|
Name |
Accession |
Description |
Interval |
E-value |
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-181 |
7.59e-103 |
|
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: 295.56 E-value: 7.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:cd03244 10 LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F-------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:cd03244 90 FsgtirsnldpfgeysdeelwqalervglkefVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP 181
Cdd:cd03244 170 VDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-181 |
4.09e-77 |
|
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: 229.99 E-value: 4.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:cd03369 14 VRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 FIMKLPEKLQA-------------EVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK 147
Cdd:cd03369 94 FSGTIRSNLDPfdeysdeeiygalRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT 173
|
170 180 190
....*....|....*....|....*....|....
gi 2004190228 148 GCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP 181
Cdd:cd03369 174 NSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-193 |
2.05e-76 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 249.27 E-value: 2.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:PLN03130 1245 LRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F-------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:PLN03130 1325 FsgtvrfnldpfnehndadlweslerahlkdvIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFA 193
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-201 |
2.19e-69 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 221.19 E-value: 2.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:COG1132 348 SYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:COG1132 427 sgtirenirygrpdatdeeveeaakaaqahefIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKpDSAFAMLLAAEVR 201
Cdd:COG1132 507 LDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQFG 577
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-187 |
3.39e-68 |
|
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: 225.60 E-value: 3.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F-------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:TIGR00957 1372 FsgslrmnldpfsqysdeevwwalelahlktfVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP-EVLAEK 187
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPsNLLQQR 1510
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-174 |
1.87e-67 |
|
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: 204.15 E-value: 1.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:cd03228 9 SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 imklpeklqaevteNG---EN-FSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHR 157
Cdd:cd03228 89 --------------SGtirENiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHR 154
|
170
....*....|....*..
gi 2004190228 158 LNTVLNCDHVLVMENGK 174
Cdd:cd03228 155 LSTIRDADRIIVLDDGR 171
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-196 |
6.83e-67 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 222.16 E-value: 6.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F-------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:PLN03232 1322 FsgtvrfnidpfsehndadlwealerahikdvIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAMLL 196
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-187 |
4.19e-66 |
|
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: 215.47 E-value: 4.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:COG2274 482 RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:COG2274 562 sgtirenitlgdpdatdeeiieaarlaglhdfIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 187
Cdd:COG2274 642 LDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-187 |
7.21e-65 |
|
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: 199.37 E-value: 7.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 5 DNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF--- 81
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFsgt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -----------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:cd03254 93 imenirlgrpnatdeevieaakeagahdfIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 133 KTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 187
Cdd:cd03254 173 ETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-199 |
3.03e-62 |
|
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: 193.97 E-value: 3.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:cd03288 27 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F-------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:cd03288 107 FsgsirfnldpeckctddrlwealeiaqlknmVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAE 199
Cdd:cd03288 187 IDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-187 |
6.43e-61 |
|
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: 198.83 E-value: 6.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:COG4988 345 SYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:COG4988 424 agtirenlrlgrpdasdeeleaaleaagldefVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 187
Cdd:COG4988 504 LDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-187 |
1.10e-57 |
|
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: 181.66 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF- 81
Cdd:cd03253 10 YDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:cd03253 89 dtigynirygrpdatdeevieaakaaqihdkIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2004190228 131 DSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 187
Cdd:cd03253 169 DTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-198 |
1.24e-57 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 195.38 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:PTZ00243 1316 MRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F------------------------IMKLPEKLQAE-------VTENGENFSVGERQLLCVARALL-RNSKIILLDEATA 128
Cdd:PTZ00243 1396 FdgtvrqnvdpfleassaevwaaleLVGLRERVASEsegidsrVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATA 1475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 129 SMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAA 198
Cdd:PTZ00243 1476 NIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-177 |
4.43e-57 |
|
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: 180.04 E-value: 4.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL--------- 80
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLfdgtiaeni 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 -----------------------FIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTL 137
Cdd:cd03249 98 rygkpdatdeeveeaakkanihdFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2004190228 138 VQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:cd03249 178 VQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-177 |
1.32e-54 |
|
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: 173.57 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:cd03251 89 ndtvaeniaygrpgatreeveeaaraanahefIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:cd03251 169 LDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-177 |
6.59e-52 |
|
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: 175.78 E-value: 6.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF-------- 81
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFndtiayni 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTL 137
Cdd:COG5265 453 aygrpdaseeeveaaaraaqihdfIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2004190228 138 VQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:COG5265 533 IQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-188 |
8.44e-52 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 174.95 E-value: 8.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:COG4987 342 RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:COG4987 422 dttlrenlrlarpdatdeelwaalervglgdwLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKP 188
Cdd:COG4987 502 LDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-177 |
1.07e-50 |
|
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: 163.81 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL- 80
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 -------------------------------FIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:cd03252 89 nrsirdnialadpgmsmervieaaklagahdFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-177 |
1.31e-48 |
|
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: 166.43 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:TIGR02203 339 RYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ---------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATA 128
Cdd:TIGR02203 419 ndtianniaygrteqadraeieralaaayaqdfVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 129 SMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-198 |
7.00e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 153.96 E-value: 7.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 5 DNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL---- 80
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLfnrs 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 ----------------------------FIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK13657 425 iednirvgrpdatdeemraaaeraqahdFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 133 KTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE---FDkpEVLAEkpDSAFAMLLAA 198
Cdd:PRK13657 505 ETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFD--ELVAR--GGRFAALLRA 569
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-175 |
7.44e-41 |
|
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: 136.58 E-value: 7.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 imklpeklQAEVTENgeNFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDA-FKGCTVLTIAHRLNT 160
Cdd:cd03246 89 --------SGSIAEN--ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPET 158
|
170
....*....|....*
gi 2004190228 161 VLNCDHVLVMENGKV 175
Cdd:cd03246 159 LASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-177 |
1.70e-40 |
|
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: 135.90 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSlEDLRTKLTVIPQDPVLFI 82
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 83 MKLPEKLqaevtenGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVL 162
Cdd:cd03247 89 TTLRNNL-------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE 161
|
170
....*....|....*
gi 2004190228 163 NCDHVLVMENGKVIE 177
Cdd:cd03247 162 HMDKILFLENGKIIM 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-174 |
4.49e-40 |
|
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: 133.91 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQdpvlf 81
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 imklpeklqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAF-KGCTVLTIAHRLNT 160
Cdd:cd00267 81 ------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPEL 142
|
170
....*....|....*
gi 2004190228 161 VLN-CDHVLVMENGK 174
Cdd:cd00267 143 AELaADRVIVLKDGK 157
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-195 |
4.93e-39 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 140.54 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF--------- 81
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFndtiannia 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTL 137
Cdd:PRK11176 439 yarteqysreqieeaarmayamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERA 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 138 VQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKpDSAFAML 195
Cdd:PRK11176 519 IQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQL 575
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
8-197 |
1.91e-38 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 140.08 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 8 PLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF------ 81
Cdd:TIGR03796 492 PPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFegtvrd 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 135
Cdd:TIGR03796 572 nltlwdptipdadlvrackdaaihdvITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 136 TLVQNTIKDafKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPdSAFAMLLA 197
Cdd:TIGR03796 652 KIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG-GAYARLIR 710
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-176 |
2.09e-38 |
|
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: 131.56 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:cd03245 11 SYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------------------IM-------------KLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:cd03245 91 ygtlrdnitlgapladderILraaelagvtdfvnKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVI 176
Cdd:cd03245 171 MDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-195 |
1.15e-37 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 137.55 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 4 RDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL--- 80
Cdd:TIGR00958 491 RPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLfsg 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 -----------------------------FIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:TIGR00958 570 svreniaygltdtpdeeimaaakaanahdFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 132 SKTDTLVQNTIKdaFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAML 195
Cdd:TIGR00958 650 AECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-170 |
9.82e-37 |
|
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: 133.95 E-value: 9.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL 80
Cdd:TIGR02857 329 VAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F--------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATA 128
Cdd:TIGR02857 408 FagtiaenirlarpdasdaeirealeragldefVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2004190228 129 SMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVM 170
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-179 |
1.58e-36 |
|
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: 128.43 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:cd03289 11 KYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:cd03289 90 sgtfrknldpygkwsdeeiwkvaeevglksvIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 131 DSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFD 179
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-178 |
1.94e-36 |
|
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: 126.85 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQDP-------- 78
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPmsslnprm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -----------VLFIMKLPEKLQAEVTENGEN--------------FSVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:cd03257 100 tigeqiaeplrIHGKLSKKEARKEAVLLLLVGvglpeevlnrypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2004190228 134 TDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEF 178
Cdd:cd03257 180 VQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-177 |
1.27e-34 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 128.68 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL-- 80
Cdd:PRK10790 350 YRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVla 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 -----------------------------FIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PRK10790 429 dtflanvtlgrdiseeqvwqaletvqlaeLARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2004190228 132 SKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:PRK10790 509 SGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-175 |
2.07e-34 |
|
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: 121.42 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL-------- 80
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLfarslqdn 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 ------------------------FIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDT 136
Cdd:cd03248 108 iayglqscsfecvkeaaqkahahsFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 2004190228 137 LVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKV 175
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-200 |
4.14e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 127.27 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 5 DNTPLvLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL---- 80
Cdd:PRK11174 361 DGKTL-AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLphgt 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 ----------------------------FIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK11174 439 lrdnvllgnpdasdeqlqqalenawvseFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 133 KTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPdSAFAMLLAAEV 200
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLAHRQ 585
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-198 |
1.11e-33 |
|
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: 125.40 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQDP-------- 78
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPysslnprm 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -VLFIMKLPEKLQAEVTENGEN-----------------------FSVGERQLLCVARALLRNSKIILLDEATASMDSKT 134
Cdd:COG1123 360 tVGDIIAEPLRLHGLLSRAERRervaellervglppdladrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSV 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 135 DTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFA-MLLAA 198
Cdd:COG1123 440 QAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANPQHPYTrALLAA 507
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-176 |
1.82e-33 |
|
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: 117.54 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQdpVLF 81
Cdd:cd03214 8 GYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--ALE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 IMKLPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLN 159
Cdd:cd03214 84 LLGLAHLADRPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLN 159
|
170
....*....|....*...
gi 2004190228 160 TVLN-CDHVLVMENGKVI 176
Cdd:cd03214 160 LAARyADRVILLKDGRIV 177
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-186 |
3.10e-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: 124.48 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF-------- 81
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFdgtiaeni 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -----------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLV 138
Cdd:COG4618 427 arfgdadpekvvaaaklagvhemILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2004190228 139 QNTIKDAFK-GCTVLTIAHRLNTVLNCDHVLVMENGKVIEF-DKPEVLAE 186
Cdd:COG4618 507 AAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-179 |
5.36e-33 |
|
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: 124.64 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:TIGR01271 1226 KYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:TIGR01271 1305 sgtfrknldpyeqwsdeeiwkvaeevglksvIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 131 DSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFD 179
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-174 |
1.44e-32 |
|
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: 116.41 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP--- 78
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 ---------VLF---IMKLPEKLQAEVTENG--------------ENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:cd03225 88 ffgptveeeVAFgleNLGLPEEEIEERVEEAlelvgleglrdrspFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2004190228 133 KTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGK 174
Cdd:cd03225 168 AGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-174 |
2.32e-32 |
|
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: 114.98 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS--LEDLRTKLTVIPQDPVLFimklPE 87
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF----PH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 88 KlqaEVTEN-GENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN- 163
Cdd:cd03229 91 L---TVLENiALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARl 167
|
170
....*....|.
gi 2004190228 164 CDHVLVMENGK 174
Cdd:cd03229 168 ADRVVVLRDGK 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-177 |
1.25e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 119.93 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:PRK11160 347 TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ----------------------------IMKL---PEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:PRK11160 427 satlrdnlllaapnasdealievlqqvgLEKLledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2004190228 131 DSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-198 |
5.16e-31 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 113.36 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP----------- 78
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPyaslhprhtvd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -----VLFIMKLPEKlQAEVTEN------GENF--------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 139
Cdd:COG1124 100 rilaePLRIHGLPDR-EERIAELleqvglPPSFldryphqlSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 140 NTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFA-MLLAA 198
Cdd:COG1124 179 NLLKDlrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGPKHPYTrELLAA 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-175 |
1.34e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.06 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -----------------------------IMKLPEK-LQAEVtengENFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:COG4619 87 ggtvrdnlpfpfqlrerkfdreralelleRLGLPPDiLDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 132 SKTDTLVQNTIKDAF--KGCTVLTIAH------RLntvlnCDHVLVMENGKV 175
Cdd:COG4619 163 PENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
11-128 |
5.88e-30 |
|
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: 107.73 E-value: 5.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF--------- 81
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------IMKLPEKLQAE---------------VTENGENFSVGERQLLCVARALLRNSKIILLDEATA 128
Cdd:pfam00005 81 rlglllkgLSKREKDARAEealeklglgdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-201 |
8.74e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 8.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP-VL 80
Cdd:PRK13632 16 SYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPdNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 FI---------------MKLPEKLQAEVTENGE-------------NFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK13632 96 FIgatveddiafglenkKVPPKKMKDIIDDLAKkvgmedyldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 133 KTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP-EVLAEKP-------DSAFAMLLAAEVR 201
Cdd:PRK13632 176 KGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNKEilekakiDSPFIYKLSKKLK 254
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-158 |
2.26e-29 |
|
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: 113.61 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 4 RDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF-- 81
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:TIGR02868 424 tvrenlrlarpdatdeelwaalervgladwLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*..
gi 2004190228 132 SKTDTLVQNTIKDAFKGCTVLTIAHRL 158
Cdd:TIGR02868 504 AETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-188 |
2.56e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 113.65 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:PRK10789 402 sdtvannialgrpdatqqeiehvarlasvhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 130 MDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKP 188
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-184 |
2.94e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 108.98 E-value: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL- 80
Cdd:COG1120 10 GYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 ------------------FIMKLPEKLQAEVTE-----NGENF--------SVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:COG1120 88 fgltvrelvalgryphlgLFGRPSAEDREAVEEalertGLEHLadrpvdelSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 130 MDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVL 184
Cdd:COG1120 168 LDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-201 |
4.76e-29 |
|
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: 112.30 E-value: 4.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIFIDEVDICILSLEDLRTKLTVIPQDP 78
Cdd:COG1123 13 RYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 ---------------VLFIMKLP-EKLQAEVTENGEN-------------FSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:COG1123 93 mtqlnpvtvgdqiaeALENLGLSrAEARARVLELLEAvglerrldryphqLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 130 MDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE-------FDKPEVLAEKPDSAFAMLLAAE 199
Cdd:COG1123 173 LDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEdgppeeiLAAPQALAAVPRLGAARGRAAP 252
|
..
gi 2004190228 200 VR 201
Cdd:COG1123 253 AA 254
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-176 |
1.11e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 104.82 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQdpvlfimklpek 88
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 89 lqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASMDSK-TDTLVqNTIKD-AFKGCTVLTIAHRLNTVLN-CD 165
Cdd:cd03216 83 -----------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERLF-KVIRRlRAQGVAVIFISHRLDEVFEiAD 150
|
170
....*....|.
gi 2004190228 166 HVLVMENGKVI 176
Cdd:cd03216 151 RVTVLRDGRVV 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-172 |
1.34e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 106.27 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RY--RDNTPLVLDsLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL----------------------------------- 44
Cdd:PTZ00265 1174 RYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgm 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 45 -------------------VEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFIMK--------------------- 84
Cdd:PTZ00265 1253 knvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSiyenikfgkedatredvkrac 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 85 -----------LPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGC--TV 151
Cdd:PTZ00265 1333 kfaaidefiesLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTI 1412
|
250 260
....*....|....*....|.
gi 2004190228 152 LTIAHRLNTVLNCDHVLVMEN 172
Cdd:PTZ00265 1413 ITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-189 |
1.18e-25 |
|
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: 99.11 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQDP 78
Cdd:cd03261 9 SFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 VLF--------IM-------KLPEKLQAEVT---------ENGEN-----FSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:cd03261 87 ALFdsltvfenVAfplrehtRLSEEEIREIVlekleavglRGAEDlypaeLSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 130 MDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:cd03261 167 LDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-192 |
2.62e-25 |
|
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: 98.18 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEdlRTKLTVIPQDPVLF-------- 81
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFphmtvykn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -----IMKLPEKLQ--AEVTE-------------NGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNT 141
Cdd:cd03299 92 iayglKKRKVDKKEieRKVLEiaemlgidhllnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 142 IKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAF 192
Cdd:cd03299 172 LKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-176 |
4.37e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 97.19 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICiLSLEDLRTKLTVIPQDPVL 80
Cdd:cd03263 8 KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F-------------IMK-LPEKLQAEVTENGE--------------NFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:cd03263 87 FdeltvrehlrfyaRLKgLPKSEIKEEVELLLrvlgltdkankrarTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2004190228 133 KTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 176
Cdd:cd03263 167 ASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-174 |
6.56e-25 |
|
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: 96.38 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 7 TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIdevdicilsledlRTKLTVIPQDP-------- 78
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGSIAYVSQEPwiqngtir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 --VLF---------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKT- 134
Cdd:cd03250 84 enILFgkpfdeeryekvikacalepdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVg 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2004190228 135 DTLVQNTIKDAFKGC-TVLTIAHRLNTVLNCDHVLVMENGK 174
Cdd:cd03250 164 RHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-177 |
7.55e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 96.88 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQ---------- 76
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQhfnllssrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 -DPVLFIMKLPEKLQAEVTENGE-----------------NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLV 138
Cdd:cd03258 100 fENVALPLEIAGVPKAEIEERVLellelvgledkadaypaQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2004190228 139 QNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:cd03258 180 LALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-184 |
1.35e-24 |
|
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: 96.10 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIFIDEVDICILS--LEDLRTKLTVIPQDPVLFI 82
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 83 M---------------KLPEKLQAEVTE---------------NGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:cd03260 95 GsiydnvayglrlhgiKLKEELDERVEEalrkaalwdevkdrlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 133 KTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVL 184
Cdd:cd03260 175 ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-182 |
2.54e-24 |
|
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: 99.37 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIFIDEVDICILS---LEDLRTKLTVIPQDP--------- 78
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPfgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 ----------VLFI-MKLPEKLQ------AEV-----------TEngenFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:COG4172 381 vgqiiaeglrVHGPgLSAAERRArvaealEEVgldpaarhrypHE----FSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 131 D-SktdtlVQNTIKDAFK------GCTVLTIAHRLNTV--LnCDHVLVMENGKVIE-------FDKPE 182
Cdd:COG4172 457 DvS-----VQAQILDLLRdlqrehGLAYLFISHDLAVVraL-AHRVMVMKDGKVVEqgpteqvFDAPQ 518
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-177 |
7.93e-24 |
|
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: 95.89 E-value: 7.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIFIDEVDICILSLEDLRT----KLTVIPQDP---- 78
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDPmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -----VLFIMKLP---------EKLQAEVTE--------NGEN--------FSVGERQLLCVARALLRNSKIILLDEATA 128
Cdd:COG0444 100 npvmtVGDQIAEPlrihgglskAEARERAIEllervglpDPERrldrypheLSGGMRQRVMIARALALEPKLLIADEPTT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 129 SMdsktDTLVQ----NTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:COG0444 180 AL----DVTIQaqilNLLKDlqRELGLAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-192 |
2.41e-23 |
|
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: 93.13 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVlDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 81
Cdd:cd03295 9 RYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -----------IMKL----PEKLQAEVTE-------NGENF--------SVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:cd03295 88 phmtveenialVPKLlkwpKEKIRERADEllalvglDPAEFadryphelSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 132 SKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAF 192
Cdd:cd03295 168 PITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-186 |
4.10e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.46 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcilslEDLRTKLTVIPQ----- 76
Cdd:COG1121 15 SYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYVPQraevd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 --------DPVL--------FIMKLPEKLQAEVTE-----NGENF--------SVGERQLLCVARALLRNSKIILLDEAT 127
Cdd:COG1121 88 wdfpitvrDVVLmgrygrrgLFRRPSRADREAVDEalervGLEDLadrpigelSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 128 ASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVL-NCDHVLVMeNGKVIEFDKP-EVLAE 186
Cdd:COG1121 168 AGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPeEVLTP 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-176 |
6.72e-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: 91.44 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdiciLSLEDLRTKLTVIPQ----- 76
Cdd:cd03235 8 SYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQrrsid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 --------DPVL--------FIMKLPEKLQAEVTE-----NGENF--------SVGERQLLCVARALLRNSKIILLDEAT 127
Cdd:cd03235 81 rdfpisvrDVVLmglyghkgLFRRLSKADKAKVDEalervGLSELadrqigelSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 128 ASMDSKT-DTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMeNGKVI 176
Cdd:cd03235 161 AGVDPKTqEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-181 |
9.22e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 91.48 E-value: 9.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT------------ 69
Cdd:cd03256 9 TYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqigmifqqf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 70 ----KLTVI-----------PQDPVLFIM-KLPEKLQA-----------EVTENGENFSVGERQLLCVARALLRNSKIIL 122
Cdd:cd03256 88 nlieRLSVLenvlsgrlgrrSTWRSLFGLfPKEEKQRAlaalervglldKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 123 LDEATASMDSKTDTLVQNTIKDAF--KGCTVLTIAHRLNTVL-NCDHVLVMENGKVIeFDKP 181
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAReYADRIVGLKDGRIV-FDGP 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-189 |
5.18e-22 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 89.65 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQD 77
Cdd:COG1127 13 KSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 PVLF--------IM-------KLPEKLQAEVT---------ENGENF-----SVGERQLLCVARALLRNSKIILLDEATA 128
Cdd:COG1127 91 GALFdsltvfenVAfplrehtDLSEAEIRELVleklelvglPGAADKmpselSGGMRKRVALARALALDPEILLYDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 129 SMD----SKTDTLVQnTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:COG1127 171 GLDpitsAVIDELIR-ELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASDD 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-175 |
7.12e-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: 88.70 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIFIDEVDICILSLEDL----RTKLTVIPQDP------ 78
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFnllpdl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -----VLFIMKLPEKLQAEVTENGENF-----------------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDT 136
Cdd:cd03255 98 talenVELPLLLAGVPKKERRERAEELlervglgdrlnhypselSGGQQQRVAIARALANDPKIILADEPTGNLDSETGK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2004190228 137 LVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKV 175
Cdd:cd03255 178 EVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-179 |
1.13e-21 |
|
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: 87.96 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEdlRTKLTVIPQDPVLF 81
Cdd:cd03259 9 TYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------IMKLPEKLQA----EVTENGENF----------SVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:cd03259 85 phltvaeniafglkLRGVPKAEIRarvrELLELVGLEgllnryphelSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 134 TDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFD 179
Cdd:cd03259 165 LREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-182 |
4.27e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.76 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP--- 78
Cdd:PRK13635 14 RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 ---------VLFIMK--------LPEKLQAEVTE-NGENF--------SVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK13635 94 fvgatvqddVAFGLEnigvpreeMVERVDQALRQvGMEDFlnrephrlSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 133 KTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPE 182
Cdd:PRK13635 174 RGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-177 |
9.29e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 9.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT---KLTVIPQ----------- 76
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrQIGMIFQhfnllssrtvf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 DPVLFIMKL----PEKLQAEVTENGE-------------NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 139
Cdd:PRK11153 101 DNVALPLELagtpKAEIKARVTELLElvglsdkadrypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2004190228 140 NTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:PRK11153 181 ELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-177 |
1.12e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQD 77
Cdd:COG2884 9 KRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 P-----------VLFIMKL----PEKLQAEVTE---------NGENF----SVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:COG2884 88 FrllpdrtvyenVALPLRVtgksRKEIRRRVREvldlvglsdKAKALphelSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 130 MDSKTdtlvQNTIKDAFK-----GCTVLtIA-HRLNTVLNCDH-VLVMENGKVIE 177
Cdd:COG2884 168 LDPET----SWEIMELLEeinrrGTTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-188 |
1.24e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 89.32 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 14 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI-DEVDICILSLEDLRTKLTVIPQDPVLF----------- 81
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFsnsiknnikys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ------------------------------------------------------------------------------IM 83
Cdd:PTZ00265 484 lyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdvskkvlihdfVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 84 KLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDaFKGC---TVLTIAHRLNT 160
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN-LKGNenrITIIIAHRLST 642
|
250 260
....*....|....*....|....*...
gi 2004190228 161 VLNCDHVLVMENGKVIEFDKPEVLAEKP 188
Cdd:PTZ00265 643 IRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-177 |
1.80e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.06 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT---KLTVIPQDPVLF----- 81
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarrKIGMIFQHFNLLssrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ---------IMKLP-EKLQAEVTE---------NGENF----SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLV 138
Cdd:COG1135 100 aenvalpleIAGVPkAEIRKRVAEllelvglsdKADAYpsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2004190228 139 QNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:COG1135 180 LDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-176 |
2.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 5 DNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS-LEDLRTKLTVIPQDP----V 79
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqiV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LFIMK------------LPEKLQAEVTENGEN-------------FSVGERQLLCVARALLRNSKIILLDEATASMDSKT 134
Cdd:PRK13633 100 ATIVEedvafgpenlgiPPEEIRERVDESLKKvgmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2004190228 135 DTLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDHVLVMENGKVI 176
Cdd:PRK13633 180 RREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-182 |
9.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.27 E-value: 9.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS-LEDLRTKLTVIPQDP-VL 80
Cdd:PRK13644 11 YPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 FIMKL--------PEKLQAEVTE--------------------NGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK13644 90 FVGRTveedlafgPENLCLPPIEirkrvdralaeiglekyrhrSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 133 KTDTLVQNTIKDAF-KGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPE 182
Cdd:PRK13644 170 DSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-186 |
1.31e-19 |
|
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: 82.87 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQDPVLF------- 81
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFpeltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -----IMKLPEKLQAEVTEN---------------GENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNT 141
Cdd:cd03224 95 nlllgAYARRRAKRKARLERvyelfprlkerrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2004190228 142 IKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAE 186
Cdd:cd03224 175 IRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-175 |
2.08e-19 |
|
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: 82.19 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS--LEDLRTKLTVIPQDPVLF------ 81
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKknINELRQKVGMVFQQFNLFphltvl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --IMKLPEKLQ----AEVTENGENF-----------------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLV 138
Cdd:cd03262 95 enITLAPIKVKgmskAEAEERALELlekvgladkadaypaqlSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEV 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 2004190228 139 QNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKV 175
Cdd:cd03262 175 LDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-157 |
3.05e-19 |
|
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: 80.66 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdicilsledlRTKLTVIPQDPVLFIMKLPEK 88
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQRPYLPLGTLREQ 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 89 LqaeVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAfkGCTVLTIAHR 157
Cdd:cd03223 84 L---IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-177 |
3.72e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS-LEDLRTKLTVIPQDPVL-------- 80
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLvpnlsvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 --FIMKLP-------------------EKLQAEV--TENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSK-TDT 136
Cdd:COG1129 99 niFLGREPrrgglidwramrrrarellARLGLDIdpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVER 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2004190228 137 L--VQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:COG1129 179 LfrIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-175 |
4.44e-19 |
|
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: 81.30 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 6 NTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIL---SLEDLRTKLTVIPQD----- 77
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQDfrllp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 ------PVLFIMKLPEKLQAEVTEN-----------------GENFSVGERQLLCVARALLRNSKIILLDEATASMDSKT 134
Cdd:cd03292 92 drnvyeNVAFALEVTGVPPREIRKRvpaalelvglshkhralPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2004190228 135 DTLVQNTIKDAFK-GCTVLTIAHRLNTVLNCDH-VLVMENGKV 175
Cdd:cd03292 172 TWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-202 |
4.61e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID--EVDICILSLEDLRTKLTVIPQDP- 78
Cdd:PRK13636 14 NYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkPIDYSRKGLMKLRESVGMVFQDPd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -VLFI-------------MKLPEKlqaEVTENGEN-----------------FSVGERQLLCVARALLRNSKIILLDEAT 127
Cdd:PRK13636 93 nQLFSasvyqdvsfgavnLKLPED---EVRKRVDNalkrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 128 ASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTV-LNCDHVLVMENGKVI-EFDKPEVLAEKpdsafAMLLAAEVRL 202
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVIlQGNPKEVFAEK-----EMLRKVNLRL 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-190 |
5.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP--- 78
Cdd:PRK13648 16 QYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -VLFIMK-----------LP-EKLQAEVTENGEN-------------FSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK13648 96 fVGSIVKydvafglenhaVPyDEMHRRVSEALKQvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 133 KTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDS 190
Cdd:PRK13648 176 DARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-176 |
1.72e-18 |
|
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: 79.13 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIFIDEVDiciLSLEDLRTKLTVIPQDPVLF------ 81
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHptltvr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -IMKLPEKLQaevtengeNFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLN 159
Cdd:cd03213 101 eTLMFAAKLR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPS 172
|
170
....*....|....*....
gi 2004190228 160 TVL--NCDHVLVMENGKVI 176
Cdd:cd03213 173 SEIfeLFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-186 |
2.17e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.86 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC--ILSLEDLRTKLTVIPQD 77
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 P--VLF---IMK----------LPE--------------KLQAEVTENGENF--SVGERQLLCVARALLRNSKIILLDEA 126
Cdd:PRK13637 92 PeyQLFeetIEKdiafgpinlgLSEeeienrvkramnivGLDYEDYKDKSPFelSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 127 TASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAE 186
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPrEVFKE 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-173 |
2.88e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.16 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 5 DNTPLVlDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIFI-DEVDICILS------LEDLRTKLTV 73
Cdd:COG4178 374 DGRPLL-EDLSLSLKPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIARpAGARVLFLPqrpylpLGTLREALLY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 74 iPQDP----------VLFIMKLP---EKLQAEvtENGEN-FSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 139
Cdd:COG4178 449 -PATAeafsdaelreALEAVGLGhlaERLDEE--ADWDQvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
170 180 190
....*....|....*....|....*....|....
gi 2004190228 140 NTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENG 173
Cdd:COG4178 526 QLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-187 |
2.06e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL--------- 80
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpegitvrel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 ----------FIMKLPEKLQAEVTENGE-------------NFSVGERQLLCVARALLRNSKIILLDEATASMD-SKTDT 136
Cdd:PRK11231 97 vaygrspwlsLWGRLSAEDNARVNQAMEqtrinhladrrltDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDiNHQVE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 137 LVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAEK 187
Cdd:PRK11231 177 LMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPeEVMTPG 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-173 |
2.86e-17 |
|
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: 76.70 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID----EVDIC------ILsleDLRTK--------L 71
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAqaspreIL---ALRRRtigyvsqfL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 TVIPQDPVLFI-------------------------MKLPEKL--QAEVTengenFSVGERQLLCVARALLRNSKIILLD 124
Cdd:COG4778 103 RVIPRVSALDVvaepllergvdreearararellarLNLPERLwdLPPAT-----FSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 125 EATASMDSKTDTLVQNTIKDAfK--GCTVLTIAHRLNTVLN-CDHVLVMENG 173
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEA-KarGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-176 |
3.17e-17 |
|
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: 76.71 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFIDEVDICILSLEDL------RT--------KL 71
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLPPHEIarlgigRTfqiprlfpEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 TVI--------PQDPVLFIMKLPEKLQAEVTENGE-----------------NFSVGERQLLCVARALLRNSKIILLDEA 126
Cdd:cd03219 91 TVLenvmvaaqARTGSGLLLARARREEREARERAEellervgladladrpagELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 127 TASMDSK-TDTLVqNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 176
Cdd:cd03219 171 AAGLNPEeTEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-200 |
3.22e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQDPVLFI----- 82
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYASLdprqt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 83 --MKLPEKLQAEVTENGE-------------------------NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 135
Cdd:PRK10261 420 vgDSIMEPLRVHGLLPGKaaaarvawllervgllpehawryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 136 TLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDH-VLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 200
Cdd:PRK10261 500 GQIINLLLDLQRdfGIAYLFISHDMAVVERISHrVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-173 |
3.76e-17 |
|
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: 76.22 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTK----LTVIPQDPVLF----- 81
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLnatve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSK-T 134
Cdd:cd03290 97 enitfgspfnkqrykavtdacslqpdIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2004190228 135 DTLVQNTIKDAFKG--CTVLTIAHRLNTVLNCDHVLVMENG 173
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-175 |
3.87e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 75.16 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 7 TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQDP--VLFIM 83
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRkrEGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 84 KLPeklqaeVTEN---GENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLN 159
Cdd:cd03215 92 DLS------VAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRElADAGKAVLLISSELD 165
|
170
....*....|....*..
gi 2004190228 160 TVLN-CDHVLVMENGKV 175
Cdd:cd03215 166 ELLGlCDRILVMYEGRI 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-176 |
7.54e-17 |
|
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: 75.48 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDN--TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEdLRTKLTVIPQDPV 79
Cdd:cd03266 10 RFRDVkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LF--------------------------IMKLPEKLQAEVTEN--GENFSVGERQLLCVARALLRNSKIILLDEATASMd 131
Cdd:cd03266 89 LYdrltarenleyfaglyglkgdeltarLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 132 sktDTLVQNTIKDAFK-----GCTVLTIAHRLNTVLN-CDHVLVMENGKVI 176
Cdd:cd03266 168 ---DVMATRALREFIRqlralGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-177 |
9.00e-17 |
|
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: 75.20 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTP--LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICilsleDLRTKLTVIPQDP 78
Cdd:cd03293 8 KTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 VLF----IMK---LPEKLQ----AEVTENGENF-----------------SVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:cd03293 83 ALLpwltVLDnvaLGLELQgvpkAEARERAEELlelvglsgfenayphqlSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 131 DSKTDTLVQNTIKDAFK--GCTVLTIAHRLN-TVLNCDHVLVMEN--GKVIE 177
Cdd:cd03293 163 DALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-177 |
3.30e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIFIDEVDICILS---LEDLRTKLTVIPQDP-------- 78
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -VLFIMKlpEKLQ-------------------AEVTENGEN-------FSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PRK15134 380 nVLQIIE--EGLRvhqptlsaaqreqqviavmEEVGLDPETrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 132 sKTdtlVQNTIKDAFKG------CTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:PRK15134 458 -KT---VQAQILALLKSlqqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-186 |
5.33e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.61 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI----DEVD---------------ICILSLE-DLRTK 70
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDmtkpgpdgrgrakryIGILHQEyDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 71 LTVIPQDPVLFIMKLPEKL---QAEVT--------ENGEN--------FSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELarmKAVITlkmvgfdeEKAEEildkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 132 SKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAE 186
Cdd:TIGR03269 460 PITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPeEIVEE 518
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-189 |
7.00e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 72.96 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSL-EDLRTKLTVIPQDPVLF------- 81
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrkltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------IMKLPEKLQAEVTE--------------NGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQN 140
Cdd:cd03218 95 nilavleIRGLSKKEREEKLEelleefhithlrksKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 141 TIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:cd03218 175 IIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-182 |
7.99e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 73.15 E-value: 7.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFIDEVDICILSLEDL------RT--------KL 71
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDITGLPPHRIarlgiaRTfqnprlfpEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 TVI-------------PQDPVLFIMKLPEKLQAEVTENGE-----------------NFSVGERQLLCVARALLRNSKII 121
Cdd:COG0411 95 TVLenvlvaaharlgrGLLAALLRLPRARREEREARERAEellervgladradepagNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 122 LLDEATASMDSK-TDTLVQ--NTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 182
Cdd:COG0411 175 LLDEPAAGLNPEeTEELAEliRRLRDER-GITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-202 |
9.30e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.99 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 14 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIFIDEVDICILS---LEDLRT-KLTVIPQDPVLFI---M 83
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPMTSLnpyM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 84 KLPEKL-----------QAEVTENG--------------------ENFSVGERQLLCVARALLRNSKIILLDEATASMD- 131
Cdd:PRK09473 115 RVGEQLmevlmlhkgmsKAEAFEESvrmldavkmpearkrmkmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDv 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 132 ---SKTDTLVqNTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFAM-LLAAEVRL 202
Cdd:PRK09473 195 tvqAQIMTLL-NELKREF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPYSIgLLNAVPRL 268
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-184 |
1.01e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.23 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDN-TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP-- 78
Cdd:PRK13650 13 KYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 ----------VLFIMK---LPEKLQAEVTENGENF--------------SVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PRK13650 93 qfvgatveddVAFGLEnkgIPHEEMKERVNEALELvgmqdfkereparlSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 132 SKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVL 184
Cdd:PRK13650 173 PEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-182 |
1.24e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.11 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP----------V 79
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTslsfefdvrqV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LFIMKLPEKLQ-AEVTENGE---------------------NFSVGERQLLCVARALLRNSKIILLDEATASMD----SK 133
Cdd:PRK09536 98 VEMGRTPHRSRfDTWTETDRaaveramertgvaqfadrpvtSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhqVR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2004190228 134 TDTLVQNTIKDafkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 182
Cdd:PRK09536 178 TLELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPA 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-187 |
1.83e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSL-EDLRTKLTVIPQDPVLF------- 81
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFrrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ----IMKLPEKLQAEVTEN------------------GENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 139
Cdd:PRK10895 98 nlmaVLQIRDDLSAEQREDranelmeefhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 140 NTIKDAF-KGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAEK 187
Cdd:PRK10895 178 RIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPtEILQDE 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-189 |
1.91e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.75 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTP---LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdiCILS-------LEDLRTKL 71
Cdd:PRK13634 11 RYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE---RVITagkknkkLKPLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 TVIPQDP--VLFimklPEKLQAEVTENGENFSVGERQLLCVARALLR--------------------------------N 117
Cdd:PRK13634 88 GIVFQFPehQLF----EETVEKDICFGPMNFGVSEEDAKQKAREMIElvglpeellarspfelsggqmrrvaiagvlamE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 118 SKIILLDEATASMDSKTdtlvQNTIKDAF------KGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-188 |
2.65e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.14 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 15 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLR-----------TKLTVIPQDPVL--- 80
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTVLdnt 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 -FIMKLPEKLQAEVTENG---------ENF--------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTI 142
Cdd:PRK10070 128 aFGMELAGINAEERREKAldalrqvglENYahsypdelSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 143 K--DAFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKP 188
Cdd:PRK10070 208 VklQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-177 |
2.85e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 71.66 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFIDEVDIcilslEDLRTKLTVIPQDPVLF---- 81
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPV-----TGPGPDRGVVFQEPALLpwlt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ----------IMKLPEKLQAEVTEN-----G-ENF--------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTL 137
Cdd:COG1116 97 vldnvalgleLRGVPKAERRERAREllelvGlAGFedayphqlSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2004190228 138 VQNTIKDAFK--GCTVLTIAH------RLntvlnCDHVLVMEN--GKVIE 177
Cdd:COG1116 177 LQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-177 |
4.21e-15 |
|
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: 70.25 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQDPVlfimKLP 86
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPP----EIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 87 E-KLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAH--RLNTVL 162
Cdd:cd03217 91 GvKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYI 170
|
170
....*....|....*
gi 2004190228 163 NCDHVLVMENGKVIE 177
Cdd:cd03217 171 KPDRVHVLYDGRIVK 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-179 |
4.83e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRL----VEPASGTIFI-DEVDICILS--LEDLRTKLTVI------- 74
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKLgETVKIGYFDqhQEELDPDKTVLdelrdga 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 75 PQDPVLFIMKL-------PEKLQAEVtengENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDaFK 147
Cdd:COG0488 405 PGGTEQEVRGYlgrflfsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FP 479
|
170 180 190
....*....|....*....|....*....|....*
gi 2004190228 148 GcTVLTIAH-R--LNTVlnCDHVLVMENGKVIEFD 179
Cdd:COG0488 480 G-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-184 |
5.74e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.96 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL-F------- 81
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFpftveev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------IMKLPEK--LQAEVTENGENF----SVGERQLLCVARALLRNS------KIILLDEATASMD---- 131
Cdd:PRK13548 97 vamgraphglsraeDDALVAAalAQVDLAHLAGRDypqlSGGEQQRVQLARVLAQLWepdgppRWLLLDEPTSALDlahq 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 132 SKTDTLVQNTIKDAfkGCTVLTIAHRLN-TVLNCDHVLVMENGKVIEFDKP-EVL 184
Cdd:PRK13548 177 HHVLRLARQLAHER--GLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPaEVL 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-200 |
6.11e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 71.72 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSL-----GmalfrLVEPASGTIFIDEVDICI-LSLEDLRTKLtvIPQDPVLF-- 81
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLlriiaG-----LETPDSGRIVLNGRDLFTnLPPRERRVGF--VFQHYALFph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ------------IMKLPEK-LQAEVTE-----NGENF--------SVGERQLLCVARALLRNSKIILLDEATASMDSK-T 134
Cdd:COG1118 90 mtvaeniafglrVRPPSKAeIRARVEEllelvQLEGLadrypsqlSGGQRQRVALARALAVEPEVLLLDEPFGALDAKvR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 135 DTLVQNTIK--DAFKGcTVLTIAH------RLntvlnCDHVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 200
Cdd:COG1118 170 KELRRWLRRlhDELGG-TTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV 237
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-189 |
6.99e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 70.40 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL-RTKLTVIPQDPVLF------- 81
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFpsltvee 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------IMKLPEKLQAEVTENGENF--------------SVGERQLLCVARALLRNSKIILLDEATASMDSKtdtLVQN 140
Cdd:COG0410 98 nlllgayARRDRAEVRADLERVYELFprlkerrrqragtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPL---IVEE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 141 ------TIKDAfkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:COG0410 175 ifeiirRLNRE--GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-185 |
1.10e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS-LEDLRTKLTVIPQDPVLF------- 81
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFpnlsvke 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --IMKLP------EKLQAEVTENGENFS---------VGERQLLCVARALLRNSKIILLDEATASMD-SKTDTLVQNTIK 143
Cdd:PRK15439 106 niLFGLPkrqasmQKMKQLLAALGCQLDldssagsleVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRIRE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 144 DAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI------EFDKPEVLA 185
Cdd:PRK15439 186 LLAQGVGIVFISHKLPEIRQlADRISVMRDGTIAlsgktaDLSTDDIIQ 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-177 |
1.10e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT---KLTVIPQDP-------- 78
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSisavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 ---------------------------VLFIMKLPE----KLQAEVtengenfSVGERQLLCVARALLRNSKIILLDEAT 127
Cdd:PRK10419 107 tvreiireplrhllsldkaerlaraseMLRAVDLDDsvldKRPPQL-------SGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2004190228 128 asmdSKTDTLVQNTIKDAFK------GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:PRK10419 180 ----SNLDLVLQAGVIRLLKklqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-173 |
1.26e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID-------------EVDICILSLEdlrtkLTVIPQD 77
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhklaaQLGIGIIYQE-----LSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 PV---LFIMKLPEK-------------------------LQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:PRK09700 96 TVlenLYIGRHLTKkvcgvniidwremrvraammllrvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2004190228 130 M-DSKTDTL--VQNTIKDAFKGctVLTIAHRLNTVLN-CDHVLVMENG 173
Cdd:PRK09700 176 LtNKEVDYLflIMNQLRKEGTA--IVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-189 |
1.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPLV---LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICI----LSLEDLRTKLTVIP 75
Cdd:PRK13641 12 YSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLKKLRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 76 QDP--VLF-------IMKLPEKLQAEVTENGE---------------------NFSVGERQLLCVARALLRNSKIILLDE 125
Cdd:PRK13641 92 QFPeaQLFentvlkdVEFGPKNFGFSEDEAKEkalkwlkkvglsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 126 ATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-177 |
1.42e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 12 DSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTK---LTVIPQDPV--------- 79
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLaslnprmti 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 ---------LFIMKLP-----EKLQAEVTENG----------ENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 135
Cdd:PRK15079 118 geiiaeplrTYHPKLSrqevkDRVKAMMLKVGllpnlinrypHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2004190228 136 TLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:PRK15079 198 AQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-174 |
1.42e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 67.47 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdicilsledlRTKLTVIPQdpvlfimklpek 88
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFEQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 89 lqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDaFKGcTVLTIAH-R--LNTVlnCD 165
Cdd:cd03221 71 -----------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE-YPG-TVILVSHdRyfLDQV--AT 135
|
....*....
gi 2004190228 166 HVLVMENGK 174
Cdd:cd03221 136 KIIELEDGK 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-196 |
1.50e-14 |
|
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: 71.52 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 8 PLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI---------------DEVDICIL---SLEDLRT 69
Cdd:TIGR00957 651 PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMkgsvayvpqqawiqnDSLRENILfgkALNEKYY 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 70 KLTVIPQDPVLFIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDT-LVQNTI--KDAF 146
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKhIFEHVIgpEGVL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 147 KGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDK-PEVLAEkpDSAFAMLL 196
Cdd:TIGR00957 811 KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSyQELLQR--DGAFAEFL 859
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-192 |
2.68e-14 |
|
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: 68.80 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDicILSLEDLRTKLTVIPQDPVLF------- 81
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD--ITNLPPHKRPVNTVFQNYALFphltvfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------IMKLPEK-LQAEVTE-----NGENF--------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQN 140
Cdd:cd03300 92 niafglrLKKLPKAeIKERVAEaldlvQLEGYanrkpsqlSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 141 TIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAF 192
Cdd:cd03300 172 ELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-178 |
3.24e-14 |
|
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: 67.99 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNtpLVLDSLNLNIQSGQTvGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIlSLEDLRTKLTVIPQDPVLF 81
Cdd:cd03264 9 RYGKK--RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------------IMK--LPEKLQAEVTENGEN-------------FSVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:cd03264 85 pnftvrefldyiaWLKgiPSKEVKARVDEVLELvnlgdrakkkigsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2004190228 134 TDTLVQNTIKDAFKGCTVLTIAHRLNTV-LNCDHVLVMENGKVIEF 178
Cdd:cd03264 165 ERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-170 |
3.59e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF- 81
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 ------------IMKL---PEKLQAE----------VTENGENFSVGERQLLcvarALLRN----SKIILLDEATASMDS 132
Cdd:PRK10247 95 dtvydnlifpwqIRNQqpdPAIFLDDlerfalpdtiLTKNIAELSGGEKQRI----SLIRNlqfmPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2004190228 133 KTDTLVQNTI----KDafKGCTVLTIAHRLNTVLNCDHVLVM 170
Cdd:PRK10247 171 SNKHNVNEIIhryvRE--QNIAVLWVTHDKDEINHADKVITL 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-193 |
3.61e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 69.74 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLtvIPQDPVLF 81
Cdd:COG3842 14 RYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM--VFQDYALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------IMKLPEKLQAE-VTE-----NGENF--------SVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:COG3842 90 phltvaenvafglrMRGVPKAEIRArVAEllelvGLEGLadryphqlSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 134 TDTLVQNTIKDAFK--GCTVLTIAH------RLntvlnCDHVLVMENGKVIEFDKPEVLAEKPDSAFA 193
Cdd:COG3842 170 LREEMREELRRLQRelGITFIYVTHdqeealAL-----ADRIAVMNDGRIEQVGTPEEIYERPATRFV 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-188 |
4.68e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIFIDEVDICILSLEDLRTKLTVIPQDP- 78
Cdd:PRK13640 15 YPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIVFQNPd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -----------VLF-----------IMKLPEKLQAEVT----ENGE--NFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:PRK13640 95 nqfvgatvgddVAFglenravprpeMIKIVRDVLADVGmldyIDSEpaNLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 131 DSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKP 188
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-192 |
6.23e-14 |
|
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: 68.44 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 15 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL----RTKLTVIPQDPVLF--------- 81
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLphrtvlenv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -----IMKLPEKLQAEVT---------ENGENF-----SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTI 142
Cdd:cd03294 124 afgleVQGVPRAEREERAaealelvglEGWEHKypdelSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 143 KD--AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKPDSAF 192
Cdd:cd03294 204 LRlqAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-177 |
8.82e-14 |
|
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: 67.46 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSlEDLRTKL------------TVIPQ- 76
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARARLrarhvgfvfqsfQLLPTl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 ---DPVLfimkLPeklqAEVTENGENF-----------------------SVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:COG4181 106 talENVM----LP----LELAGRRDARararallervglghrldhypaqlSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 131 DSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:COG4181 178 DAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-186 |
9.59e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 9.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLgM-ALFRLVEPASGTIFID--EVDI---------------------------- 59
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDgkPVRIrsprdaialgigmvhqhfmlvpnltvae 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 60 -CILSLEDlrTKLTVIPqdpvlfimklPEKLQAEVTENGENF-------------SVGERQLLCVARALLRNSKIILLDE 125
Cdd:COG3845 100 nIVLGLEP--TKGGRLD----------RKAARARIRELSERYgldvdpdakvedlSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 126 ATASM-DSKTDTLVQnTIKD-AFKGCTVLTIAHRLNTVL-NCDHVLVMENGKVI-EFDKPEV----LAE 186
Cdd:COG3845 168 PTAVLtPQEADELFE-ILRRlAAEGKSIIFITHKLREVMaIADRVTVLRRGKVVgTVDTAETseeeLAE 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-189 |
1.33e-13 |
|
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: 67.57 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI------------------FIDEVDICILSLEDLRTKL 71
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisfssqfswimpgTIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 TV----IPQDpvlfIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDtlvqntiKDAFK 147
Cdd:cd03291 132 VVkacqLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE-------KEIFE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 148 GC--------TVLTIAHRLNTVLNCDHVLVMENGKVIEFDK-PEVLAEKPD 189
Cdd:cd03291 201 SCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTfSELQSLRPD 251
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-194 |
1.33e-13 |
|
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: 66.98 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-----------LRTKLTVIpqDPV 79
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfvfqhyaLFRHMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LF-------------------IMKLPEKLQAEVTENG--ENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLV 138
Cdd:cd03296 96 AFglrvkprserppeaeirakVHELLKLVQLDWLADRypAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 139 QNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFAM 194
Cdd:cd03296 176 RRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASPFVY 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-175 |
1.47e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVdicilSLEDLRTKLTVIPQDPVLF 81
Cdd:PRK11247 21 RYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 IMK--------------LPEKLQA--------EVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 139
Cdd:PRK11247 94 PWKkvidnvglglkgqwRDAALQAlaavgladRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2004190228 140 NTIKDAFK--GCTVLTIAHRLN-TVLNCDHVLVMENGKV 175
Cdd:PRK11247 174 DLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-202 |
1.73e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLE---DLRTKLTVIPQDP--------- 78
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNPygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 VLFIMKLP-------------EKLQAEVTENG---EN-------FSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 135
Cdd:PRK11308 111 VGQILEEPllintslsaaerrEKALAMMAKVGlrpEHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 136 TLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFAM-LLAAEVRL 202
Cdd:PRK11308 191 AQVLNLMMDLQQelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQaLLSATPRL 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-185 |
1.96e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 13 SLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP---------VLFIM 83
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 84 KLPEKLQAEVTENGEN-----------------------FSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQN 140
Cdd:PRK15112 111 DFPLRLNTDLEPEQREkqiietlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 141 TIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEF-DKPEVLA 185
Cdd:PRK15112 191 LMLElqEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERgSTADVLA 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-201 |
2.31e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.65 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIFIDEVDICILSLEDLRTK--------LTVIPQDPV 79
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHgtyEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 L---F---------IM----------KLPEKLQAEVTENG--ENFSVGERQLLCVARALLRNSKIILLDEATASM-DSKT 134
Cdd:PRK13549 100 LeniFlgneitpggIMdydamylraqKLLAQLKLDINPATpvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtESET 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 135 DTLVqNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEkpDSAFAMLLAAEVR 201
Cdd:PRK13549 180 AVLL-DIIRDlKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTE--DDIITMMVGRELT 245
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-192 |
3.94e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.67 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFID--EV--------DICI------ 61
Cdd:PRK11432 15 RFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDgeDVthrsiqqrDICMvfqsya 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 62 ----LSLED---LRTKLTVIPQDPVlfIMKLPEKLQAEVTENGEN-----FSVGERQLLCVARALLRNSKIILLDEATAS 129
Cdd:PRK11432 89 lfphMSLGEnvgYGLKMLGVPKEER--KQRVKEALELVDLAGFEDryvdqISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 130 MDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKPDSAF 192
Cdd:PRK11432 167 LDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-176 |
5.61e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 64.98 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 5 DNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIFIDEVDI-------CI---LSLEDLRTKL 71
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRkpdqfqkCVayvRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 TVIPQDPVLFIMKLPEKL-----QAEVTENG--------------ENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:cd03234 97 TVRETLTYTAILRLPRKSsdairKKRVEDVLlrdlaltriggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2004190228 133 KTDTLVQNTIKD-AFKGCTVLTIAH--RLNTVLNCDHVLVMENGKVI 176
Cdd:cd03234 177 FTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-192 |
9.35e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.48 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSL-----GmalfrLVEPASGTIFIDEVDIcilslEDLRTK---LTVIPQDPVLF 81
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV-----TDLPPKdrnIAMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------IMKLP-EKLQAEVTENGE-------------NFSVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:COG3839 88 phmtvyeniafplkLRKVPkAEIDRRVREAAEllgledlldrkpkQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 134 tdtLVQNT---IKDAFK--GCTV----------LTIAhrlntvlncDHVLVMENGKVIEFDKPEVLAEKPDSAF 192
Cdd:COG3839 168 ---LRVEMraeIKRLHRrlGTTTiyvthdqveaMTLA---------DRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-189 |
1.01e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.09 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 7 TPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI------------------FIDEVDICILSLEDLR 68
Cdd:TIGR01271 439 TP-VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswimpgTIKDNIIFGLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 69 TKLTV----IPQDpvlfIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDtlvqntiKD 144
Cdd:TIGR01271 518 YTSVIkacqLEED----IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE-------KE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 145 AFKGC--------TVLTIAHRLNTVLNCDHVLVMENGKVIEFDK-PEVLAEKPD 189
Cdd:TIGR01271 587 IFESClcklmsnkTRILVTSKLEHLKKADKILLLHEGVCYFYGTfSELQAKRPD 640
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-177 |
1.11e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGT----------------IFIDEVDICILSLEDLRTK---- 70
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsvvirgsvayvpqvswIFNATVRENILFGSDFESErywr 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 71 ---LTVIPQDPVLFimklPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNT-IKDAF 146
Cdd:PLN03232 713 aidVTALQHDLDLL----PGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDEL 788
|
170 180 190
....*....|....*....|....*....|.
gi 2004190228 147 KGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:PLN03232 789 KGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-176 |
1.42e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDI----------CI------------------ 61
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykrakYIgrvfqdpmmgtapsmtie 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 62 --LSLEDLRTK-----LTVIPQDPVLFI-------MKLPEKLQAEVtengENFSVGERQLLCVARALLRNSKIILLDEAT 127
Cdd:COG1101 101 enLALAYRRGKrrglrRGLTKKRRELFRellatlgLGLENRLDTKV----GLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 128 ASMDSKTDTLV----QNTIKDafKGCTVLTIAHRLNTVLNC-DHVLVMENGKVI 176
Cdd:COG1101 177 AALDPKTAALVleltEKIVEE--NNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-174 |
1.87e-12 |
|
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: 63.27 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 4 RDNTPLvLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIlSLEDLRTKLTVIPQDPVL--- 80
Cdd:COG4133 12 RGERLL-FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLkpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 --------FIMKL------PEKLQAEVTENG---------ENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTL 137
Cdd:COG4133 90 ltvrenlrFWAALyglradREAIDEALEAVGlagladlpvRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 2004190228 138 VQNTIKD-AFKGCTVLTIAHRLNTVLNCdHVLVMENGK 174
Cdd:COG4133 170 LAELIAAhLARGGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-177 |
2.20e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIFIDEVDICILSLEDLRTKLTVIPQDP------ 78
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -----VLFIMKL------PEKLQAEVTENGE-----------------NFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:PRK14247 98 sifenVALGLKLnrlvksKKELQERVRWALEkaqlwdevkdrldapagKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 131 DSKTDTLVQNTIKDAFKGCTVLTIAH------RLNtvlncDHVLVMENGKVIE 177
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVE 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-186 |
3.83e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVdicILSLEDLRT----KLTVIpqDPVLF---I 82
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSALLELGAgfhpELTGR--ENIYLngrL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 83 MKLP-----EKLQ--AEVTENGE-------NFSVGERQLLCVARALLRNSKIILLDEATASMDS----KTDTLVQNTIKd 144
Cdd:COG1134 116 LGLSrkeidEKFDeiVEFAELGDfidqpvkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIRELRE- 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2004190228 145 afKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAE 186
Cdd:COG1134 195 --SGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPeEVIAA 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-177 |
5.51e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVD-------------ICILSLEdlrtkLTVIPQD 77
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaalaagVAIIYQE-----LHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 PV---LFIMKLPEK--------LQAEVTEN----GENF---------SVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:PRK11288 95 TVaenLYLGQLPHKggivnrrlLNYEAREQlehlGVDIdpdtplkylSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2004190228 134 -TDTL--VQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:PRK11288 175 eIEQLfrVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-185 |
6.21e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI--DEVDICILSLEDLRTKLTVIPQDP- 78
Cdd:PRK13638 10 RYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -----------VLFIMKLPEKLQAEVTE---------NGENF--------SVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:PRK13638 88 qqifytdidsdIAFSLRNLGVPEAEITRrvdealtlvDAQHFrhqpiqclSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 131 DSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLA 185
Cdd:PRK13638 168 DPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPgEVFA 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-199 |
7.17e-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: 63.16 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP----ASGTIFIDEVDICILSLEDLRT----KLTVIPQDP--- 78
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -------------VLFI---MKlPEKLQAEVTE--------NGEN--------FSVGERQLLCVARALLRNSKIILLDEA 126
Cdd:COG4172 105 lnplhtigkqiaeVLRLhrgLS-GAAARARALEllervgipDPERrldayphqLSGGQRQRVMIAMALANEPDLLIADEP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 127 TasmdskT--DTLVQNTIKDAFK------GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFA-MLL 196
Cdd:COG4172 184 T------TalDVTVQAQILDLLKdlqrelGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELFAAPQHPYTrKLL 257
|
...
gi 2004190228 197 AAE 199
Cdd:COG4172 258 AAE 260
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-184 |
7.62e-12 |
|
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: 62.00 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcILSLEDLRTKLTVIPQDPV-- 79
Cdd:cd03265 9 KYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGIVFQDLSvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 --------LFIMK----LPEKLQAEVTEN-------GE-------NFSVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:cd03265 86 deltgwenLYIHArlygVPGAERRERIDElldfvglLEaadrlvkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 134 TDTLVQNTIKDAFK--GCTVLTIAHRLNTV-LNCDHVLVMENGKVIEFDKPEVL 184
Cdd:cd03265 166 TRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-192 |
7.84e-12 |
|
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: 62.02 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGtifideVDICIL-------SLEDLRTKL--- 71
Cdd:COG1119 12 RRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRLFgerrggeDVWELRKRIglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 ------TVIPQDPVL-----------FIMKLPEKLQAEVTEN-----------GENF---SVGERQLLCVARALLRNSKI 120
Cdd:COG1119 84 spalqlRFPRDETVLdvvlsgffdsiGLYREPTDEQRERAREllellglahlaDRPFgtlSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 121 ILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEF-DKPEVLAEKPDSAF 192
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAgPKEEVLTSENLSEA 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-191 |
9.66e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIL-------------SLEDLRTKLTVIPQ 76
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 DPVLF--------IMKLPEKL----QAEVTENGENF------------------SVGERQLLCVARALLRNSKIILLDEA 126
Cdd:PRK10619 100 HFNLWshmtvlenVMEAPIQVlglsKQEARERAVKYlakvgideraqgkypvhlSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004190228 127 TASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKPDSA 191
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-191 |
1.07e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.04 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDI---CILSLEDL---RTKLTVIPQDPVLFIM 83
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVlefRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 84 KL--------------PEK-----LQAEVTENGE-------------NFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PRK14271 116 SImdnvlagvrahklvPRKefrgvAQARLTEVGLwdavkdrlsdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 132 SKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSA 191
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-189 |
1.28e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.03 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP------------ 78
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnqfvgatvedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 VLF------------IMKLPEKLQAE-----VTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD--SKTDTL-V 138
Cdd:PRK13642 103 VAFgmenqgipreemIKRVDEALLAVnmldfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptGRQEIMrV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 139 QNTIKDAFKgCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP-EVLAEKPD 189
Cdd:PRK13642 183 IHEIKEKYQ-LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPsELFATSED 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-177 |
1.50e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIdevdicilsledLRTKLTVIPQ----------DPVL 80
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQvswifnatvrDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 F---------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 139
Cdd:PLN03130 701 FgspfdperyeraidvtalqhdLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
170 180 190
....*....|....*....|....*....|....*....
gi 2004190228 140 NT-IKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:PLN03130 781 DKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-175 |
1.82e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE----PASGTIFIDEV---------DI--------CILSLEDLRT 69
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTvqregrlarDIrksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 70 KLTVIPQDPVLFIMKLP---------------EKLQAeVTENG---------ENFSVGERQLLCVARALLRNSKIILLDE 125
Cdd:PRK09984 100 RLSVLENVLIGALGSTPfwrtcfswftreqkqRALQA-LTRVGmvhfahqrvSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 126 ATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKV 175
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-179 |
2.14e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIFI----------------------DEV---DIC 60
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIpkglrigylpqeppldddltvlDTVldgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 61 ILSLEDLRTKLTVIPQDPVLFIMKLpEKLQAEVTENGE--------------------------NFSVGERQLLCVARAL 114
Cdd:COG0488 89 LRALEAELEELEAKLAEPDEDLERL-AELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 115 LRNSKIILLDEATASMDSKTDTLVQNTIKDaFKGcTVLTIAH-R--LNTVlnCDHVLVMENGKVIEFD 179
Cdd:COG0488 168 LSEPDLLLLDEPTNHLDLESIEWLEEFLKN-YPG-TVLVVSHdRyfLDRV--ATRILELDRGKLTLYP 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-199 |
2.43e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL-----VEPASGTIFIDEVDICILSLEDLR----TKLT 72
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 73 VIPQDPVLFIMKLP--EKLQAEV----------TENGE----------------------NFSVGERQLLCVARALLRNS 118
Cdd:PRK15134 96 MIFQEPMVSLNPLHtlEKQLYEVlslhrgmrreAARGEilncldrvgirqaakrltdyphQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 119 KIILLDEATASMdsktDTLVQNTIKDAFK------GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSA 191
Cdd:PRK15134 176 ELLIADEPTTAL----DVSVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHP 251
|
....*....
gi 2004190228 192 FA-MLLAAE 199
Cdd:PRK15134 252 YTqKLLNSE 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-190 |
2.55e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.88 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID-------EVDICILSLE--------DLRTKLTVI 74
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglkvndpKVDERLIRQEagmvfqqfYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 75 pqDPVLF------------IMKLPEKLQAEV--TENGENF----SVGERQLLCVARALLRNSKIILLDEATASMDSKTDT 136
Cdd:PRK09493 96 --ENVMFgplrvrgaskeeAEKQARELLAKVglAERAHHYpselSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 137 LVQNTIKD-AFKGCTVLTIAHRLNTVLNCDHVLV-MENGKVIEFDKPEVLAEKPDS 190
Cdd:PRK09493 174 EVLKVMQDlAEEGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIKNPPS 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-186 |
2.75e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIfidevDICILSLED----LRTKLTVIPQ- 76
Cdd:PRK13537 16 RYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-----SLCGEPVPSrarhARQRVGVVPQf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 ---DP----------------------------VLFIMKLPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDE 125
Cdd:PRK13537 89 dnlDPdftvrenllvfgryfglsaaaaralvppLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 126 ATASMDSKTDTLVQNTIKDAF-KGCTVLTIAH------RLntvlnCDHVLVMENGKVIEFDKPEVLAE 186
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-201 |
2.79e-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: 61.76 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIFIDEVDICILSLEDLRTK--------LTVIPQDPV 79
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHgtwDGEIYWSGSPLKASNIRDTERAgiviihqeLTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 L-------------FIMKLP------EKLQAEVTENGEN-------FSVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:TIGR02633 96 AeniflgneitlpgGRMAYNamylraKNLLRELQLDADNvtrpvgdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 134 TDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEkpDSAFAMLLAAEVR 201
Cdd:TIGR02633 176 ETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSE--DDIITMMVGREIT 243
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-189 |
3.28e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.43 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIFIDEVDICILSLeDLRTKLTV--IP 75
Cdd:COG1137 12 SYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 76 QDP--------------VLFIMKLPEKLQAEVTEN--------------GENFSVGERQLLCVARALLRNSKIILLDEAT 127
Cdd:COG1137 85 QEAsifrkltvednilaVLELRKLSKKEREERLEElleefgithlrkskAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 128 ASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:COG1137 165 AGVDPIAVADIQKIIRHlKERGIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-176 |
3.67e-11 |
|
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: 59.81 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 14 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICilSLEDLRTKLTVIPQDPVLFI----------- 82
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAhltveqnvglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 83 ----MKLPEKLQAEV-------------TENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD- 144
Cdd:cd03298 95 lspgLKLTAEDRQAIevalarvglagleKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDl 174
|
170 180 190
....*....|....*....|....*....|....
gi 2004190228 145 -AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVI 176
Cdd:cd03298 175 hAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-177 |
4.13e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.15 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDI-----------CILSLEDL----------- 67
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqkgLIRQLRQHvgfvfqnfnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 68 --RTKLTVIPQDPVLF-------IMKLPEKLQAEVTENGEN------FSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK11264 98 phRTVLENIIEGPVIVkgepkeeATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2004190228 133 KTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:PRK11264 178 ELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-177 |
5.64e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 14 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFIMKL-PEKLQAE 92
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLgPEGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 93 VT-----------------ENGE----NFSVGERQLLCVARALLRNSKIILLDEATASMDSK------TDTLVQntIKDa 145
Cdd:PRK10522 422 PAlvekwlerlkmahklelEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPL--LQE- 498
|
170 180 190
....*....|....*....|....*....|..
gi 2004190228 146 fKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:PRK10522 499 -MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-202 |
6.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP--V 79
Cdd:PRK13647 13 RYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LFIMKLPEKL----------QAEVTENGE-----------------NFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK13647 92 VFSSTVWDDVafgpvnmgldKDEVERRVEealkavrmwdfrdkppyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 133 K-TDTLVqnTIKDAF--KGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKpdsafAMLLAAEVRL 202
Cdd:PRK13647 172 RgQETLM--EILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE-----DIVEQAGLRL 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-184 |
8.72e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQD----------PV 79
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlpaaegmtvrEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LFIMKLP-------------EKLQAEVTENG---------ENFSVGERQLLCVARALLRNSKIILLDEATASMD--SKTD 135
Cdd:PRK10575 106 VAIGRYPwhgalgrfgaadrEKVEEAISLVGlkplahrlvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiaHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 136 T--LVQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVL 184
Cdd:PRK10575 186 VlaLVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-189 |
8.79e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.75 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPLV---LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LEDLRTKLTVIP 75
Cdd:PRK13643 11 YQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 76 QDP--VLF---IMK--------------LPEKLQAEVTE-----------NGENFSVGERQLLCVARALLRNSKIILLDE 125
Cdd:PRK13643 91 QFPesQLFeetVLKdvafgpqnfgipkeKAEKIAAEKLEmvgladefwekSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 126 ATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-187 |
8.98e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.84 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI----------------------DEVDICILSLEDL 67
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararlararigvvpqfDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 68 -----------RTKLTVIPqdPVLFIMKLPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDT 136
Cdd:PRK13536 136 lvfgryfgmstREIEAVIP--SLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 137 LVQNTIKDAF-KGCTVLTIAH------RLntvlnCDHVLVMENGKVIEFDKPEVLAEK 187
Cdd:PRK13536 210 LIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
11-176 |
1.14e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 58.46 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQ---SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVdicilSLEDLRTKLTVIPQD---------- 77
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-----VLFDSRKKINLPPQQrkiglvfqqy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 ---P-------VLFIMKL--PEKLQAEVTENGENF-------------SVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:cd03297 85 alfPhlnvrenLAFGLKRkrNREDRISVDELLDLLgldhllnrypaqlSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2004190228 133 KTDTLVQNTIKDAFK--GCTVLTIAHRLNTV-LNCDHVLVMENGKVI 176
Cdd:cd03297 165 ALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-184 |
1.24e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.02 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LEDLRTKLTVIP 75
Cdd:PRK13646 12 YQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 76 QDP--VLFimklPEKLQAEVTENGENF--------------------------------SVGERQLLCVARALLRNSKII 121
Cdd:PRK13646 92 QFPesQLF----EDTVEREIIFGPKNFkmnldevknyahrllmdlgfsrdvmsqspfqmSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 122 LLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVL 184
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-175 |
1.39e-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: 58.42 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-----------LRTK 70
Cdd:cd03301 9 RFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamvfqnyaLYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 71 LTVIpqDPVLFIMKL----PEKLQAEVTENGE-------------NFSVGERQLLCVARALLRNSKIILLDEATASMDSK 133
Cdd:cd03301 87 MTVY--DNIAFGLKLrkvpKDEIDERVREVAEllqiehlldrkpkQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2004190228 134 TDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKV 175
Cdd:cd03301 165 LRVQMRAELKRLQQrlGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-179 |
1.42e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 58.31 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLE-DLRTKLTVIpqDPVLFIMKL--- 85
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRLlgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 86 -----PEKLQ--AEVTENGE-------NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGC-T 150
Cdd:cd03220 115 srkeiDEKIDeiIEFSELGDfidlpvkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkT 194
|
170 180 190
....*....|....*....|....*....|
gi 2004190228 151 VLTIAHRLNTVLN-CDHVLVMENGKVIEFD 179
Cdd:cd03220 195 VILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-157 |
1.55e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE--PASGTIFIDEVDI--------CILSLEDLRTKL 71
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFgreaslidAIGRKGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 72 TVIPQ----DPVLFIMKLPEklqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK 147
Cdd:COG2401 117 ELLNAvglsDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLAR 184
|
170
....*....|..
gi 2004190228 148 --GCTVLTIAHR 157
Cdd:COG2401 185 raGITLVVATHH 196
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
14-185 |
2.18e-10 |
|
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: 59.04 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 14 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF------------ 81
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFdrllgldgeadp 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --IMKLPEKLQ-AEVT--ENGE----NFSVGERQLLCVARALLRNSKIILLDEATASMDSktdtlvqnTIKDAF------ 146
Cdd:COG4615 431 arARELLERLElDHKVsvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP--------EFRRVFytellp 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2004190228 147 ----KGCTVLTIAH-----RLntvlnCDHVLVMENGKVIEFDKPEVLA 185
Cdd:COG4615 503 elkaRGKTVIAISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-193 |
2.27e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC-----------ILSLEDLRTKLTVipQDP 78
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLShvppyqrpinmMFQSYALFPHMTV--EQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 VLFIMKLPEKLQAEVTENGE-----------------NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNT 141
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVNemlglvhmqefakrkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 142 IKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFA 193
Cdd:PRK11607 192 VVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-181 |
3.08e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.32 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC----------------ILSLEDLRTKLTV 73
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhelitnpyskkIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 74 IPQDP--VLF-------IMKLPEKLQAEVTEN-------------GENF--------SVGERQLLCVARALLRNSKIILL 123
Cdd:PRK13631 121 VFQFPeyQLFkdtiekdIMFGPVALGVKKSEAkklakfylnkmglDDSYlerspfglSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 124 DEATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP 181
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-176 |
3.09e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LED----LRTKLTVIPQDPV--- 79
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSskeaLENgismVHQELNLVLQRSVmdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LFIMKLPEK---------------------LQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSK-TDTL 137
Cdd:PRK10982 94 MWLGRYPTKgmfvdqdkmyrdtkaifdeldIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKeVNHL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2004190228 138 VQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 176
Cdd:PRK10982 174 FTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-182 |
5.91e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPV---------- 79
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtpgditvqel 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 ----------LFIMKLPEKLQAE------------VTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD--SKTD 135
Cdd:PRK10253 102 vargryphqpLFTRWRKEDEEAVtkamqatgithlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDisHQID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2004190228 136 TLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 182
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPK 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-176 |
6.38e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIL---SLEDLR--------------TKLT 72
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRrehfgfifqryhllSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 73 VIPQDPVLFIMKLPEK---------------LQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTL 137
Cdd:PRK10535 103 AAQNVEVPAVYAGLERkqrllraqellqrlgLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2004190228 138 VQNTIKDAF-KGCTVLTIAHRLNTVLNCDHVLVMENGKVI 176
Cdd:PRK10535 183 VMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-175 |
1.63e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIlSLEDLRTKLTVIPQ-----------DPV 79
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQhnilfhhltvaEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LFIMKLPEKLQAEV-----------------TENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTI 142
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAqlemeamledtglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....
gi 2004190228 143 KDAFKGCTVLTIAHRLNTV-LNCDHVLVMENGKV 175
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRL 1138
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
20-182 |
1.85e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.92 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 20 SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFidevdicILSLEDLRTKLTVipqdpvlfimklpEKLQAEVTENGEN 99
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-------YIDGEDILEEVLD-------------QLLLIIVGGKKAS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 100 FSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ-------NTIKDAFKGCTVLTIAHRLNTVLncDHVLVMEN 172
Cdd:smart00382 61 GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLLKSEKNLTVILTTNDEKDLG--PALLRRRF 138
|
170
....*....|
gi 2004190228 173 GKVIEFDKPE 182
Cdd:smart00382 139 DRRIVLLLIL 148
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-183 |
2.06e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSL------------EDlRTKLTVIPQD 77
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdairagiayvpED-RKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 PVLFIMKLP-------------EKLQAEVTENGENFSV--------------GERQLLCVARALLRNSKIILLDEATASM 130
Cdd:COG1129 346 SIRENITLAsldrlsrgglldrRRERALAEEYIKRLRIktpspeqpvgnlsgGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 131 D--SKTDtlVQNTIKD-AFKGCTVLTIAHRLNTVL-NCDHVLVMENGKVI-EFDKPEV 183
Cdd:COG1129 426 DvgAKAE--IYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-187 |
3.78e-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: 55.58 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSL--------------GMALFRL--------VEPAS----------GTIFIDEV 57
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLmhvlrgmdqyeptsGRIIYHValcekcgyVERPSkvgepcpvcgGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 58 DICILS---LEDLRTKLTVIPQ--------DPVL--FIMKLPE-------------------KLQAEVTENGENFSVGER 105
Cdd:TIGR03269 95 DFWNLSdklRRRIRKRIAIMLQrtfalygdDTVLdnVLEALEEigyegkeavgravdliemvQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 106 QLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 182
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTPD 254
|
....*
gi 2004190228 183 VLAEK 187
Cdd:TIGR03269 255 EVVAV 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-176 |
3.87e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI-------------DEVDICILSLEdlrtkLTVIPQ- 76
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpkssQEAGIGIIHQE-----LNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 ----------------------------DPVLFIMKLPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEAT- 127
Cdd:PRK10762 95 tiaeniflgrefvnrfgridwkkmyaeaDKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTd 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 128 ASMDSKTDTL--VQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 176
Cdd:PRK10762 171 ALTDTETESLfrVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-181 |
4.02e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.75 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LEDLRTKLTVIP 75
Cdd:PRK13649 12 YQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 76 QDP--VLFimklPEKLQAEVTENGENFSVGERQLLCVARALLR--------------------------------NSKII 121
Cdd:PRK13649 92 QFPesQLF----EETVLKDVAFGPQNFGVSQEEAEALAREKLAlvgiseslfeknpfelsggqmrrvaiagilamEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 122 LLDEATASMDSKTdtlvQNTIKDAFK-----GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP 181
Cdd:PRK13649 168 VLDEPTAGLDPKG----RKELMTLFKklhqsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
10-189 |
8.52e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIfidevdicilsLEDLRTKLTVIPQ----DPVL----- 80
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTLpltvn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 -FIMKLP-----------EKLQAE--VTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAF 146
Cdd:PRK09544 88 rFLRLRPgtkkedilpalKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2004190228 147 K--GCTVLTIAHRLNTVL-NCDHVLVMeNGKVIEFDKPEVLAEKPD 189
Cdd:PRK09544 168 RelDCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-177 |
8.79e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 6 NTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEV------DICILSLEDLRTKLTVIPQDPV 79
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 80 LF-----------------------IMKLPEK------LQAEVTEN----GENFSVGERQLLCVARALLRNSKIILLDEA 126
Cdd:PRK14246 101 PFphlsiydniayplkshgikekreIKKIVEEclrkvgLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 127 TASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
10-184 |
1.36e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIL-SLEDLRTKLTVIPQDPVLF------- 81
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFsrmtvee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 --------------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNT 141
Cdd:PRK11614 100 nlamggffaerdqfqerikwVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2004190228 142 IKDAF-KGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVL 184
Cdd:PRK11614 180 IEQLReQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-202 |
1.65e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 8 PLVlDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA----SGTIFIDEVDIcilSLEDLRTKLT-VIPQDP---- 78
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPV---APCALRGRKIaTIMQNPrsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -VLFIMK------------------LPEKLQAEVTENGE--------NFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PRK10418 93 nPLHTMHtharetclalgkpaddatLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 132 SktdtLVQNTIKD------AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKPDSAFA-MLLAAEVRL 202
Cdd:PRK10418 173 V----VAQARILDllesivQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKHAVTrSLVSAHLAL 247
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-177 |
1.66e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 6 NTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALfrLVEPA----SGTIFIDEVDICILSLEDlRTKLTV-------- 73
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEE-RAHLGIflafqypi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 74 -IP-----------------------QDPVLFIMKLPEKL------QAEVTEN-GENFSVGERQLLCVARALLRNSKIIL 122
Cdd:CHL00131 95 eIPgvsnadflrlaynskrkfqglpeLDPLEFLEIINEKLklvgmdPSFLSRNvNEGFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 123 LDEATASMDskTDTLVQ-----NTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 177
Cdd:CHL00131 175 LDETDSGLD--IDALKIiaegiNKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIK 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-192 |
1.86e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.03 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 5 DNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIFIDEVDICILSLED-----------LRT 69
Cdd:PRK09452 25 DGKE-VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAENrhvntvfqsyaLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 70 KLTVIpqDPVLFIMKLPEKLQAEVTE-----------------NGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 132
Cdd:PRK09452 100 HMTVF--ENVAFGLRMQKTPAAEITPrvmealrmvqleefaqrKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 133 KTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAF 192
Cdd:PRK09452 178 KLRKQMQNELKALQRklGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-178 |
1.90e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIdEVDICILSLEDLRTKLTVipQDPVLF-------- 81
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-ERSIAYVPQQAWIMNATV--RGNILFfdeedaar 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------------IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKT-DTLVQNTIKDAFK 147
Cdd:PTZ00243 752 ladavrvsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGALA 831
|
170 180 190
....*....|....*....|....*....|.
gi 2004190228 148 GCTVLTIAHRLNTVLNCDHVLVMENGKViEF 178
Cdd:PTZ00243 832 GKTRVLATHQVHVVPRADYVVALGDGRV-EF 861
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-176 |
1.92e-08 |
|
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: 52.72 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI-------------FIDEVDICILSLEDLRTKLTVIPQ 76
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrrkkFLRRIGVVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 ----------DPVLFIMKLPE-----KLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNT 141
Cdd:cd03267 116 fyllaaiydlPPARFKKRLDElsellDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 2004190228 142 IKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVI 176
Cdd:cd03267 196 LKEYNRerGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-200 |
2.27e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.78 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT-------------------- 69
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVgfvfqhyalfrhmtvfdnia 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 70 -KLTVIP--QDPVLFI-----MKLPEKLQAEVTEN--GENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 139
Cdd:PRK10851 97 fGLTVLPrrERPNAAAikakvTQLLEMVQLAHLADryPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004190228 140 NTIK---DAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 200
Cdd:PRK10851 177 RWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-202 |
2.44e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 14 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDE----------VDICILSLEDLR----TKLTVIPQDP- 78
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQEPm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 ----------------------------------VLFIMKLPEKlQAEVTENGENFSVGERQLLCVARALLRNSKIILLD 124
Cdd:PRK10261 115 tslnpvftvgeqiaesirlhqgasreeamveakrMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 125 EATASMDSKTDTLVQNTIKDAFKGCT--VLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFAM-LLAAEV 200
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAPQHPYTRaLLAAVP 273
|
..
gi 2004190228 201 RL 202
Cdd:PRK10261 274 QL 275
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-180 |
3.37e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.09 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--VEP---ASGTIFIDEVDICILSLE--DLRTKLTVIPQDPVLFIM 83
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 84 ---------------KLPEKLQAEVT-----------------ENGENFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PRK14239 101 siyenvvyglrlkgiKDKQVLDEAVEkslkgasiwdevkdrlhDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2004190228 132 SKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDK 180
Cdd:PRK14239 181 PISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-190 |
5.03e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 51.25 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 17 NIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICI----------LSLEDLRTKLTVIPQDPVLF---IM 83
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYkpqyikadyeGTVRDLLSSITKDFYTHPYFkteIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 84 KlPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDafkgctvlTIAHRLNTVLN 163
Cdd:cd03237 101 K-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR--------FAENNEKTAFV 171
|
170 180 190
....*....|....*....|....*....|...
gi 2004190228 164 CDHVLVMEN---GKVIEFD-KPEV--LAEKPDS 190
Cdd:cd03237 172 VEHDIIMIDylaDRLIVFEgEPSVngVANPPQS 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-202 |
5.93e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 51.64 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 25 GIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDicilsLEDLRTKLTVIP---------QDPVLF-------------- 81
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV-----LQDSARGIFLPPhrrrigyvfQEARLFphlsvrgnllygrk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -IMKLPEKLQ-AEVTE----------NGENFSVGERQLLCVARALLRNSKIILLDEATASMD--SKTDTL-VQNTIKDAF 146
Cdd:COG4148 104 rAPRAERRISfDEVVEllgighlldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDlaRKAEILpYLERLRDEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 147 kGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAEKPDSAFAMLLAAEVRL 202
Cdd:COG4148 184 -DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLaEVLSRPDLLPLAGGEEAGSVL 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-175 |
9.50e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.58 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLE---DLRT-KLTVIPQ--------- 76
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNqKLGFIYQfhhllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 ------DPVLFIMKLPEKLQAEVTE-------------NGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKT-DT 136
Cdd:PRK11629 104 alenvaMPLLIGKKKPAEINSRALEmlaavglehranhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNaDS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2004190228 137 LVQNTIK-DAFKGCTVLTIAHRLNTVLNCDHVLVMENGKV 175
Cdd:PRK11629 184 IFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-181 |
9.54e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC-----ILSLEDLRTKLTVI 74
Cdd:PRK13645 16 YAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkIKEVKRLRKEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 75 PQDP--VLF----------------------IMKLPEKL------QAEVTENGENFSVGERQLLCVARALLRNSKIILLD 124
Cdd:PRK13645 96 FQFPeyQLFqetiekdiafgpvnlgenkqeaYKKVPELLklvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 125 EATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP 181
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-142 |
1.78e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.49 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcilSLEDLRTKLTVI-PQD---PVLFIMk 84
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPALTVA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 85 lpEKLQ--AEVTENGE---------------------NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNT 141
Cdd:PRK13539 92 --ENLEfwAAFLGGEEldiaaaleavglaplahlpfgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
.
gi 2004190228 142 I 142
Cdd:PRK13539 170 I 170
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-179 |
4.28e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDE-VDICILS---LEDLRTKLTVIPQDPVLFIMK 84
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgIKLGYFAqhqLEFLRADESPLQHLARLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 85 LPEKLQ----------AEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD-----SKTDTLVQntikdaFKGC 149
Cdd:PRK10636 406 LEQKLRdylggfgfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrqALTEALID------FEGA 479
|
170 180 190
....*....|....*....|....*....|
gi 2004190228 150 TVLTIAHRLNTVLNCDHVLVMENGKVIEFD 179
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-189 |
8.66e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL------RT--------KLTVI 74
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIarmgvvRTfqhvrlfrEMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 75 PQDPV---------LF--IMKLPEKLQAE---------------VTE--NGE--NFSVGERQLLCVARALLRNSKIILLD 124
Cdd:PRK11300 99 ENLLVaqhqqlktgLFsgLLKTPAFRRAEsealdraatwlervgLLEhaNRQagNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 125 EATASMDSK-TDTLVQ--NTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:PRK11300 179 EPAAGLNPKeTKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-134 |
1.23e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.39 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDI--------CILSLEDLRTKLTVipQDPVLF 81
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgaergVVFQNEGLLPWRNV--QDNVAF 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 IMKLP--EKLQAEVT-----------ENGENF----SVGERQLLCVARALLRNSKIILLDEATASMDSKT 134
Cdd:PRK11248 94 GLQLAgvEKMQRLEIahqmlkkvgleGAEKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-161 |
1.27e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.34 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 6 NTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC-------ILSLEDLRTKLTVIPQDP 78
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFnqniyerRVNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 VLFIM--------------------------------KLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEA 126
Cdd:PRK14258 98 NLFPMsvydnvaygvkivgwrpkleiddivesalkdaDLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 2004190228 127 TASMDS----KTDTLVQNTIKDAfkGCTVLTIAHRLNTV 161
Cdd:PRK14258 178 CFGLDPiasmKVESLIQSLRLRS--ELTMVIVSHNLHQV 214
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-178 |
1.33e-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: 46.87 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIFIDEVDICILSLEDLRTKLTVIPQDP 78
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 VLFIMKLPEKLQAEVTENGENF----SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIK---DAFKGCTV 151
Cdd:cd03233 94 HFPTLTVRETLDFALRCKGNEFvrgiSGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRtmaDVLKTTTF 173
|
170 180
....*....|....*....|....*...
gi 2004190228 152 LTIAHRLNTVLNC-DHVLVMENGKVIEF 178
Cdd:cd03233 174 VSLYQASDEIYDLfDKVLVLYEGRQIYY 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-178 |
1.34e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIFIDE------VDICILSLEDLRTKLTVIP--Q 76
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMItgqeQPDSGTIEIGEtvklayVDQSRDALDPNKTVWEEISggL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 77 DpvlfIMKLpeklqAEVTENGE------NF------------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLV 138
Cdd:TIGR03719 412 D----IIKL-----GKREIPSRayvgrfNFkgsdqqkkvgqlSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2004190228 139 QNTIkDAFKGCTVLtIAH------RLNTvlncdHVLVMENGKVIEF 178
Cdd:TIGR03719 483 EEAL-LNFAGCAVV-ISHdrwfldRIAT-----HILAFEGDSHVEW 521
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-176 |
1.73e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 3 YRdNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIdevdICILSLEDLRTKLTV-IPQD---- 77
Cdd:PRK15056 16 WR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVAyVPQSeevd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 78 ---PVLF-------------IMKLPEKLQAEVTEN---------------GEnFSVGERQLLCVARALLRNSKIILLDEA 126
Cdd:PRK15056 91 wsfPVLVedvvmmgryghmgWLRRAKKRDRQIVTAalarvdmvefrhrqiGE-LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 127 TASMDSKTDTLVQNTIKDAF-KGCTVLTIAHRLNTVLN-CDHVlVMENGKVI 176
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
15-131 |
1.74e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.88 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 15 NLNIQSGQTVGIVGRTGSGKSSL--GMALFrlVEPASGTIFIDEVD----------ICILSLE-DLRTKLTV-----IPQ 76
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLlnLIAGF--LTPASGSLTLNGQDhtttppsrrpVSMLFQEnNLFSHLTVaqnigLGL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 77 DPVL-----------------FIMKLPEKLQAEVtengenfSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PRK10771 97 NPGLklnaaqreklhaiarqmGIEDLLARLPGQL-------SGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
99-189 |
1.85e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.14 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 99 NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHR-LNTVLNCDHVLVMENGKVIE 177
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
90
....*....|..
gi 2004190228 178 FDKPEVLAEKPD 189
Cdd:PRK14267 229 VGPTRKVFENPE 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-175 |
4.89e-06 |
|
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: 46.36 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA-SGTIFIDEVDICILS-LEDLRTKLTVIPQD-------PVL- 80
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPILg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 --------------FIMKLPEKLQAEVTENG---------------ENFSVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:TIGR02633 356 vgknitlsvlksfcFKMRIDAAAELQIIGSAiqrlkvktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2004190228 132 SKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKV 175
Cdd:TIGR02633 436 VGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-187 |
5.25e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 9 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTK-LTVIPQDP-----VL-- 80
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrglVPdm 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 -----FIMKLPEKLQ---------AEVTENGE------------------NFSVGERQLLCVARALLRNSKIIL------ 122
Cdd:COG3845 352 svaenLILGRYRRPPfsrggfldrKAIRAFAEelieefdvrtpgpdtparSLSGGNQQKVILARELSRDPKLLIaaqptr 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004190228 123 -LDEATASMdsktdtlVQNTIKDAF-KGCTVLTIAHRLNTVLN-CDHVLVMENGKVI-EFDKPEVLAEK 187
Cdd:COG3845 432 gLDVGAIEF-------IHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREE 493
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
95-189 |
5.86e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.54 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 95 ENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRL-------------NTV 161
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqqaarvsdmtaffNVE 226
|
90 100
....*....|....*....|....*...
gi 2004190228 162 LNCDHVlvmENGKVIEFDKPEVLAEKPD 189
Cdd:PRK14243 227 LTEGGG---RYGYLVEFDRTEKIFNSPQ 251
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-180 |
6.73e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAS--GTIFIDEVDICILSLEdlRTKLtvIPQDPVLF------ 81
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK--RTGF--VTQDDILYphltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 -------IMKLPEKLQAEVT----------------EN---GENF----SVGERQLLCVARALLRNSKIILLDEATASMD 131
Cdd:PLN03211 159 etlvfcsLLRLPKSLTKQEKilvaesviselgltkcENtiiGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2004190228 132 SKTD-TLVQNTIKDAFKGCTVLTIAHRLNTVL--NCDHVLVMENGKVIEFDK 180
Cdd:PLN03211 239 ATAAyRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEGRCLFFGK 290
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-177 |
7.58e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.30 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 21 GQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL---------RTKLTVIPQDP-------VLFIMK 84
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 85 LPEKLQAevteNGEN-----------------------------FSVGERQLLCVARALLRNSKIILLDEATASMDSKtd 135
Cdd:PRK11701 112 IGERLMA----VGARhygdiratagdwlerveidaariddlpttFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS-- 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 136 tlVQNTIKDAFKGCT------VLTIAHRLNTV-LNCDHVLVMENGKVIE 177
Cdd:PRK11701 186 --VQARLLDLLRGLVrelglaVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-189 |
2.22e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.99 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 1 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIFIDEVDICILS---LEDLRTKLTV 73
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMSrsrLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 74 IPQDPVLFI---------------MKLPE---------KLQAEVTENGEN-----FSVGERQLLCVARALLRNSKIILLD 124
Cdd:PRK11831 89 LFQSGALFTdmnvfdnvayplrehTQLPApllhstvmmKLEAVGLRGAAKlmpseLSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 125 EATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 189
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
101-186 |
2.60e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 44.27 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 101 SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLNC--DHVLVMENGKVIE 177
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAY 247
|
....*....
gi 2004190228 178 FDKPEVLAE 186
Cdd:TIGR00955 248 LGSPDQAVP 256
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-186 |
2.70e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID-EVDICILSlEDLRTKLTVIpqDPVL 80
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNgEVSVIAIS-AGLSGQLTGI--ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 81 FIM-------KLPEKLQAEVTENGE----------NFSVGERQLLCVARALLRNSKIILLDEATASMDSktdTLVQNTIK 143
Cdd:PRK13546 108 FKMlcmgfkrKEIKAMTPKIIEFSElgefiyqpvkKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ---TFAQKCLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 144 DAFK----GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEF-DKPEVLAE 186
Cdd:PRK13546 185 KIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYgELDDVLPK 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-177 |
3.82e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIFID-------------EVDICILSLEdlrtkLTVI 74
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVYPHgsyEGEILFDgevcrfkdirdseALGIVIIHQE-----LALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 75 PQDPV---LFI---------------MKLPEKLQAEV--TENGE----NFSVGERQLLCVARALLRNSKIILLDEATASM 130
Cdd:NF040905 91 PYLSIaenIFLgnerakrgvidwnetNRRARELLAKVglDESPDtlvtDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 131 -DSKTDTLVqNTIKDaFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 177
Cdd:NF040905 171 nEEDSAALL-DLLLE-LKaqGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-176 |
4.83e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.77 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI------------------FIDEVDIC------ILSLE 65
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQktrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 66 DLRTKLTVIPQ-----------------DPVLFIMKLPE--KLQAEVTE-----------NGENFSVGERQLLCVARALL 115
Cdd:PRK13651 102 EIRRRVGVVFQfaeyqlfeqtiekdiifGPVSMGVSKEEakKRAAKYIElvgldesylqrSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2004190228 116 RNSKIILLDEATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLN-CDHVLVMENGKVI 176
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVLEwTKRTIFFKDGKII 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-178 |
4.95e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 8 PLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID-EVDICILSLE-----DLRTkltvipqDPVLF 81
Cdd:PLN03073 522 PLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSaKVRMAVFSQHhvdglDLSS-------NPLLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 82 IMK----LPE-KLQAEVTENG----------ENFSVGERQLLCVARALLRNSKIILLDEATASMD-SKTDTLVQNTIkdA 145
Cdd:PLN03073 595 MMRcfpgVPEqKLRAHLGSFGvtgnlalqpmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQGLV--L 672
|
170 180 190
....*....|....*....|....*....|....
gi 2004190228 146 FKGcTVLTIAHRLNTVL-NCDHVLVMENGKVIEF 178
Cdd:PLN03073 673 FQG-GVLMVSHDEHLISgSVDELWVVSEGKVTPF 705
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-164 |
8.42e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 17 NIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDevdicilsledlrTKLTV--IPQ-----DPVLFIM-KLPEK 88
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------------TKLEVayFDQhraelDPEKTVMdNLAEG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 89 LQaEVTENG---------ENF--------------SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIkDA 145
Cdd:PRK11147 408 KQ-EVMVNGrprhvlgylQDFlfhpkramtpvkalSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DS 485
|
170 180
....*....|....*....|...
gi 2004190228 146 FKGcTVLTIAH-RL---NTVLNC 164
Cdd:PRK11147 486 YQG-TVLLVSHdRQfvdNTVTEC 507
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-143 |
8.56e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.46 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 18 IQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID----------EVDICILSLEDLRTKLTVIPQDP-----VLFI 82
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDYDGTVEEFLRSANTDDFGSSyykteIIKP 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 83 MKLPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIK 143
Cdd:COG1245 443 LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-202 |
1.09e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 41.71 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP----------- 78
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddqifsptveq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 79 -VLF---IMKLPEKLQAEVTENG--------------ENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQN 140
Cdd:PRK13652 99 dIAFgpiNLGLDEETVAHRVSSAlhmlgleelrdrvpHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004190228 141 TIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDsafamlLAAEVRL 202
Cdd:PRK13652 179 FLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD------LLARVHL 237
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-156 |
2.82e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 7 TPLvLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLV--------------------EP---ASGTIF------IDEV 57
Cdd:PRK11147 16 APL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqDPprnVEGTVYdfvaegIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 58 DICILSLEDLRTKLTVIPQDPVLFIM-KLPEKL--------QAEVTENGENFSVGERQLLC-----------VARALLRN 117
Cdd:PRK11147 95 AEYLKRYHDISHLVETDPSEKNLNELaKLQEQLdhhnlwqlENRINEVLAQLGLDPDAALSslsggwlrkaaLGRALVSN 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 2004190228 118 SKIILLDEATASMDSKTDTLVQNTIKDaFKGCTVLtIAH 156
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISH 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
18-199 |
2.91e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.86 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 18 IQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDevdicilsledlRTKLTVIPQDPVLfimklpeklqaevteng 97
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVYKPQYIDL----------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 98 enfSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIK----DAFKgcTVLTIAH---RLNTVLNCDHVLVM 170
Cdd:cd03222 73 ---SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlseEGKK--TALVVEHdlaVLDYLSDRIHVFEG 147
|
170 180
....*....|....*....|....*....
gi 2004190228 171 ENGKVIEFDKPEVLAEKPDSAFAMLLAAE 199
Cdd:cd03222 148 EPGVYGIASQPKGTREGINRFLRGYLITF 176
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
24-156 |
3.39e-04 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 39.67 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 24 VGIVGRTGSGKSSLGMALFRLVEPAsgtifiDEVDICILSLEdlrtkltvipqDPVLFIM-----KLPEKLQAEVTENGE 98
Cdd:cd19516 14 VYVAGATGSGKSTLLAAIYRYILEN------DPPDRKIITYE-----------DPIEFVYdgiksKHSIIVQSQIPRHFK 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2004190228 99 NFSVGERQllcvarALLRNSKIILLDEATasmDSKTdtlVQNTIKDAFKGCTVLTIAH 156
Cdd:cd19516 77 SFAKAVRE------ALRRKPSLIGVGELR---DQET---ISAAVEASLTGHPVYSTVH 122
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-186 |
3.55e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL-FIMKLPEKL 89
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKgLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 90 QAEVT--------------ENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSktdTLVQNTIK--DAFK--GCTV 151
Cdd:PRK13545 120 IKEIIpeiiefadigkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ---TFTKKCLDkmNEFKeqGKTI 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 2004190228 152 LTIAHRLNTVLN-CDHVLVMENGKVIEF-DKPEVLAE 186
Cdd:PRK13545 197 FFISHSLSQVKSfCTKALWLHYGQVKEYgDIKEVVDH 233
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-156 |
7.80e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 26 IVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDI-------CILSLEDLRTKLTVIPQDPVLF---IMKLPEKLQAEVT- 94
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpyCTYIGHNLGLKLEMTVFENLKFwseIYNSAETLYAAIHy 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004190228 95 --------ENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTI-KDAFKGCTVLTIAH 156
Cdd:PRK13541 111 fklhdlldEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvMKANSGGIVLLSSH 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-59 |
1.20e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 1.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALF-----RLVepaSGTIFID--EVDI 59
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDgkEVDV 328
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-67 |
1.50e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 1.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004190228 2 RYRDNTPLVLDSLNlnIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL 67
Cdd:PRK10938 12 RLSDTKTLQLPSLT--LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL 75
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
101-179 |
1.51e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 37.99 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 101 SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVL--NCDHVLVME-NGKVI 176
Cdd:cd03232 110 SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASIfeKFDRLLLLKrGGKTV 189
|
...
gi 2004190228 177 EFD 179
Cdd:cd03232 190 YFG 192
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-41 |
1.89e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.57 E-value: 1.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2004190228 2 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLgMAL 41
Cdd:NF033858 10 RYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSL-LSL 46
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
23-43 |
2.01e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 38.21 E-value: 2.01e-03
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-175 |
3.87e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.60 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 10 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAS-GTIFID--EVD-----------ICILSlEDlRTKLTVIP 75
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDgkPVKirnpqqaiaqgIAMVP-ED-RKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 76 QDPVLFIMKLPEKLQ----------AEVTENGE-----------------NFSVGERQLLCVARALLRNSKIILLDEATA 128
Cdd:PRK13549 355 VMGVGKNITLAALDRftggsriddaAELKTILEsiqrlkvktaspelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2004190228 129 SMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKV 175
Cdd:PRK13549 435 GIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
25-44 |
4.52e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 36.16 E-value: 4.52e-03
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
11-170 |
9.68e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 35.38 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 11 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRlvepASGTIFIDEVdicilsledlrtkLTVIPQDPVLFImklpEKLQ 90
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLISF-------------LPKFSRNKLIFI----DQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004190228 91 AeVTENGENF----------SVGERQLLCVARALLRNSK--IILLDEATASMD-SKTDTLVqNTIKDAF-KGCTVLTIAH 156
Cdd:cd03238 70 F-LIDVGLGYltlgqklstlSGGELQRVKLASELFSEPPgtLFILDEPSTGLHqQDINQLL-EVIKGLIdLGNTVILIEH 147
|
170
....*....|....
gi 2004190228 157 RLNTVLNCDHVLVM 170
Cdd:cd03238 148 NLDVLSSADWIIDF 161
|
|
| |
