENILDRDIS----------E 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767157600 189 LSQGQRQLLCLARSMLGARNIMLIDEATASIDYISDAKIQKTIRETMKNTTILTIAHRLrSVIDY 253
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDY 276
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-74 |
3.12e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767157600 20 YIsPPAnwPQTGD--VELKNLSLRYSphsSKAL-DNVSFKVKAGTKVGIVGRTGAGKS 74
Cdd:PRK11819 313 FI-PPG--PRLGDkvIEAENLSKSFG---DRLLiDDLSFSLPPGGIVGIIGPNGAGKS 364
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
61-80 |
4.11e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 38.21 E-value: 4.11e-03
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-98 |
4.24e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 24 PANWPQTGDV--ELKNLSLRYSPHSS-KALDNVSFKVKAGTKVGIVGRTGAGKS----SIIAAIY--RLSdwenGTIIID 94
Cdd:NF040905 247 PERTPKIGEVvfEVKNWTVYHPLHPErKVVDDVSLNVRRGEIVGIAGLMGAGRTelamSVFGRSYgrNIS----GTVFKD 322
|
....
gi 767157600 95 NKDI 98
Cdd:NF040905 323 GKEV 326
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
33-220 |
5.86e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 37.40 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 33 VELKNLSLRYSphSSKALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIIIDnkdikhiplERLRnsISC 112
Cdd:PRK09544 5 VSLENVSVSFG--QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 113 IPQ----DPTLfDGTVRS--NLDPFDRYSDvqIYGVLSKVglieecDELSLISEQEQpnfsshklrnrfidlntvvksgg 186
Cdd:PRK09544 72 VPQklylDTTL-PLTVNRflRLRPGTKKED--ILPALKRV------QAGHLIDAPMQ----------------------- 119
|
170 180 190
....*....|....*....|....*....|....
gi 767157600 187 sNLSQGQRQLLCLARSMLGARNIMLIDEATASID 220
Cdd:PRK09544 120 -KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
49-267 |
6.95e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.95 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 49 ALDNVSFKVKAGTKVGIVGRTGAGKSSIIAAIYRLSDWENGTIiidnkDIKhiplerlrNSISCIpqdptlfdgTVRSNL 128
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIK--------GSAALI---------AISSGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767157600 129 DpfdrysdvqiyGVLSKVGLIEECDELSLISEQEQPNFSSHKLrnRFIDLNTVVKSGGSNLSQGQRQLLCLARSMLGARN 208
Cdd:PRK13545 97 N-----------GQLTGIENIELKGLMMGLTKEKIKEIIPEII--EFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767157600 209 IMLIDEATASIDYISDAKIQKTIRETMKN-TTILTIAHRLRSVIDY-DKILVMEMGRVKEY 267
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFcTKALWLHYGQVKEY 224
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
62-80 |
9.45e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.29 E-value: 9.45e-03
|
| |
