|
Name |
Accession |
Description |
Interval |
E-value |
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-278 |
0e+00 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 516.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKR 80
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK13650 81 HKIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMR-EDLVDLDLD 239
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRgNDLLQLGLD 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 251820877 240 RPFTTELASSLRQTGLDLPLRYFTEEELEETLWELISKK 278
Cdd:PRK13650 241 IPFTTSLVQSLRQNGYDLPEGYLTEKELEEQLWELISKM 279
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-261 |
2.57e-158 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 441.10 E-value: 2.57e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNVWDKRRLI 83
Cdd:TIGR04520 1 IEVENVSFSY-PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:TIGR04520 80 GMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMRED-LVDLDLDRPF 242
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVElLKEIGLDVPF 239
|
250
....*....|....*....
gi 251820877 243 TTELASSLRQTGLDLPLRY 261
Cdd:TIGR04520 240 ITELAKALKKRGIPLPPDI 258
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-262 |
6.42e-146 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 410.18 E-value: 6.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKR 80
Cdd:PRK13635 2 KEEIIRVEHISFRY-PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMR-EDLVDLDLD 239
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSgHMLQEIGLD 240
|
250 260
....*....|....*....|...
gi 251820877 240 RPFTTELASSLRQTGLDLPLRYF 262
Cdd:PRK13635 241 VPFSVKLKELLKRNGILLPNTYL 263
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-233 |
1.45e-117 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 336.23 E-value: 1.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:COG1122 79 LVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMREDL 233
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-262 |
6.99e-114 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 328.98 E-value: 6.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKR 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK13642 81 RKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELF-MREDLVDLDLD 239
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFaTSEDMVEIGLD 240
|
250 260
....*....|....*....|...
gi 251820877 240 RPFTTELASSLRQTGLDLPLRYF 262
Cdd:PRK13642 241 VPFSSNLMKDLRKNGFDLPEKYL 263
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-251 |
1.34e-105 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 307.69 E-value: 1.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:PRK13632 8 IKVENVSFSYP-NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:PRK13632 87 IIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMREDLVDL-DLDRPFT 243
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILEKaKIDSPFI 246
|
....*...
gi 251820877 244 TELASSLR 251
Cdd:PRK13632 247 YKLSKKLK 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-258 |
6.23e-104 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 304.03 E-value: 6.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGD---IYIDGDALTIDNVWDK 79
Cdd:PRK13640 4 NIVEFKHVSFTY-PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:PRK13640 83 REKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMREDLV-DLDL 238
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLkEIGL 242
|
250 260
....*....|....*....|
gi 251820877 239 DRPFTTELASSLRQTGLDLP 258
Cdd:PRK13640 243 DIPFVYKLKNKLKEKGISVP 262
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-217 |
2.19e-102 |
|
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: 297.07 E-value: 2.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNQeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGM 85
Cdd:cd03225 1 ELKNLSFSYPD-GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:cd03225 80 VFQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQ 217
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-258 |
2.39e-102 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 299.70 E-value: 2.39e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQ---YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNV 76
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEStekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 WDKRRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMR-EDLVD 235
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEvEMMKK 240
|
250 260
....*....|....*....|...
gi 251820877 236 LDLDRPFTTELASSLRQTGLDLP 258
Cdd:PRK13633 241 IGLDVPQVTELAYELKKEGVDIP 263
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-250 |
3.58e-102 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 298.97 E-value: 3.58e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL 82
Cdd:PRK13648 6 SIIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKII 162
Cdd:PRK13648 85 IGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMRED-LVDLDLDRP 241
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEeLTRIGLDLP 244
|
....*....
gi 251820877 242 FTTELASSL 250
Cdd:PRK13648 245 FPIKINQML 253
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-258 |
6.51e-99 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 290.89 E-value: 6.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL 82
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 ---IGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVVALR 158
Cdd:TIGR04521 81 rkkVGLVFQFPEHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMRED-LVDL 236
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAeYADRVIVMHKGKIVLDGTPREVFSDVDeLEKI 240
|
250 260
....*....|....*....|..
gi 251820877 237 DLDRPFTTELASSLRQTGLDLP 258
Cdd:TIGR04521 241 GLDVPEITELARKLKEKGLPVP 262
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
7.97e-79 |
|
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: 247.12 E-value: 7.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGDIYIDGDALTIDNVW 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DKRRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVAL 157
Cdd:COG1123 80 LRGRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 158 RPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMR 230
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAeIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-258 |
1.08e-78 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 239.95 E-value: 1.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNV--WDKR 80
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMT--DFKTREPARLSGGQKQRVAIAGVVALR 158
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMR-EDLVDL 236
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAkLADRIIVMNKGKCELQGTPREVFKEvETLESI 242
|
250 260
....*....|....*....|..
gi 251820877 237 DLDRPFTTELASSLRQTGLDLP 258
Cdd:PRK13637 243 GLAVPQVTYLVRKLRKKGFNIP 264
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
1.65e-78 |
|
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: 246.35 E-value: 1.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQYT--LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRR 81
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 L---IGMVFQNPDNQFVGA-TVEDDVAFGLENQGI-PLEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAIAGVV 155
Cdd:COG1123 340 LrrrVQMVFQDPYSSLNPRmTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELF 228
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRyIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-230 |
3.26e-75 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 233.07 E-value: 3.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDalTIDNVWDKR 80
Cdd:COG3842 2 AMPALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR--DVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPdnqfvgA-----TVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVV 155
Cdd:COG3842 77 RNVGMVFQDY------AlfphlTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELFMR 230
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEaLALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-249 |
2.02e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 222.66 E-value: 2.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnvwDK 79
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNPdnqfvgA-----TVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGV 154
Cdd:COG1116 79 GPDRGVVFQEP------AllpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 155 VALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKN--GQVESIstpnelfmre 231
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEaVFLADRVVVLSArpGRIVEE---------- 222
|
250
....*....|....*...
gi 251820877 232 dlVDLDLDRPFTTELASS 249
Cdd:COG1116 223 --IDVDLPRPRDRELRTS 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-261 |
3.84e-72 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 222.65 E-value: 3.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDN--VWDKRR 81
Cdd:PRK13639 1 ILETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKI 161
Cdd:PRK13639 79 TVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVAL-SDRVIVMKNGQVESISTPNELFMREDLVD-LDLD 239
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETIRkANLR 237
|
250 260
....*....|....*....|...
gi 251820877 240 RPFTTELASSL-RQTGLDLPLRY 261
Cdd:PRK13639 238 LPRVAHLIEILnKEDNLPIKMGY 260
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-261 |
1.52e-71 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 221.22 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNQEDEqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRR 81
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKI 161
Cdd:PRK13652 79 FVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMREDLV-DLDLD 239
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPeMADYIYVMDKGRIVAYGTVEEIFLQPDLLaRVHLD 238
|
250 260
....*....|....*....|..
gi 251820877 240 RPFTTELASSLRQTGLDLPLRY 261
Cdd:PRK13652 239 LPSLPKLIRSLQAQGIAIDMAY 260
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-258 |
3.18e-68 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 212.93 E-value: 3.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNVWDKRRL 82
Cdd:PRK13644 1 MIRLENVSYSY--PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKII 162
Cdd:PRK13644 79 VGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMREDLVDLDLDRPF 242
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPS 237
|
250
....*....|....*.
gi 251820877 243 TTELASSLRQTGLDLP 258
Cdd:PRK13644 238 LIELAENLKMHGVVIP 253
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-219 |
1.27e-67 |
|
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: 208.91 E-value: 1.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRRLIG 84
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPDNqFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03259 76 MVFQDYAL-FPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVE 219
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEaLALADRIAVMNEGRIV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
1.30e-67 |
|
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: 209.84 E-value: 1.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVW 77
Cdd:COG1127 2 SEPMIEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DKRRLIGMVFQNpdnqfvGA-----TVEDDVAFGL-ENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAI 151
Cdd:COG1127 79 ELRRRIGMLFQG------GAlfdslTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 152 AGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELF 228
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEELL 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-228 |
5.70e-67 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 211.86 E-value: 5.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRR 81
Cdd:COG3839 1 MASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--DLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPDNqFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKI 161
Cdd:COG3839 76 NIAMVFQSYAL-YPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELF 228
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAmTLADRIAVMNDGRIQQVGTPEELY 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-258 |
4.96e-66 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 207.57 E-value: 4.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID----NVWD 78
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 79 KRRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVVAL 157
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 158 RPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMR-EDLVD 235
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAArYADQIVVMHKGTVFLQGTPREIFADpDELEA 242
|
250 260
....*....|....*....|....
gi 251820877 236 LDLDRPFTTELASSL-RQTGLDLP 258
Cdd:PRK13634 243 IGLDLPETVKFKRALeEKFGISFP 266
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-260 |
2.15e-65 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 205.35 E-value: 2.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKR 80
Cdd:PRK13647 1 MDNIIEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK13647 79 SKVGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPnELFMREDLVD-LDL 238
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAeWADQVIVLKEGRVLAEGDK-SLLTDEDIVEqAGL 236
|
250 260
....*....|....*....|...
gi 251820877 239 DRPFTTELASSLRQTGLD-LPLR 260
Cdd:PRK13647 237 RLPLVAQIFEDLPELGQSkLPLT 259
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-215 |
3.90e-65 |
|
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: 202.70 E-value: 3.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnvwDKRRLI 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:cd03293 76 GYVFQQ-DALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKN 215
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEaVFLADRVVVLSA 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-218 |
4.74e-65 |
|
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: 202.74 E-value: 4.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKY-NQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNVWDK-- 79
Cdd:cd03257 1 LLEVKNLSVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNPDNQF-VGATVEDDVAFGLENQGIP--LEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAIAGVV 155
Cdd:cd03257 81 RKEIQMVFQDPMSSLnPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAkIADRVAVMYAGKI 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-252 |
2.69e-64 |
|
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: 201.57 E-value: 2.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKY-NQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDK--RR 81
Cdd:COG1124 2 LEVRNLSVSYgQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT--RRRRKafRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPDnqfvGA-----TVEDDVAFGLENQGIPleEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVV 155
Cdd:COG1124 80 RVQMVFQDPY----ASlhprhTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVEsistpnELFMREDLV 234
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAhLCDRVAVMQNGRIV------EELTVADLL 227
|
250
....*....|....*...
gi 251820877 235 DlDLDRPFTTELASSLRQ 252
Cdd:COG1124 228 A-GPKHPYTRELLAASLA 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-228 |
7.68e-64 |
|
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: 200.11 E-value: 7.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKY-NQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTI---DNVWDK 79
Cdd:cd03258 1 MIELKNVSKVFgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:cd03258 81 RRRIGMIFQH-FNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELF 228
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-218 |
1.82e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 202.62 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGD---ALTIDNVWDK 79
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:COG1135 81 RRKIGMIFQH-FNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 160 KIIILDEATSMLDPEGR---LDLIKivrEIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG1135 160 KVLLCDEATSALDPETTrsiLDLLK---DINRELGLTIVLITHEMDVVrRICDRVAVLENGRI 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-228 |
1.35e-62 |
|
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: 197.57 E-value: 1.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnVWDKR--- 80
Cdd:COG1120 1 MLEAENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA---SLSRRela 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFvGATVEDDVAFG----LENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:COG1120 75 RRIAYVPQEPPAPF-GLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELF 228
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAArYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-227 |
1.71e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 196.82 E-value: 1.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRlIG 84
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:COG1131 77 YVPQEP-ALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDEL 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
3.05e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 195.65 E-value: 3.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTI--DNVW 77
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DK--RRLIGMVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVV 155
Cdd:COG1136 81 ARlrRRHIGFVFQFF-NLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESIS 222
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-202 |
8.42e-62 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 193.41 E-value: 8.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 17 EDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID--NVWDKRRLIGMVFQNPDNQF 94
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSrkGLLERRQRVGLVFQDPDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 95 VGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE 174
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*...
gi 251820877 175 GRLDLIKIVREIKERhGMTVISITHDLD 202
Cdd:TIGR01166 162 GREQMLAILRRLRAE-GMTVVISTHDVD 188
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-218 |
9.36e-62 |
|
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: 194.25 E-value: 9.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNV-WDK-- 79
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtDISKLSEKeLAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:cd03255 81 RRHIGFVFQSF-NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-230 |
1.02e-61 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 198.45 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIdNVWDKRRLIG 84
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnqfvgA-----TVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:COG1118 79 FVFQHY------AlfphmTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREI-KERHGMTVIsITHDLDEV-ALSDRVIVMKNGQVESISTPNELFMR 230
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVF-VTHDQEEAlELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-228 |
6.64e-61 |
|
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: 192.45 E-value: 6.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRRLIG 84
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03300 76 TVFQNY-ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELF 228
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEaLTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-229 |
1.86e-59 |
|
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: 190.16 E-value: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL----IGMVFQN----PDNqf 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSfallPHR-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 95 vgaTVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE 174
Cdd:cd03294 118 ---TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 175 GRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELFM 229
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEaLRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
2.02e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 189.05 E-value: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNV-WDK-RR 81
Cdd:COG1126 1 MIEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdINKlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPdNQFVGATVEDDVAFGLEN-QGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:COG1126 78 KVGMVFQQF-NLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 161 IIILDEATSMLDPEgrldLIKIV----REIKERhGMTVISITHDLD---EVAlsDRVIVMKNGQVESISTPNELF 228
Cdd:COG1126 157 VMLFDEPTSALDPE----LVGEVldvmRDLAKE-GMTMVVVTHEMGfarEVA--DRVVFMDGGRIVEEGPPEEFF 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-218 |
1.14e-58 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 190.40 E-value: 1.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWD---KR 80
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK11153 82 RQIGMIFQH-FNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 161 IIILDEATSMLDPEGR---LDLIKivrEIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:PRK11153 161 VLLCDEATSALDPATTrsiLELLK---DINRELGLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-240 |
1.83e-58 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 188.13 E-value: 1.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAL--TIDNVWDKR 80
Cdd:PRK13636 4 YILKVEELNYNY--SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK13636 82 ESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVAL-SDRVIVMKNGQVESISTPNELFMREDL---VDL 236
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEKEMlrkVNL 241
|
....
gi 251820877 237 DLDR 240
Cdd:PRK13636 242 RLPR 245
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-228 |
1.79e-57 |
|
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: 183.86 E-value: 1.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVWDKRR 81
Cdd:cd03261 1 IELRGLTKSF---GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNpdnqfvGA-----TVEDDVAFGL-ENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVV 155
Cdd:cd03261 78 RMGMLFQS------GAlfdslTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELF 228
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-217 |
1.73e-56 |
|
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: 179.31 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT--IDNVWDKRRL 82
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPdNQFVGATVEDDVAFGLenqgipleemrsrvdealelvgmtdfktreparlSGGQKQRVAIAGVVALRPKII 162
Cdd:cd03229 78 IGMVFQDF-ALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQ 217
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAArLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
3.12e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 181.06 E-value: 3.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnvwDKR 80
Cdd:COG1121 3 MMPAIELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNP--DNQFVgATVEDDVAFGLENQ----GIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGV 154
Cdd:COG1121 75 RRIGYVPQRAevDWDFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 155 VALRPKIIILDEATSMLDPEGRLDLIKIVREIKeRHGMTVISITHDLDEVA-LSDRVIVMKNGQVESiSTPNELFMREDL 233
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVLTPENL 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-218 |
3.45e-56 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 180.25 E-value: 3.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVWDKR 80
Cdd:COG2884 1 MIRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQN----PDNqfvgaTVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:COG2884 79 RRIGVVFQDfrllPDR-----TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKeRHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVdRMPKRVLELEDGRL 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-258 |
9.49e-56 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 181.18 E-value: 9.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID----NVWD 78
Cdd:PRK13641 3 IKFENVDYIYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 79 KRRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAIAGVVAL 157
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 158 RPKIIILDEATSMLDPEGRLDLIKIVREIkERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFM-REDLVD 235
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKEIFSdKEWLKK 241
|
250 260
....*....|....*....|...
gi 251820877 236 LDLDRPFTTELASSLRQTGLDLP 258
Cdd:PRK13641 242 HYLDEPATSRFASKLEKGGFKFS 264
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-218 |
1.13e-55 |
|
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: 178.49 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID--NVWDKRRL 82
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkkNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNpDNQFVGATVEDDVAFGLEN-QGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKI 161
Cdd:cd03262 78 VGMVFQQ-FNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLD---EVAlsDRVIVMKNGQV 218
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGfarEVA--DRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
1.71e-55 |
|
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: 181.40 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA---ESGDIYIDGDALTIDNVWDK 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRL----IGMVFQNPDNqfvgA-----TVEDDVAFGLE-NQGIPLEEMRSRVDEALELVGMTD---FKTREPARLSGGQK 146
Cdd:COG0444 81 RKIrgreIQMIFQDPMT----SlnpvmTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 147 QRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQ-VESISTp 224
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAeIADRVAVMYAGRiVEEGPV- 235
|
....
gi 251820877 225 NELF 228
Cdd:COG0444 236 EELF 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-258 |
6.54e-55 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 178.78 E-value: 6.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwDK--- 79
Cdd:PRK13649 3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSK-NKdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 --RRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:PRK13649 82 qiRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMREDLVD 235
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
250 260
....*....|....*....|....
gi 251820877 236 -LDLDRPFTTELASSLRQTGLDLP 258
Cdd:PRK13649 241 eKQLGVPKITKFAQRLADRGISFS 264
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-227 |
8.64e-55 |
|
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: 188.12 E-value: 8.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTID-NVWdkRRL 82
Cdd:COG2274 474 IELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGiDLRQIDpASL--RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQnpDNQFVGATVEDDVAFGleNQGIPLEEMRsrvdEALELVGMTDFKTREP-----------ARLSGGQKQRVAI 151
Cdd:COG2274 551 IGVVLQ--DVFLFSGTIRENITLG--DPDATDEEII----EAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 152 AGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIkeRHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-236 |
1.66e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 178.89 E-value: 1.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYN--QEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-----DIYIDGDALT---- 72
Cdd:PRK13631 21 ILRVKNLYCVFDekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNNheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 73 -------IDNVWDKRRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGM-TDFKTREPARLSGG 144
Cdd:PRK13631 101 tnpyskkIKNFKELRRRVSMVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 145 QKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKeRHGMTVISITHDLDEV-ALSDRVIVMKNGQVESIST 223
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
250
....*....|...
gi 251820877 224 PNELFMREDLVDL 236
Cdd:PRK13631 260 PYEIFTDQHIINS 272
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-228 |
3.98e-54 |
|
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: 175.22 E-value: 3.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwdKRRLIG 84
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGATVEDDVAFGLE----NQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:cd03296 78 FVFQHY-ALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELF 228
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEaLEVADRVVVMNKGRIEQVGTPDEVY 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-218 |
2.05e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.69 E-value: 2.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:COG4619 1 LELEGLSFRV---GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGATVEDDVAFGLENQGIPLEemRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:COG4619 78 YVPQEP--ALWGGTVRDNLPFPFQLRERKFD--RERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-230 |
2.18e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 177.99 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnVWDKRRL-------IGMVFQNpdnqFv 95
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDIT---KLSKKELrelrrkkMSMVFQH----F- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 96 gA-----TVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSM 170
Cdd:COG4175 115 -AllphrTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 171 LDPEGRLDLIKIVREIKERHGMTVISITHDLDEvALS--DRVIVMKNGQVESISTPNELFMR 230
Cdd:COG4175 194 LDPLIRREMQDELLELQAKLKKTIVFITHDLDE-ALRlgDRIAIMKDGRIVQIGTPEEILTN 254
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-257 |
2.47e-53 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 175.20 E-value: 2.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-----DIYIDGDALTIDNVW 77
Cdd:PRK13645 7 IILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DKRRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELFMREDLVD 235
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
250 260
....*....|....*....|...
gi 251820877 236 -LDLDRPFTTELASSLRQTGLDL 257
Cdd:PRK13645 247 kIEIDPPKLYQLMYKLKNKGIDL 269
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-230 |
1.25e-52 |
|
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: 171.36 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQedeqYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRRLIG 84
Cdd:cd03299 1 LKVENLSKDWKE----FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03299 75 YVPQN-YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMR 230
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWaLADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-218 |
2.15e-52 |
|
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: 168.77 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGM 85
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQnpdnqfvgatveddvafglenqgipleemrsrvdeALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:cd03214 78 VPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVAL-SDRVIVMKNGQV 218
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-255 |
2.37e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 172.61 E-value: 2.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIdGDALTIDNVWDK-----R 80
Cdd:PRK13643 5 EKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKeikpvR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:PRK13643 84 KKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMREDLVDL-D 237
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDVFQEVDFLKAhE 242
|
250
....*....|....*...
gi 251820877 238 LDRPFTTELASSLRQTGL 255
Cdd:PRK13643 243 LGVPKATHFADQLQKTGA 260
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-258 |
3.57e-52 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 172.58 E-value: 3.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDI------------------ 64
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 65 YIDGDALT------IDNVWDKRRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGM-TDFKTRE 137
Cdd:PRK13651 83 VLEKLVIQktrfkkIKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 138 PARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNG 216
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVlEWTKRTIFFKDG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 251820877 217 QVESISTPNELFMRED-LVDLDLDRPFTTELASSLRQTGLDLP 258
Cdd:PRK13651 242 KIIKDGDTYDILSDNKfLIENNMEPPKLLNFVNKLEKKGIDVP 284
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-228 |
3.98e-52 |
|
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: 170.17 E-value: 3.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNpdnqfVG----ATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTD--FKTREPARLSGGQKQRVAIAGVVALR 158
Cdd:cd03295 79 YVIQQ-----IGlfphMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELF 228
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEaFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-216 |
4.95e-52 |
|
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: 169.25 E-value: 4.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaltidNVWDKRRLIGM 85
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQNPD-NQFVGATVEDDVAFGLENQ----GIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:cd03235 73 VPQRRSiDRDFPISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKeRHGMTVISITHDLDEV-ALSDRVIVMKNG 216
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-228 |
4.95e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 173.98 E-value: 4.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDalTIDNVWDKRR 81
Cdd:PRK09452 12 SPLVELRGISKSF---DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKI 161
Cdd:PRK09452 87 HVNTVFQSY-ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELF 228
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEaLTMSDRIVVMRDGRIEQDGTPREIY 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-227 |
2.12e-51 |
|
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: 168.13 E-value: 2.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEdeqYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGDIYIDGD---ALTIDNV 76
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKdiyDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 WDKRRlIGMVFQNPdNQFVGaTVEDDVAFGLENQGI-PLEEMRSRVDEALELVGMTD-FKTREPAR-LSGGQKQRVAIAG 153
Cdd:cd03260 78 ELRRR-VGMVFQKP-NPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDeVKDRLHALgLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhgMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNEL 227
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-228 |
3.72e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 167.62 E-value: 3.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYtlndvSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwdKRRLIG 84
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF-----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVaLRPK-III 163
Cdd:COG3840 75 MLFQE-NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VRKRpILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELF 228
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAArIADRVLLVADGRIAADGPTAALL 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
23-245 |
1.24e-50 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 170.03 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT-IDNV---WDKRRLIGMVFQNPdNQFVGAT 98
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkQSPVelrEVRRKKIGMVFQQF-ALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 99 VEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLD 178
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 179 LIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNEL-------FMREDLVDLDLDRPFTTE 245
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEaIRIGDRIVIMKAGEIVQVGTPDEIlrnpaneYVEEFIGKVDLSQVFDAE 242
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-227 |
1.33e-50 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 166.57 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEdeqYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRlIG 84
Cdd:COG4555 2 IEVENLSKKYGKV---PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:COG4555 78 VLPDER-GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERHGMTVISiTHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFS-SHIMQEVeALCDRVVILHKGKVVAQGSLDEL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-227 |
1.49e-50 |
|
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: 174.18 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:COG4988 337 IELEDVSFSY--PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGATVEDDVAFGleNQGIPLEEMRsrvdEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAG 153
Cdd:COG4988 415 WVPQNP--YLFAGTIRENLRLG--RPDASDEELE----AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-218 |
4.60e-50 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 165.78 E-value: 4.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNL--KYKYN----QEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID 74
Cdd:COG4167 1 MSALLEVRNLskTFKYRtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 75 NVWDKRRLIGMVFQNPDNQF-----VGATVEddvafglenqgIPL--------EEMRSRVDEALELVGM----TDFKtre 137
Cdd:COG4167 81 DYKYRCKHIRMIFQDPNTSLnprlnIGQILE-----------EPLrlntdltaEEREERIFATLRLVGLlpehANFY--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 138 PARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNG 216
Cdd:COG4167 147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKhISDKVLVMHQG 226
|
..
gi 251820877 217 QV 218
Cdd:COG4167 227 EV 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-221 |
4.63e-50 |
|
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: 163.96 E-value: 4.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRRLIG 84
Cdd:cd03301 1 VELENVTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQN----PDnqfvgATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:cd03301 76 MVFQNyalyPH-----MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESI 221
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEaMTMADRIAVMNDGQIQQI 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-217 |
5.41e-50 |
|
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: 162.55 E-value: 5.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:cd03228 1 IEFKNVSFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGATVEDDVafglenqgipleemrsrvdealelvgmtdfktreparLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03228 80 YVPQDP--FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIkeRHGMTVISITHDLDEVALSDRVIVMKNGQ 217
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-227 |
5.96e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.04 E-value: 5.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVwdkRR 81
Cdd:COG1132 340 IEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESL---RR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQnpDNQFVGATVEDDVAFGleNQGIPLEEMRsrvdEALELVGMTDFKTREP-----------ARLSGGQKQRVA 150
Cdd:COG1132 415 QIGVVPQ--DTFLFSGTIRENIRYG--RPDATDEEVE----EAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIkeRHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-228 |
1.94e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 166.06 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTID--NVWDKRRLIGMVFQNPdnqfVGA-- 97
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSgrELRPLRRRMQMVFQDP----YASln 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 98 ---TVEDDVAFGLENQGI-PLEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLD 172
Cdd:COG4608 110 prmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 173 PEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELF 228
Cdd:COG4608 190 VSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-227 |
2.33e-49 |
|
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: 162.54 E-value: 2.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwDKRRLIG 84
Cdd:cd03265 1 IEVENLVKKYGDFE---AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnqfvgaTVEDDVAfGLEN-------QGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVAL 157
Cdd:cd03265 77 IVFQDL-------SVDDELT-GWENlyiharlYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 158 RPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-218 |
3.02e-49 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 161.66 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALtidNVWDKRRLIGM 85
Cdd:cd03226 1 RIENISFSYK--KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQNPDNQFVGATVEDDVAFGLENQGIPLEemrsRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:cd03226 76 VMQDVDYQLFTDSVREELLLGLKELDAGNE----QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVAL-SDRVIVMKNGQV 218
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-227 |
8.71e-49 |
|
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: 161.13 E-value: 8.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTidNVWDKRRLI 83
Cdd:cd03263 1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRT--DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:cd03263 78 GYCPQF-DALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 164 LDEATSMLDPEGRLDLIKIVReiKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLIL--EVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-218 |
1.05e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 159.10 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTiDNVWDKRRLIG 84
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPDNqfvgatveddvafglenqgipleemrsrvdealelvgMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03230 77 YLPEEPSL-------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-241 |
1.06e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 163.03 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQED--EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGdaLTIDN-VWDK-- 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD--ITITHkTKDKyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 ---RRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVV 155
Cdd:PRK13646 81 rpvRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMR-EDL 233
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDkKKL 240
|
....*...
gi 251820877 234 VDLDLDRP 241
Cdd:PRK13646 241 ADWHIGLP 248
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-230 |
3.12e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 163.74 E-value: 3.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwdKRRLIGMVFQNPdNQFVGATVEDD 102
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI--QQRDICMVFQSY-ALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKI 182
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 251820877 183 VREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELFMR 230
Cdd:PRK11432 179 IRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-259 |
4.46e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 160.94 E-value: 4.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQYTLN-DVSFHVKQGewlsIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnvWDKRRL 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNlDFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD----YSKRGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGM------VFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:PRK13638 73 LALrqqvatVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISiTHDLDEV-ALSDRVIVMKNGQVESISTPNELFMREDLVD 235
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
250 260
....*....|....*....|....*
gi 251820877 236 -LDLDRPFTTELasslrQTGLDLPL 259
Cdd:PRK13638 232 qAGLTQPWLVKL-----HTQLGLPL 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-220 |
1.08e-47 |
|
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: 166.01 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGDIYIDGDALTIDNVWDKRRL---IGMVFQNPdnqfVGA-- 97
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPLrrrMQVVFQDP----FGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 98 ---TVEDDVAFGLENQGIPL--EEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSML 171
Cdd:COG4172 377 prmTVGQIIAEGLRVHGPGLsaAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 251820877 172 DPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQ-VES 220
Cdd:COG4172 457 DVSVQAQILDLLRDLQREHGLAYLFISHDLAVVrALAHRVMVMKDGKvVEQ 507
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-169 |
1.52e-47 |
|
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: 155.50 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPdNQFVGATVEDD 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDP-QLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 103 VAFGLENQGIPLEEMRSRVDEALELVGMTDFKTR----EPARLSGGQKQRVAIAGVVALRPKIIILDEATS 169
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-218 |
3.37e-47 |
|
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: 157.60 E-value: 3.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT---IDNVWdkRRLIGMVFQNPdNQFVGATV 99
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglpPHEIA--RLGIGRTFQIP-RLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLENQGIP----------LEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATS 169
Cdd:cd03219 93 LENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 251820877 170 MLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03219 173 GLNPEETEELAELIRELRER-GITVLLVEHDMDVVmSLADRVTVLDQGRV 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-218 |
5.11e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.53 E-value: 5.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQytLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL- 82
Cdd:COG3638 2 MLELRNLSKRYPGGTPA--LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 --IGMVFQNP---DNQfvgaTVEDDVAFGLENQ--------GIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRV 149
Cdd:COG3638 80 rrIGMIFQQFnlvPRL----SVLTNVLAGRLGRtstwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 150 AIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDeVAL--SDRVIVMKNGQV 218
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVD-LARryADRIIGLRDGRV 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-226 |
5.44e-47 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 157.63 E-value: 5.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnVWDKRRL-- 82
Cdd:PRK13548 3 LEARNLSVRLGG---RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA---DWSPAELar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 -IGMVFQNPDNQFvGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA----- 156
Cdd:PRK13548 77 rRAVLPQHSSLSF-PFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 157 -LRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVAL-SDRVIVMKNGQVESISTPNE 226
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-217 |
7.78e-47 |
|
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: 153.94 E-value: 7.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGM 85
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQnpdnqfvgatveddvafglenqgipleemrsrvdealelvgmtdfktreparLSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:cd00267 78 VPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQ 217
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
23-218 |
3.84e-46 |
|
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: 155.20 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLiGMV--FQNPdNQFVGATVE 100
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-GIArtFQNP-RLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 101 DDVAFGLENQG---------------IPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:COG0411 98 ENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVmGLADRIVVLDFGRV 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-228 |
1.29e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 157.30 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRRLI 83
Cdd:PRK11607 19 LLEIRNLTKSF---DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:PRK11607 94 NMMFQSY-ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELF 228
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-218 |
4.23e-45 |
|
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: 152.34 E-value: 4.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-- 82
Cdd:cd03256 1 IEVENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 -IGMVFQNPdnQFVG-ATVEDDVAFGLENQ--------GIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIA 152
Cdd:cd03256 79 qIGMIFQQF--NLIErLSVLENVLSGRLGRrstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDeVALS--DRVIVMKNGQV 218
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVD-LAREyaDRIVGLKDGRI 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-218 |
6.38e-45 |
|
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: 149.12 E-value: 6.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-IGMVFQnpdnqfvgatved 101
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 dvafglenqgipleemrsrvdealelvgmtdfktreparLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIK 181
Cdd:cd03216 83 ---------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 251820877 182 IVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03216 124 VIRRLRAQ-GVAVIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-218 |
1.23e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 157.49 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-IGMVFQNPdNQFVGATVED 101
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQEL-NLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAFGLENQGIPL---EEMRSRVDEALELVGMtDFKTREPAR-LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRL 177
Cdd:COG1129 99 NIFLGREPRRGGLidwRAMRRRARELLARLGL-DIDPDTPVGdLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 251820877 178 DLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG1129 178 RLFRIIRRLKAQ-GVAIIYISHRLDEVfEIADRVTVLRDGRL 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-227 |
4.96e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.47 E-value: 4.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDK--RR 81
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERliRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNpDNQFVGATVEDDVAFG-LENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK09493 78 EAGMVFQQ-FYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKErHGMTVISITHDLD---EVAlsDRVIVMKNGQVESISTPNEL 227
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGfaeKVA--SRLIFIDKGRIAEDGDPQVL 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-227 |
6.50e-43 |
|
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: 153.77 E-value: 6.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVwdkRR 81
Cdd:COG4987 334 LELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlRDLDEDDL---RR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPDnqFVGATVEDDVAFGleNQGIPLEEMRsrvdEALELVGMTDFKTREP-----------ARLSGGQKQRVA 150
Cdd:COG4987 410 RIAVVPQRPH--LFDTTLRENLRLA--RPDATDEELW----AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIkeRHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEA--LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-227 |
9.15e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 149.46 E-value: 9.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDalTIDNVWDKRRLIG 84
Cdd:PRK10851 3 IEIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGATVEDDVAFGL----ENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK10851 78 FVFQHY-ALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNEL 227
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEaMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-233 |
9.65e-43 |
|
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: 146.09 E-value: 9.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNVWdKRRLI 83
Cdd:cd03252 1 ITFEHVRFRY-KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhDLALADPAW-LRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQnpDNQFVGATVEDDVAfgLENQGIPLEemrsRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIA 152
Cdd:cd03252 79 GVVLQ--ENVLFNRSIRDNIA--LADPGMSME----RVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKErhGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMRED 232
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
.
gi 251820877 233 L 233
Cdd:cd03252 229 L 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-228 |
1.63e-42 |
|
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: 152.15 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE----SGDIYIDGDALTIDN 75
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEaVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 VWDKRRL----IGMVFQ------NPDNqfvgaTVEDDVAFGLE-NQGIPLEEMRSRVDEALELVGMtdfktREPAR---- 140
Cdd:COG4172 83 ERELRRIrgnrIAMIFQepmtslNPLH-----TIGKQIAEVLRlHRGLSGAAARARALELLERVGI-----PDPERrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 141 ----LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGR---LDLIKivrEIKERHGMTVISITHDLDEVA-LSDRVIV 212
Cdd:COG4172 153 yphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQaqiLDLLK---DLQRELGMALLLITHDLGVVRrFADRVAV 229
|
250
....*....|....*..
gi 251820877 213 MKNGQ-VESISTPnELF 228
Cdd:COG4172 230 MRQGEiVEQGPTA-ELF 245
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-227 |
1.69e-42 |
|
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: 145.37 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGATVEDDVAFGLENQgiPLEEmrsrVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAG 153
Cdd:cd03249 81 LVSQEP--VLFDGTIAENIRYGKPDA--TDEE----VEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRldliKIVREI--KERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESE----KLVQEAldRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-241 |
1.84e-42 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 144.92 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNvwdKRRLIgmVFQNPdNQFVGATVEDD 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG---PDRMV--VFQNY-SLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLE--NQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLI 180
Cdd:TIGR01184 75 IALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 181 KIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESIStpnelfmreDLVDLDLDRP 241
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEaLLLSDRVVMLTNGPAANIG---------QILEVPFPRP 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-234 |
2.78e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 145.26 E-value: 2.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:COG4559 2 LEAENLSVRLGG---RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPDNQFvGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGV-------VAL 157
Cdd:COG4559 79 VLPQHSSLAF-PFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 158 RPKIIILDEATSMLDPEGRLDLIKIVREIKeRHGMTVISITHDLDEVAL-SDRVIVMKNGQVESISTPNELfMREDLV 234
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGTPEEV-LTDELL 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-222 |
2.21e-41 |
|
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: 141.66 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHVKqGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGdaltidNVWD----------KRRLIGMVFQNpDNQF 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG------TVLFdsrkkinlppQQRKIGLVFQQ-YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 95 VGATVEDDVAFGLenQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE 174
Cdd:cd03297 88 PHLNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 251820877 175 GRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESIS 222
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-240 |
2.79e-41 |
|
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: 145.63 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAL--TIDNVW---DKRRlIGMVFQNPdNQFVGATV 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFlppHRRR-IGYVFQEA-RLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLENqgIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDL 179
Cdd:COG4148 95 RGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 180 IKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMREDLVDLDLDR 240
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVArLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGE 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-248 |
3.02e-41 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 145.37 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDalTIDNVWDKRR 81
Cdd:PRK11650 1 MAGLKLQAVRKSY--DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR--VVNELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQN----PDnqfvgATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVAL 157
Cdd:PRK11650 77 DIAMVFQNyalyPH-----MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 158 RPKIIILDEATSMLDPEGRldlIKIVREIKERH---GMTVISITHD-LDEVALSDRVIVMKNGQVESISTPNELFmredl 233
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLR---VQMRLEIQRLHrrlKTTSLYVTHDqVEAMTLADRVVVMNGGVAEQIGTPVEVY----- 223
|
250
....*....|....*
gi 251820877 234 vdldlDRPFTTELAS 248
Cdd:PRK11650 224 -----EKPASTFVAS 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-218 |
4.86e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.87 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-IGMVFQNPdnQFVGA-TVE 100
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHF--MLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 101 DDVAFGLENQG---IPLEEMRSRVDEALELVGMT-DFKTRePARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGR 176
Cdd:COG3845 99 ENIVLGLEPTKggrLDRKAARARIRELSERYGLDvDPDAK-VEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 251820877 177 LDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG3845 178 DELFEILRRLAAE-GKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-218 |
1.52e-40 |
|
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: 139.47 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDK-----RRLIGMVFQnpDNQFV-G 96
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGRaipylRRKIGVVFQ--DFRLLpD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 97 ATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGR 176
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 251820877 177 LDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:cd03292 173 WEIMNLLKKINKA-GTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-226 |
1.60e-40 |
|
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: 140.26 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT-IDNvwDKR 80
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaLDE--DAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 -----RLIGMVFQNpdNQFVGA-TVeddvafgLENQGIPLE-----EMRSRVDEALELVGMTDFKTREPARLSGGQKQRV 149
Cdd:COG4181 85 arlraRHVGFVFQS--FQLLPTlTA-------LENVMLPLElagrrDARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 150 AIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNE 226
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
1.66e-40 |
|
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: 139.15 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMniIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwDKR 80
Cdd:COG4133 1 MM--LEAENLSCRR---GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFqnPDNQFVGA-TVEDDVAFGLENQGIPLEemRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:COG4133 75 RRLAYLG--HADGLKPElTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISiTHDLDEVAlSDRVIVMKN 215
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT-THQPLELA-AARVLDLGD 204
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-227 |
1.08e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 138.20 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDK---R 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ--ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQ------------NPDNQFVGATVEDDVAFGLENqgiplEEMRSRVDEALELVGMTDFKTREPARLSGGQKQR 148
Cdd:TIGR02315 79 RRIGMIFQhynlierltvleNVLHGRLGYKPTWRSLLGRFS-----EEDKERALSALERVGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 149 VAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-228 |
1.73e-39 |
|
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: 137.36 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEdeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNVWdKRRLI 83
Cdd:cd03254 3 IEFENVNFSYDEK--KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGiDIRDISRKS-LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPdNQFVGaTVEDDVAFGleNQGIPLEEmrsrVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIA 152
Cdd:cd03254 80 GVVLQDT-FLFSG-TIMENIRLG--RPNATDEE----VIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGRLDLIKIVREIkeRHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELF 228
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-218 |
2.96e-39 |
|
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: 136.57 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNVwDKRRLI 83
Cdd:cd03245 3 IEFRNVSFSYP-NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtDIRQLDPA-DLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPdnQFVGATVEDDVAFGLenqgiPLEEMRsRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIA 152
Cdd:cd03245 81 GYVPQDV--TLFYGTLRDNITLGA-----PLADDE-RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKErhGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-218 |
1.11e-38 |
|
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: 135.98 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL-EAESGDIYIDGDALTIDNVWDKR 80
Cdd:COG1119 1 DPLLELRNVTVRRG---GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVfqNPD--NQF-VGATVEDDVAFGLENQ-GI---PLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAG 153
Cdd:COG1119 78 KRIGLV--SPAlqLRFpRDETVLDVVLSGFFDSiGLyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALS-DRVIVMKNGQV 218
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-228 |
1.21e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.08 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDgLLE-AESGDIYIDGDALTID-------NV 76
Cdd:COG4598 9 LEVRDLHKSFGDLE---VLKGVSLTARKGDVISIIGSSGSGKSTFLRCIN-LLEtPDSGEIRVGGEEIRLKpdrdgelVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 WDKRRL------IGMVFQNpDNQFVGATVeddvafgLEN--------QGIPLEEMRSRVDEALELVGMTDFKTREPARLS 142
Cdd:COG4598 85 ADRRQLqrirtrLGMVFQS-FNLWSHMTV-------LENvieapvhvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 143 GGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKErHGMTVISITHDLD---EValSDRVIVMKNGQVE 219
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGfarDV--SSHVVFLHQGRIE 233
|
....*....
gi 251820877 220 SISTPNELF 228
Cdd:COG4598 234 EQGPPAEVF 242
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-218 |
1.31e-38 |
|
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: 134.63 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWlSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTiDNVWDKRRLIG 84
Cdd:cd03264 1 LQLENLTKRY---GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQ--NPDNQFvgaTVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKII 162
Cdd:cd03264 76 YLPQefGVYPNF---TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVALS-DRVIVMKNGQV 218
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLcNQVAVLNKGKL 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-227 |
2.93e-38 |
|
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: 134.28 E-value: 2.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGaTVEDDVAFGLENqgipleEMRSRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAG 153
Cdd:cd03251 80 LVSQDV-FLFND-TVAENIAYGRPG------ATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRldliKIVREIKER--HGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESE----RLVQAALERlmKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
3.52e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 134.78 E-value: 3.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGDIYIDGDaltidN 75
Cdd:COG1117 8 LEPKIEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGE-----D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 VWDK-------RRLIGMVFQNPdNQFVgATVEDDVAFGLENQGI-PLEEMRSRVDEALELVGMTD-FKTR--EPA-RLSG 143
Cdd:COG1117 80 IYDPdvdvvelRRRVGMVFQKP-NPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDeVKDRlkKSAlGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 144 GQKQRVAIAGVVALRPKIIILDEATSMLDP------EgrlDLIkivREIKERHgmTVISITHDLDEVA-LSDRVIVMKNG 216
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPistakiE---ELI---LELKKDY--TIVIVTHNMQQAArVSDYTAFFYLG 229
|
250
....*....|....
gi 251820877 217 QVESISTPNELFMR 230
Cdd:COG1117 230 ELVEFGPTEQIFTN 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-228 |
4.52e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 138.24 E-value: 4.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGdaLTIDNVWD------KRRLIGMVFQNpDNQFVG 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDaelrevRRKKIAMVFQS-FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 97 ATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGR 176
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 177 LDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELF 228
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-218 |
4.64e-38 |
|
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: 133.00 E-value: 4.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFH-----------VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwdKRRLIGMVFQNpD 91
Cdd:cd03298 3 LDKIRFSygeqpmhfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP--ADRPVSMLFQE-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 92 NQFVGATVEDDVAFGLeNQGIPL-EEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSM 170
Cdd:cd03298 80 NLFAHLTVEQNVGLGL-SPGLKLtAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 251820877 171 LDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAkRLAQRVVFLDNGRI 207
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-233 |
2.13e-37 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 139.71 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR03797 452 IEVDRVTFRY-RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNpdNQFVGATVEDDVAFGlenQGIPLEEmrsrVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAG 153
Cdd:TIGR03797 531 VVLQN--GRLMSGSIFENIAGG---APLTLDE----AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIAR 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRldliKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMREDL 233
Cdd:TIGR03797 602 ALVRKPRILLFDEATSALDNRTQ----AIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGL 677
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-227 |
2.42e-37 |
|
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: 131.97 E-value: 2.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVwdkRR 81
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSL---RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQnpDNQFVGATVEDDVAFGleNQGIPLEEMRsrvdEALELVGMTDFKTREP-----------ARLSGGQKQRVA 150
Cdd:cd03253 76 AIGVVPQ--DTVLFNDTIGYNIRYG--RPDATDEEVI----EAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKErhGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-218 |
2.49e-37 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 132.99 E-value: 2.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNL----KYKYNQEDEQY--TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID 74
Cdd:PRK15112 1 VETLLEVRNLsktfRYRTGWFRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 75 NVWDKRRLIGMVFQNPDN-----QFVGATVedDVAFGLeNQGIPLEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQR 148
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTslnprQRISQIL--DFPLRL-NTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 149 VAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKhISDQVLVMHQGEV 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-219 |
3.91e-37 |
|
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: 137.96 E-value: 3.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIdnvWDKRRL-- 82
Cdd:COG4618 331 LSVENLTVVP-PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ---WDREELgr 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 -IGMVFQNPdnQFVGATVEDDVA-FGlenqgiplEEMRSRVDEALELVGMTD--------FKTR---EPARLSGGQKQRV 149
Cdd:COG4618 407 hIGYLPQDV--ELFDGTIAENIArFG--------DADPEKVVAAAKLAGVHEmilrlpdgYDTRigeGGARLSGGQRQRI 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 150 AIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVMKNGQVE 219
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-218 |
5.01e-37 |
|
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: 129.26 E-value: 5.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:cd03246 1 LEVENVSFRY-PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNpDNQFVGaTVEDDVafglenqgipleemrsrvdealelvgmtdfktreparLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03246 80 YLPQD-DELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-213 |
8.78e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 131.14 E-value: 8.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKY-NQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDnvwDKR 80
Cdd:COG4525 1 MSMLTVRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP---GAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RliGMVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:COG4525 78 R--GVVFQK-DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDE-VALSDRVIVM 213
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEaLFLATRLVVM 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-218 |
9.02e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 130.47 E-value: 9.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYTLndvsfHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRRLIG 84
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFDL-----TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNpDNQFVGATVEDDVAFGLeNQGIPL-EEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:PRK10771 75 MLFQE-NNLFSHLTVAQNIGLGL-NPGLKLnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAArIAPRSLVVADGRI 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-228 |
1.79e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 130.26 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIdGDaLTIDN------ 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHG---QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GD-ITIDTarslsq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 ----VWDKRRLIGMVFQNpDNQFVGATVEDDVAFG-LENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVA 150
Cdd:PRK11264 76 qkglIRQLRQHVGFVFQN-FNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVIsITHDLD---EVAlsDRVIVMKNGQVESISTPNEL 227
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSfarDVA--DRAIFMDQGRIVEQGPAKAL 231
|
.
gi 251820877 228 F 228
Cdd:PRK11264 232 F 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-234 |
3.19e-36 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 129.93 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYN------QEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT-IDNV 76
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 WDK--RRLIGMVFQNPDNQF-VGATVEDDVAFGLEN-QGIPLEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAI 151
Cdd:TIGR02769 82 QRRafRRDVQLVFQDSPSAVnPRMTVRQIIGEPLRHlTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 152 AGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQ-VESISTPNELFM 229
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQiVEECDVAQLLSF 241
|
....*
gi 251820877 230 REDLV 234
Cdd:TIGR02769 242 KHPAG 246
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-218 |
3.92e-36 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 128.17 E-value: 3.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDnvwdKRRLIG 84
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA----ARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVfqnPDNQ--FVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKII 162
Cdd:cd03269 74 YL---PEERglYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVeELCDRVLLLNKGRA 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-218 |
6.64e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 6.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnvWDKRRLI 83
Cdd:COG4152 1 MLELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 G-----------MvfqnpdnqfvgaTVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIA 152
Cdd:COG4152 74 GylpeerglypkM------------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGRlDLIK-IVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNV-ELLKdVIRELAAK-GTTVIFSSHQMELVeELCDRIVIINKGRK 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-233 |
9.34e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 131.00 E-value: 9.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAL-----TIDNVWDKRRlIGMVFQNPdNQFVGATV 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkGIFLPPEKRR-IGYVFQEA-RLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLENQGIPleEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDL 179
Cdd:TIGR02142 93 RGNLRYGMKRARPS--ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 180 IKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMREDL 233
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLrLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-233 |
1.92e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.51 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnVWDKRRL-- 82
Cdd:COG4604 2 IEIKNVSKRYGG---KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA---TTPSRELak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 -IGMVFQnpDNQFVGA-TVEDDVAFGL--ENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALR 158
Cdd:COG4604 76 rLAILRQ--ENHINSRlTVRELVAFGRfpYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELfMREDL 233
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAScYADHIVAMKDGRVVAQGTPEEI-ITPEV 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-218 |
2.66e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.10 E-value: 2.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIyIDGDALTIDNVWDKRrligMVFQnpDNQFVG-ATVED 101
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTR----LMFQ--DARLLPwKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAFGLENQgipleeMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIK 181
Cdd:PRK11247 101 NVGLGLKGQ------WRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQD 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 251820877 182 IVREIKERHGMTVISITHDLDE-VALSDRVIVMKNGQV 218
Cdd:PRK11247 175 LIESLWQQHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-215 |
4.53e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 125.29 E-value: 4.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGDIYIDGDALTIDNVwdKRRLIGMVFQNpDNQFVGATVED 101
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRIGILFQD-DLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAFGLENqGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIK 181
Cdd:COG4136 96 NLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180 190
....*....|....*....|....*....|....
gi 251820877 182 IVREIKERHGMTVISITHDLDEVALSDRVIVMKN 215
Cdd:COG4136 175 FVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-223 |
5.31e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.73 E-value: 5.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKY------NQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDN 75
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 VWDK---RRLIGMVFQNPdnqfVGA-----TVEDDVAFGLEN-QGIPLEEMRSRVDEALELVGMTD-FKTREPARLSGGQ 145
Cdd:PRK10419 81 RAQRkafRRDIQMVFQDS----ISAvnprkTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 146 KQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQ-VESIST 223
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVErFCQRVMVMDNGQiVETQPV 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-218 |
6.84e-35 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 124.64 E-value: 6.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAltIDNVWDKRRLIG 84
Cdd:cd03268 1 LKTNDLTKTYG---KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGA-TVEDDVAFGLENQGIPleemRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:cd03268 76 ALIEAP--GFYPNlTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQkVADRIGIINKGKL 204
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-213 |
1.20e-34 |
|
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: 130.87 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR02857 322 LEFSGVSVAY--PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGATVEDDVAFGLenqgipLEEMRSRVDEALELVGMTDF-KTRE----------PARLSGGQKQRVAIAG 153
Cdd:TIGR02857 400 WVPQHP--FLFAGTIAENIRLAR------PDASDAEIREALERAGLDEFvAALPqgldtpigegGAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVALSDRVIVM 213
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-218 |
1.56e-34 |
|
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: 124.14 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDnVWDKRRLI 83
Cdd:cd03244 3 IEFKNVSLRYR-PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDISKIG-LHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPdnQFVGATVEDDVAfglenqgiPLEEMR-SRVDEALELVGMTDFKTREPARL-----------SGGQKQRVAI 151
Cdd:cd03244 81 SIIPQDP--VLFSGTIRSNLD--------PFGEYSdEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 152 AGVVALRPKIIILDEATSMLDPEGRLDLIKIVREikERHGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-232 |
1.86e-34 |
|
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: 124.19 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-I 83
Cdd:cd03218 1 LRAENLSKRYG---KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:cd03218 78 GYLPQEA-SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERhGMTVIsIT-HDLDE-VALSDRVIVMKNGQVESISTPNELFMRED 232
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDR-GIGVL-ITdHNVREtLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-233 |
3.76e-34 |
|
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: 129.84 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR02203 331 VEFRNVTFRY-PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQnpDNQFVGATVEDDVAFGlENQGIPleemRSRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAG 153
Cdd:TIGR02203 410 LVSQ--DVVLFNDTIANNIAYG-RTEQAD----RAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 154 VVALRPKIIILDEATSMLDPEG-RLDLIKIVREIKERhgmTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMRED 232
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESeRLVQAALERLMQGR---TTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
.
gi 251820877 233 L 233
Cdd:TIGR02203 560 L 560
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-213 |
5.46e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.96 E-value: 5.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaltidnvwdkrRLIGMVFQN---PDNqfVGATV 99
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRsevPDS--LPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLENQGIPLE----EMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEG 175
Cdd:NF040873 75 RDLVAMGRWARRGLWRrltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 251820877 176 RLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVM 213
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-228 |
6.03e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 126.30 E-value: 6.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALtiDNVWDKRRLIGMVFQN----PDnqfvgATV 99
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM--NDVPPAERGVGMVFQSyalyPH-----LSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDL 179
Cdd:PRK11000 93 AENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 251820877 180 -IKIVReIKERHGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELF 228
Cdd:PRK11000 173 rIEISR-LHKRLGRTMIYVTHDQVEaMTLADKIVVLDAGRVAQVGKPLELY 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-218 |
8.08e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 123.66 E-value: 8.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQE--DEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRR 81
Cdd:COG1101 1 MLELKNLSKTFNPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPdnqFVG----ATVEDDVA--------FGLeNQGIpLEEMRSRVDEALELVGMtDFKTREPAR---LSGGQK 146
Cdd:COG1101 81 YIGRVFQDP---MMGtapsMTIEENLAlayrrgkrRGL-RRGL-TKKRRELFRELLATLGL-GLENRLDTKvglLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 147 QrvAIAGVVAL--RPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDL-DEVALSDRVIVMKNGQV 218
Cdd:COG1101 155 Q--ALSLLMATltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeQALDYGNRLIMMHEGRI 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-228 |
1.53e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 124.43 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYN-QEDEQY------TL---NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT- 72
Cdd:PRK15079 8 LLEVADLKVHFDiKDGKQWfwqppkTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 73 -IDNVW-DKRRLIGMVFQ------NPDnqfvgATVEDDVAFGLE--NQGIPLEEMRSRVDEALELVGM-TDFKTREPARL 141
Cdd:PRK15079 88 mKDDEWrAVRSDIQMIFQdplaslNPR-----MTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 142 SGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVES 220
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKhISDRVLVMYLGHAVE 242
|
....*...
gi 251820877 221 ISTPNELF 228
Cdd:PRK15079 243 LGTYDEVY 250
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-218 |
2.24e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 121.66 E-value: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDgLLE-AESGDIYIDG------DALTIDNVW 77
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLEtPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DKRRLIGMVFQNPdNQFVGATVEDD-VAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:COG4161 79 LLRQKVGMVFQQY-NLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLdEVA--LSDRVIVMKNGQV 218
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEV-EFArkVASQVVYMEKGRI 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-233 |
2.35e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 127.13 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 18 DEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIdglleAESGDIYIDGDALtidNVWDKRRL------IGMVF 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQPL---HNLNRRQLlpvrhrIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 88 QNPDNQF-VGATVEDDVAFGLENQGIPL--EEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:PRK15134 369 QDPNSSLnPRLNVLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV------ESI-STPNELFMREDL 233
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQGEVveqgdcERVfAAPQQEYTRQLL 526
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-218 |
3.10e-33 |
|
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: 121.00 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-I 83
Cdd:cd03224 1 LEVENLNAGYGKSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPDNqFVGATVEDDVAFGLENQGIplEEMRSRVDEALELVgmTDFKTREPAR---LSGGQKQRVAIAGVVALRPK 160
Cdd:cd03224 78 GYVPEGRRI-FPELTVEENLLLGAYARRR--AKRKARLERVYELF--PRLKERRKQLagtLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFAlEIADRAYVLERGRV 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-218 |
5.71e-33 |
|
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: 120.17 E-value: 5.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTidNVWDKRR 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVK--EPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNpDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKI 161
Cdd:cd03266 79 RLGFVSDS-TGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVeRLCDRVVVLHRGRV 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-218 |
6.18e-33 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 120.27 E-value: 6.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLI 83
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPdnQFVGATVEDDVAFGLenQGIPLEemrsRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIA 152
Cdd:cd03248 91 SLVGQEP--VLFARSLQDNIAYGL--QSCSFE----CVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-233 |
9.67e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 126.76 E-value: 9.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT-IDNVWdK 79
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqYDHHY-L 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNPdnQFVGATVEDDVAFGLenQGIPLEEMRSRVDEAlelvGMTDFKTREP-----------ARLSGGQKQR 148
Cdd:TIGR00958 554 HRQVALVGQEP--VLFSGSVRENIAYGL--TDTPDEEIMAAAKAA----NAHDFIMEFPngydtevgekgSQLSGGQKQR 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 149 VAIAGVVALRPKIIILDEATSMLDPEGRldliKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELF 228
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
....*
gi 251820877 229 MREDL 233
Cdd:TIGR00958 702 EDQGC 706
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-218 |
3.00e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKY--NQedeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDgLLE-AESGDIYIDGDALTIDNVWDK-- 79
Cdd:PRK11124 3 IQLNGINCFYgaHQ-----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN-LLEmPRSGTLNIAGNHFDFSKTPSDka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 ----RRLIGMVFQNPdNQFVGATVeddvafgLEN--------QGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQ 147
Cdd:PRK11124 77 irelRRNVGMVFQQY-NLWPHLTV-------QQNlieapcrvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLdEVA--LSDRVIVMKNGQV 218
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEV-EVArkTASRVVYMENGHI 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-230 |
3.18e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.84 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNVWDK--RRLIGMVFQNP-----DNQF 94
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqDLLKADPEAQKllRQKIQIVFQNPygslnPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 95 VGATVEDDVAFgleNQGIPLEEMRSRVDEALELVGM-TDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDP 173
Cdd:PRK11308 111 VGQILEEPLLI---NTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 174 EGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMR 230
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-232 |
1.36e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.94 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKynqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGD---ALTIDNVW 77
Cdd:PRK11831 4 VANLVDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DKRRLIGMVFQNpDNQFVGATVEDDVAFGL-ENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:PRK11831 81 TVRKRMSMLFQS-GALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELFMRED 232
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-227 |
3.54e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.90 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRR 81
Cdd:COG1137 1 MMTLEAENLVKSYGK---RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 L-IGMVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:COG1137 78 LgIGYLPQEA-SIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERhGMTVIsIT-HDLDE-VALSDRVIVMKNGQVESISTPNEL 227
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVL-ITdHNVREtLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-235 |
3.54e-31 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 116.81 E-value: 3.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 10 LKYKYNQEDEQYTLNDVSFHVK-------------QGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALtidNV 76
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL---ES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 WDKRRLIGMVFQNPDN--QFVGATVEDDVAFG-------LENQGIpleEMRSRVDEALELVGMTDFKTREPARLSGGQKQ 147
Cdd:PRK10575 78 WSSKAFARKVAYLPQQlpAAEGMTVRELVAIGrypwhgaLGRFGA---ADREKVEEAISLVGLKPLAHRLVDSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNE 226
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAE 234
|
....*....
gi 251820877 227 LfMREDLVD 235
Cdd:PRK10575 235 L-MRGETLE 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-245 |
3.84e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 117.88 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNL--KYKYNQEDE------------QYT----LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIY 65
Cdd:COG4586 1 IIEVENLskTYRVYEKEPglkgalkglfrrEYReveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 66 IDGDaltidNVWDKR----RLIGMVFqnpdnqfvgatveddvafGLENQ------------------GIPLEEMRSRVDE 123
Cdd:COG4586 81 VLGY-----VPFKRRkefaRRIGVVF------------------GQRSQlwwdlpaidsfrllkaiyRIPDAEYKKRLDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 124 ALELVGMTDFKTRePAR-LSGGQKQRVAIAGvvAL--RPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHD 200
Cdd:COG4586 138 LVELLDLGELLDT-PVRqLSLGQRMRCELAA--ALlhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 251820877 201 LDEV-ALSDRVIVMKNGQV---ESISTPNELFMREDLVDLDLDRPFTTE 245
Cdd:COG4586 215 MDDIeALCDRVIVIDHGRIiydGSLEELKERFGPYKTIVLELAEPVPPL 263
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
5.56e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.56 E-value: 5.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNL--KYKYNQE-----------------DEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES 61
Cdd:COG1134 1 MSSMIEVENVskSYRLYHEpsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 62 GDIYIDGD--ALtIDnvwdkrrlIGMVFqNPDnqfvgATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDF-----K 134
Cdd:COG1134 81 GRVEVNGRvsAL-LE--------LGAGF-HPE-----LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFidqpvK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 135 TreparLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVM 213
Cdd:COG1134 146 T-----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRrLCDRAIWL 219
|
250
....*....|...
gi 251820877 214 KNGQVESISTPNE 226
Cdd:COG1134 220 EKGRLVMDGDPEE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-228 |
8.91e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 115.53 E-value: 8.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-------DALTIDNVwD 78
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkDIFQIDAI-K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 79 KRRLIGMVFQNPdNQFVGATVEDDVAFGLENQGIPLE-EMRSRVDEALELVGM----TDFKTREPARLSGGQKQRVAIAG 153
Cdd:PRK14246 88 LRKEVGMVFQQP-NPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhgMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELF 228
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-228 |
8.93e-31 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 8.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTI--DN----- 75
Cdd:PRK10619 4 NKLNVIDLHKRYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrDKdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 VWDKRRL------IGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTD-FKTREPARLSGGQKQR 148
Cdd:PRK10619 81 VADKNQLrllrtrLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 149 VAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKErHGMTVISITHDLdEVA--LSDRVIVMKNGQVESISTPNE 226
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEM-GFArhVSSHVIFLHQGKIEEEGAPEQ 238
|
..
gi 251820877 227 LF 228
Cdd:PRK10619 239 LF 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
2-228 |
1.15e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 116.76 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNQEDEQYTLND-VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE------AESgdIYIDGDALTID 74
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDrISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmAEK--LEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 75 NVWDKRRLIG----MVFQNPDNQFVGA-TVEDDVAFGLE-NQGIPLEEMRSRVDEALELVGMTDFKTR---EPARLSGGQ 145
Cdd:PRK11022 79 SEKERRNLVGaevaMIFQDPMTSLNPCyTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 146 KQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTP 224
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAeAAHKIIVMYAGQVVETGKA 238
|
....
gi 251820877 225 NELF 228
Cdd:PRK11022 239 HDIF 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-218 |
1.26e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 114.20 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVWDKRRLIGMVFQNpDNQFVGATV 99
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRRQIGMIFQD-HHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDL 179
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 251820877 180 IKIVREIKeRHGMTVISITHDLDEVALSD-RVIVMKNGQV 218
Cdd:PRK10908 177 LRLFEEFN-RVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-203 |
2.10e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.41 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAltIDNVWDKRrliGMVFQNpDNQFVGATVEDD 102
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGPGAER---GVVFQN-EGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKI 182
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170 180
....*....|....*....|.
gi 251820877 183 VREIKERHGMTVISITHDLDE 203
Cdd:PRK11248 171 LLKLWQETGKQVLLITHDIEE 191
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-218 |
3.83e-30 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 112.88 E-value: 3.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAltidnvWDKRRL-- 82
Cdd:TIGR03740 1 LETKNLSKRFGK---QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP------WTRKDLhk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPDnQFVGATVEDDVAFGLENQGIPleemRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKII 162
Cdd:TIGR03740 72 IGSLIESPP-LYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:TIGR03740 147 ILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQqLADHIGIISEGVL 202
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-201 |
6.77e-30 |
|
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: 117.46 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR02868 335 LELRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGATVEDDVAFGleNQGIPLEEMRsrvdEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAG 153
Cdd:TIGR02868 413 VCAQDA--HLFDTTVRENLRLA--RPDATDEELW----AALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIKErhGMTVISITHDL 201
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-218 |
8.31e-30 |
|
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: 117.61 E-value: 8.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-D--ALTIDNVwdkRRLIGMVFQnpDNQFVGATV 99
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqDirDVTQASL---RAAIGIVPQ--DTVLFNDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGleNQGIPLEEmrsrVDEALELVGMTDFKTREPA-----------RLSGGQKQRVAIAGVVALRPKIIILDEAT 168
Cdd:COG5265 449 AYNIAYG--RPDASEEE----VEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 251820877 169 SMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:COG5265 523 SALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-230 |
8.98e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.70 E-value: 8.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGDIYIDGDALTIDNV 76
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 WDKRRLIGMVFQNPdNQFVGATVEDDVAFGLENQGI--PLEEMRSRVDEALELVGMTD-FKTR--EPA-RLSGGQKQRVA 150
Cdd:PRK14247 78 IELRRRVQMVFQIP-NPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDeVKDRldAPAgKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhgMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFM 229
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAArISDYVAFLYKGQIVEWGPTREVFT 234
|
.
gi 251820877 230 R 230
Cdd:PRK14247 235 N 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-219 |
1.30e-29 |
|
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: 111.47 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 9 NLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGD-ALTIDnvwdkrrlIGMVF 87
Cdd:cd03220 24 GILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvSSLLG--------LGGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 88 QNpdnqfvGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEA 167
Cdd:cd03220 96 NP------ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 168 TSMLDPEGRLDLIKIVREIKErHGMTVISITHDLDEV-ALSDRVIVMKNGQVE 219
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIkRLCDRALVLEKGKIR 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-218 |
1.88e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 116.29 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 19 EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALtidNVWDKRRL---IGMVFQnpDNQFV 95
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL---KQWDRETFgkhIGYLPQ--DVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 96 GATVEDDVA-FGlenqgiplEEMRSR-VDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAGVVALRPKII 162
Cdd:TIGR01842 405 PGTVAENIArFG--------ENADPEkIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-218 |
1.90e-29 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 111.08 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDK-RRLIG 84
Cdd:TIGR03410 2 EVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPDnQFVGATVEDDVAFGLENQGiplEEMRSRVDEALELVG-MTDFKTREPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:TIGR03410 79 YVPQGRE-IFPRLTVEENLLTGLAALP---RRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFArELADRYYVMERGRV 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-234 |
3.92e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.87 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTI--DNVWDKR- 80
Cdd:PRK11231 2 TLRTENLTVGYG---TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlsSRQLARRl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDnqfvGATVEDDVAFG----LENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA 156
Cdd:PRK11231 79 ALLPQHHLTPE----GITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELfMREDLV 234
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASrYCDHLVVLANGHVMAQGTPEEV-MTPGLL 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-236 |
3.94e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 110.46 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRR 81
Cdd:COG0410 1 MPMLEVENLHAGY---GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 L-IGMVfqnPDNQ--FVGATVEDDVAFGLENQGiPLEEMRSRVDEALELvgmtdF---KTREPAR---LSGGQKQRVAIA 152
Cdd:COG0410 78 LgIGYV---PEGRriFPSLTVEENLLLGAYARR-DRAEVRADLERVYEL-----FprlKERRRQRagtLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELFMRE 231
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLADP 227
|
....*
gi 251820877 232 DLVDL 236
Cdd:COG0410 228 EVREA 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-227 |
4.36e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.83 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPdnQFVGATVEDD 102
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA--GLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLENQgiPLEEMRsrvdEALELVGMTDFKTREPA-----------RLSGGQKQRVAIAGVVALRPKIIILDEATSML 171
Cdd:PRK13657 429 IRVGRPDA--TDEEMR----AAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 172 DPEGRLDLIKIVREIkeRHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:PRK13657 503 DVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-229 |
5.20e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.64 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLID--GLLEAE---SGDIYIDGDAL---TIDN 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIyspRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 VwDKRRLIGMVFQNPdNQFvGATVEDDVAFGLENQGIpleEMRSRVDEALE--LVGMT---DFKTR---EPARLSGGQKQ 147
Cdd:PRK14239 82 V-DLRKEIGMVFQQP-NPF-PMSIYENVVYGLRLKGI---KDKQVLDEAVEksLKGASiwdEVKDRlhdSALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNE 226
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASrISDRTGFFLDGDLIEYNDTKQ 233
|
...
gi 251820877 227 LFM 229
Cdd:PRK14239 234 MFM 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-228 |
1.42e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.03 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNQEDEQYTL-NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGDIYIDGDALTIDn 75
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVvNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 vwDKRRL-------IGMVFQNPdnqFVGA----TVEDDVAFGLE-NQGIPLEEMRSRVDEALELVGMTDFKTR---EPAR 140
Cdd:PRK15134 82 --SEQTLrgvrgnkIAMIFQEP---MVSLnplhTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 141 LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVE 219
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCV 236
|
....*....
gi 251820877 220 SISTPNELF 228
Cdd:PRK15134 237 EQNRAATLF 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-227 |
1.95e-28 |
|
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: 113.36 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQY--TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIY-------IDGDALTID 74
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVvkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 75 NVWDKRRLIGMVFQNPDnQFVGATVEDDV--AFGLEnqgIPLEEMRSRVDEALELVGMTDFKTRE-----PARLSGGQKQ 147
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYD-LYPHRTVLDNLteAIGLE---LPDELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNE 226
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEE 514
|
.
gi 251820877 227 L 227
Cdd:TIGR03269 515 I 515
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
3.29e-28 |
|
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: 107.91 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLkYK----YNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID- 74
Cdd:COG4778 1 MTTLLEVENL-SKtftlHLQGGKRLPvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 75 ---------NVwdKRRLIGMVfqnpdNQF------VGAtvEDDVAFGLENQGIPLEEMRSRVDEALELVGMtdfktrePA 139
Cdd:COG4778 80 aqaspreilAL--RRRTIGYV-----SQFlrviprVSA--LDVVAEPLLERGVDREEARARARELLARLNL-------PE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 140 RL--------SGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRV 210
Cdd:COG4778 144 RLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVReAVADRV 222
|
....*..
gi 251820877 211 IVMKNGQ 217
Cdd:COG4778 223 VDVTPFS 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-228 |
3.88e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 113.03 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 19 EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG---DALTIDNVWDKRRLIGMVFQNP----- 90
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqriDTLSPGKLQALRRDIQFIFQDPyasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 91 DNQFVGATV-EDDVAFGLenqgIPLEEMRSRVDEALELVGMT-DFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEAT 168
Cdd:PRK10261 416 PRQTVGDSImEPLRVHGL----LPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 169 SMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELF 228
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVEIGPRRAVF 552
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-227 |
4.07e-28 |
|
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: 112.58 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQE--DEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL 82
Cdd:COG4615 328 LELRGVTYRYPGEdgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQnpD----NQFVGATVEDDVAfglenqgipleemrsRVDEALELVGMTD--------FKTREparLSGGQKQRVA 150
Cdd:COG4615 408 FSAVFS--DfhlfDRLLGLDGEADPA---------------RARELLERLELDHkvsvedgrFSTTD---LSQGQRKRLA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 151 IagVVAL---RPkIIILDEATSMLDPEGRldlikivR--------EIKERhGMTVISITHDLDEVALSDRVIVMKNGQVE 219
Cdd:COG4615 468 L--LVALledRP-ILVFDEWAADQDPEFR-------RvfytellpELKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
....*...
gi 251820877 220 SISTPNEL 227
Cdd:COG4615 537 ELTGPAAL 544
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
6.25e-28 |
|
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: 105.59 E-value: 6.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqedeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL- 82
Cdd:cd03215 4 VLEVRGLSVKG-------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVfqnPdnqfvgatvEDdvafglenqgipleemrsRVDEALelvgMTDFKTRE----PARLSGGQKQRVAIAGVVALR 158
Cdd:cd03215 77 IAYV---P---------ED------------------RKREGL----VLDLSVAEnialSSLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
8.94e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.24 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGDIYIDGDALTIDN 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGS---NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 V--WDKRRLIGMVFQNPdNQFVGATVEDDVAFGLENQGI--PLEEMRSRVDEALELVGMTD-FKTR---EPARLSGGQKQ 147
Cdd:PRK14267 78 VdpIEVRREVGMVFQYP-NPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDeVKDRlndYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNE 226
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAArVSDYVAFLYLGKLIEVGPTRK 234
|
..
gi 251820877 227 LF 228
Cdd:PRK14267 235 VF 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-261 |
9.49e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.87 E-value: 9.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYNQEDEQY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDN--VWDK 79
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRL------------IGMVFQNPDNQF-----VGATVEDDVAFgleNQGIPLEEMRSRVDEALELVGMTDFKT---REPA 139
Cdd:PRK10261 91 SEQsaaqmrhvrgadMAMIFQEPMTSLnpvftVGEQIAESIRL---HQGASREEAMVEAKRMLDQVRIPEAQTilsRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 140 RLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAeIADRVLVMYQGEA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 251820877 219 ESISTPNELFMREdlvdldlDRPFTTELASSLRQ----TGLDLPLRY 261
Cdd:PRK10261 248 VETGSVEQIFHAP-------QHPYTRALLAAVPQlgamKGLDYPRRF 287
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-228 |
1.19e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 108.66 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGdiYIDGDAL----TIDN 75
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANG--RIGGSATfngrEILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 VWDKR--RL----IGMVFQNPDNQF-----VGATVEDDVAF--GLENQGIPLEEMRsrvdeALELVGMTDFKTR---EPA 139
Cdd:PRK09473 86 LPEKElnKLraeqISMIFQDPMTSLnpymrVGEQLMEVLMLhkGMSKAEAFEESVR-----MLDAVKMPEARKRmkmYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 140 RLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQV 218
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAGRT 240
|
250
....*....|
gi 251820877 219 ESISTPNELF 228
Cdd:PRK09473 241 MEYGNARDVF 250
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-224 |
2.01e-27 |
|
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: 105.19 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDnVWDKRRLI 83
Cdd:cd03369 7 IEVENLSVRYAPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGiDISTIP-LEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPdNQFVGAtveddvafglenqgipleeMRSRVDEALElvgMTDFKTREPAR-------LSGGQKQRVAIAGVVA 156
Cdd:cd03369 85 TIIPQDP-TLFSGT-------------------IRSNLDPFDE---YSDEEIYGALRvsegglnLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 157 LRPKIIILDEATSMLDPEGRLDLIKIVREikERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTP 224
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2-245 |
2.16e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.16 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRR 81
Cdd:PRK09536 1 MPMIDVSDLSVEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPDNQF---VGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALR 158
Cdd:PRK09536 78 RVASVPQDTSLSFefdVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKErHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMREDLVDLD 237
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
....*...
gi 251820877 238 LDRPFTTE 245
Cdd:PRK09536 237 DARTAVGT 244
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-219 |
2.46e-27 |
|
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: 104.32 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTI--DNVwdkRRL 82
Cdd:cd03247 1 LSINNVSFSY-PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDleKAL---SSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPdnqFVGATVEddvafgLENQGIpleemrsrvdealelvgmtdfktrepaRLSGGQKQRVAIAGVVALRPKII 162
Cdd:cd03247 77 ISVLNQRP---YLFDTTL------RNNLGR---------------------------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 163 ILDEATSMLDPEGRLDLIKIVREIKErhGMTVISITHDLDEVALSDRVIVMKNGQVE 219
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-219 |
2.56e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.67 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 9 NLKYKYnQEDEQYT--LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL---- 82
Cdd:PRK11629 10 NLCKRY-QEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQN----PDnqfvgATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALR 158
Cdd:PRK11629 89 LGFIYQFhhllPD-----FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVE 219
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-213 |
3.55e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.18 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYkynQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL 82
Cdd:PRK10247 6 PLLQLQNVGY---LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPdnQFVGATVEDDVAFGLENQGIPLEEMRSRVDeaLELVGMTDFKTREP-ARLSGGQKQRVAIAGVVALRPKI 161
Cdd:PRK10247 83 VSYCAQTP--TLFGDTVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVM 213
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-228 |
2.32e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.96 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGDIYIDGDALTID-NVWDKR--- 80
Cdd:PRK14258 8 IKVNNLSFYY---DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFFNqNIYERRvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 ----RLIGMVFQNPDnqFVGATVEDDVAFGLENQGI-PLEEMRSRVDEALELVGMTD---FKTREPA-RLSGGQKQRVAI 151
Cdd:PRK14258 84 nrlrRQVSMVHPKPN--LFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDeikHKIHKSAlDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 152 AGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKN-----GQVESISTPN 225
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSrLSDFTAFFKGnenriGQLVEFGLTK 241
|
...
gi 251820877 226 ELF 228
Cdd:PRK14258 242 KIF 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-224 |
9.66e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.04 E-value: 9.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAltidnvwdkrrliGMVF--QNPdnQFVGATVE 100
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-------------RVLFlpQRP--YLPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 101 DDVAFGLENQGIPLEEMRsrvdEALELVGMTDFKTR--EPAR----LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE 174
Cdd:COG4178 444 EALLYPATAEAFSDAELR----EALEAVGLGHLAERldEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 175 GRLDLIKIVREikERHGMTVISITHDLDEVALSDRVIVMKN---GQVESISTP 224
Cdd:COG4178 520 NEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGdgsWQLLPAEAP 570
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-231 |
1.33e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 101.99 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 20 QYTL-NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQN---PDNqfv 95
Cdd:PRK10253 19 KYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNattPGD--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 96 gATVEDDVAFG-LENQgiPL-----EEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATS 169
Cdd:PRK10253 96 -ITVQELVARGrYPHQ--PLftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 170 MLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMRE 231
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACrYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-217 |
1.33e-25 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 105.44 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:PRK10522 323 LELRNVTFAY--QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQnpdnqfvgatveDDVAFG--LENQGIPLEEmrSRVDEALELVGMTDfKTREP------ARLSGGQKQRVAIAGVVA 156
Cdd:PRK10522 401 AVFT------------DFHLFDqlLGPEGKPANP--ALVEKWLERLKMAH-KLELEdgrisnLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 157 LRPKIIILDEATSMLDPEGR----LDLIKIVREIkerhGMTVISITHDLDEVALSDRVIVMKNGQ 217
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRrefyQVLLPLLQEM----GKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-218 |
1.90e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAESGDIYIDGDALTIDNVwDKR-RL 82
Cdd:COG0396 2 EIKNLHVSV---EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSP-DERaRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 -IGMVFQNPDnQFVGATVEDDVAFGLENQG---IPLEEMRSRVDEALELVGM-TDFKTRE-PARLSGGQKQRVAIAGVVA 156
Cdd:COG0396 78 gIFLAFQYPV-EIPGVSVSNFLRTALNARRgeeLSAREFLKLLKEKMKELGLdEDFLDRYvNEGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 157 LRPKIIILDEATSMLDpegrLDLIKIVRE-IKERH--GMTVISITHD---LDEVAlSDRVIVMKNGQV 218
Cdd:COG0396 157 LEPKLAILDETDSGLD----IDALRIVAEgVNKLRspDRGILIITHYqriLDYIK-PDFVHVLVDGRI 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-218 |
2.06e-25 |
|
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: 100.48 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGdaltidNV-WDKR----RLIGMVFQNPDNQFVGA 97
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVpWKRRkkflRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 98 TVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFkTREPAR-LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGR 176
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEEL-LDTPVRqLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 251820877 177 LDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
2.75e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqedeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL- 82
Cdd:COG1129 256 VLEVEGLSVGG-------VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAg 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVfqnPDNQ-----FVGATVEDDVA---------FGLenqgIPLEEMRSRVDEALELVGMtdfKTREPAR----LSGG 144
Cdd:COG1129 329 IAYV---PEDRkgeglVLDLSIRENITlasldrlsrGGL----LDRRRERALAEEYIKRLRI---KTPSPEQpvgnLSGG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 145 QKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELlGLSDRILVMREGRI 472
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-218 |
3.69e-25 |
|
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: 98.78 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYT---LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE--SGDIYIDGDALTIDNVwdk 79
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQnpdnqfvgatveDDVAFGlenqgipleemRSRVDEAL----ELVGmtdfktreparLSGGQKQRVAIAGVV 155
Cdd:cd03213 81 RKIIGYVPQ------------DDILHP-----------TLTVRETLmfaaKLRG-----------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 156 ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDL--DEVALSDRVIVMKNGQV 218
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-199 |
1.24e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.64 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMniIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKR 80
Cdd:PRK13539 1 MM--LEGEDLACVRG---GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGmvFQNPDNQFVgaTVEDDVAF--GLENQGipleemRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAG-VVAL 157
Cdd:PRK13539 76 HYLG--HRNAMKPAL--TVAENLEFwaAFLGGE------ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARlLVSN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 251820877 158 RPkIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISiTH 199
Cdd:PRK13539 146 RP-IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA-TH 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-201 |
1.24e-24 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 97.43 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYkynQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR01189 1 LAARNLAC---SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNpdnqfvgatveddvafGLENQGIPLEEMR----------SRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGV 154
Cdd:TIGR01189 78 LGHLP----------------GLKPELSALENLHfwaaihggaqRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251820877 155 VALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDL 201
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-247 |
1.40e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.88 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTiDNVWDKRRLI 83
Cdd:PRK13537 7 PIDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-SRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMV--FQNPDNQFvgATVEDDVAFGlENQGIPLEEMRSRVDEALE---LVGMTDFKTREparLSGGQKQRVAIAGVVALR 158
Cdd:PRK13537 83 GVVpqFDNLDPDF--TVRENLLVFG-RYFGLSAAAARALVPPLLEfakLENKADAKVGE---LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 159 PKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMRE---DLV 234
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGAPHALIESEigcDVI 235
|
250
....*....|....*
gi 251820877 235 DLDLDRPFT--TELA 247
Cdd:PRK13537 236 EIYGPDPVAlrDELA 250
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-227 |
1.92e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.40 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAL---TIDNVwdkRR 81
Cdd:PRK11176 342 IEFRNVTFTY-PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLASL---RN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPdnQFVGATVEDDVAFGLENQgipleEMRSRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVA 150
Cdd:PRK11176 418 QVALVSQNV--HLFNDTIANNIAYARTEQ-----YSREQIEEAARMAYAMDFINKMDngldtvigengVLLSGGQRQRIA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREI-KERhgmTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELqKNR---TSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-218 |
2.67e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.54 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYNQEDEQYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRR 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 L----IGMVFQNpdnqFVGATVEDdvafGLENQGIPL-------EEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVA 150
Cdd:PRK10584 85 LrakhVGFVFQS----FMLIPTLN----ALENVELPAllrgessRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-226 |
4.93e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDEQY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG-DALTIDNvwD 78
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqDVATLDA--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 79 -----KRRLIGMVFQNPdNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAG 153
Cdd:PRK10535 79 alaqlRREHFGFIFQRY-HLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNE 226
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
5.75e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.39 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES---GDIYIDGDALTID--- 74
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQ---ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 75 --NVWDKRRLIGMVFQ--NPDNQFvgaTVEDDVAFGLENQgIPL---------EEMRSRVDEALELVGMTDFKTREPARL 141
Cdd:PRK09984 78 arDIRKSRANTGYIFQqfNLVNRL---SVLENVLIGALGS-TPFwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 142 SGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLD-EVALSDRVIVMKNGQV 218
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-218 |
7.25e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.56 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:PRK10790 341 IDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNP----DNQFVGATVEDDVAfglenqgiplEEmrsRVDEALELVGMTDFKTREPA-----------RLSGGQKQRV 149
Cdd:PRK10790 419 MVQQDPvvlaDTFLANVTLGRDIS----------EE---QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 150 AIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhgMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-231 |
1.07e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDK-R 80
Cdd:PRK10895 1 MATLTAKNLAKAYK---GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPdNQFVGATVEDDVAFGLE-NQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:PRK10895 78 RGIGYLPQEA-SIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDE-VALSDRVIVMKNGQVESISTPNELFMRE 231
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVREtLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-218 |
1.91e-23 |
|
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: 95.03 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE---AESGDIYIDGDALTIDNVwdkRRLIGMVFQnpDNQFV-GAT 98
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQF---QKCVAYVRQ--DDILLpGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 99 VEDDVAFG--LENQGIPLEEMRSRVDE--ALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE 174
Cdd:cd03234 98 VRETLTYTaiLRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251820877 175 GRLDLIKIVREIKERHGMTVISI---THDLDEvaLSDRVIVMKNGQV 218
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIhqpRSDLFR--LFDRILLLSSGEI 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-199 |
2.94e-23 |
|
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: 92.99 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYkyNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAltidNVWdkrrlig 84
Cdd:cd03223 1 IELENLSL--ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLL------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnQFVGATVEDDVAFglenqgiPLEEMrsrvdealelvgmtdfktreparLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03223 68 FLPQRP--YLPLGTLREQLIY-------PWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 251820877 165 DEATSMLDPEGRLDLIKIVREikerHGMTVISITH 199
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-228 |
3.21e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.93 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA-----ESGDIYIDGDAL-TIDNVWDKRRLIGMVFQNPdNQFVG 96
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRP-NPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 97 ATVEDDVAFGLENQGIPLEEMRSRVDEALELVGMTD-FKTR---EPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLD 172
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDaVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 173 PEGRLDLIKIVREIKERhgMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELF 228
Cdd:PRK14271 196 PTTTEKIEEFIRSLADR--LTVIIVTHNLAQAArISDRAALFFDGRLVEEGPTEQLF 250
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-227 |
3.97e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.06 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLiGMV--FQNP---------DN 92
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVrtFQHVrlfremtviEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 93 QFVGA--TVEDDVAFGLENQGIPLEEMRSRVDEA---LELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEA 167
Cdd:PRK11300 101 LLVAQhqQLKTGLFSGLLKTPAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 168 TSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-217 |
1.30e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.92 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE--AESGDIYIDGDALTIDNVWDKRRL-IGMVFQN---------P 90
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAgIAIIHQElalvkelsvL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 91 DNQFVGATVeddVAFGLENqgipLEEMRSRVDEALELVGMtDFKTREPAR-LSGGQKQRVAIAGVVALRPKIIILDEATS 169
Cdd:PRK13549 101 ENIFLGNEI---TPGGIMD----YDAMYLRAQKLLAQLKL-DINPATPVGnLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 251820877 170 ML-DPEGRLdLIKIVREIKeRHGMTVISITHDLDEV-ALSDRVIVMKNGQ 217
Cdd:PRK13549 173 SLtESETAV-LLDIIRDLK-AHGIACIYISHKLNEVkAISDTICVIRDGR 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-218 |
1.65e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.73 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR01193 474 IVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGaTVEDDVAFGlENQGIPLEEmrsrVDEALELVGMTD--------FKTR---EPARLSGGQKQRVAIAG 153
Cdd:TIGR01193 552 YLPQEP-YIFSG-SILENLLLG-AKENVSQDE----IWAACEIAEIKDdienmplgYQTElseEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 154 VVALRPKIIILDEATSMLDpegRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLD---TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-217 |
2.36e-22 |
|
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: 91.76 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQ--YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaltidnvwdkrrl 82
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPdnQFVGATVEDDVAFGLenqgiPLEEMR-SRVDEALELVgmTDFKTRePAR-----------LSGGQKQRVA 150
Cdd:cd03250 68 IAYVSQEP--WIQNGTIRENILFGK-----PFDEERyEKVIKACALE--PDLEIL-PDGdlteigekginLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIK--IVREIKErhGMTVISITHDLDEVALSDRVIVMKNGQ 217
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-252 |
2.83e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.68 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDI-YIDGDALTID----N 75
Cdd:PRK11701 3 DQPLLSVRGLTKLY---GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDlyalS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 VWDKRRLI----GMVFQNPDNQF-----VGATV-EDDVAFGLENQGipleEMRSRVDEALELVGMtdfktrEPARL---- 141
Cdd:PRK11701 80 EAERRRLLrtewGFVHQHPRDGLrmqvsAGGNIgERLMAVGARHYG----DIRATAGDWLERVEI------DAARIddlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 142 ---SGGQKQRVAIAGVVALRPKIIILDEATSMLD--PEGR-LDLIK-IVREIkerhGMTVISITHDLdEVA--LSDRVIV 212
Cdd:PRK11701 150 ttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQARlLDLLRgLVREL----GLAVVIVTHDL-AVArlLAHRLLV 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 251820877 213 MKNGQV-ESISTpnelfmreDLVDLDLDRPFTTELASSLRQ 252
Cdd:PRK11701 225 MKQGRVvESGLT--------DQVLDDPQHPYTQLLVSSVLQ 257
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-233 |
2.92e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.02 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALtidNVWDKRRLIGMVFQNPDNQF-VGATVED 101
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVAYVPQSEEVDWsFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAFGLENQ----GIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRL 177
Cdd:PRK15056 100 VVMMGRYGHmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 178 DLIKIVREIKErHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMREDL 233
Cdd:PRK15056 180 RIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENL 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-217 |
3.14e-22 |
|
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: 89.82 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIyidgdaltidnVWDKRRLIG 84
Cdd:cd03221 1 IELENLSKTY---GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQnpdnqfvgatveddvafglenqgipleemrsrvdealelvgmtdfktreparLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:cd03221 67 YFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 165 DEATSMLDPEGRLDLIkivREIKERHGmTVISITHD---LDEVAlsDRVIVMKNGQ 217
Cdd:cd03221 95 DEPTNHLDLESIEALE---EALKEYPG-TVILVSHDryfLDQVA--TKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-213 |
3.23e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 91.40 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 18 DEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNpdnqfvga 97
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 98 tveddvafGLENQGIPLEEMR--------SRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATS 169
Cdd:cd03231 83 --------GIKTTLSVLENLRfwhadhsdEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 251820877 170 MLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVM 213
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
5-230 |
5.26e-22 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 95.34 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR01192 335 VEFRHITFEFANSSQ--GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQnpDNQFVGATVEDDVAFGLEnqGIPLEEmrsrVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAG 153
Cdd:TIGR01192 413 TVFQ--DAGLFNRSIRENIRLGRE--GATDEE----VYEAAKAAAAHDFILKRSngydtlvgergNRLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIVREIkeRHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMR 230
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDAL--RKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-230 |
6.26e-22 |
|
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: 95.47 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHvkQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAL--TIDNVwdkRRLIGMVFQNpDNQFVGATVEDD 102
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetNLDAV---RQSLGMCPQH-NILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKI 182
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 251820877 183 VreIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPneLFMR 230
Cdd:TIGR01257 1104 L--LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP--LFLK 1148
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-220 |
3.93e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAltidnvwdkRrlIGMVFQNPDnQFVGATVEDD 102
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL---------R--IGYLPQEPP-LDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLEnqgiPLEEMRSRVDEALELVGMTD---------------------------------FKTREPAR----LSGGQ 145
Cdd:COG0488 82 VLDGDA----ELRALEAELEELEAKLAEPDedlerlaelqeefealggweaearaeeilsglgFPEEDLDRpvseLSGGW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 146 KQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLikiVREIKERHGmTVISITHD---LDEVAlsDRVIVMKNGQVES 220
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWL---EEFLKNYPG-TVLVVSHDryfLDRVA--TRILELDRGKLTL 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-205 |
6.03e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVR-------LIDGLlEAEsGDIYIDGDAL---TIDNVwDKRRLIGMVFQNPdN 92
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF-RVE-GKVTFHGKNLyapDVDPV-EVRRRIGMVFQKP-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 93 QFvGATVEDDVAFGLENQGIPlEEMRSRVDEALELVGMTDF---KTREPA-RLSGGQKQRVAIAGVVALRPKIIILDEAT 168
Cdd:PRK14243 102 PF-PKSIYDNIAYGARINGYK-GDMDELVERSLRQAALWDEvkdKLKQSGlSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 251820877 169 SMLDPEGRLDLIKIVREIKERHgmTVISITHDLDEVA 205
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAA 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-218 |
1.04e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.14 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE-AESGDIYIDGDALTIDNVWDKRRL-IGMVFQnpDNQFVGATVED 101
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQgIAMVPE--DRKRDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAfglenQGIPLEEM-----RSRVDEALELVGMTDF------KTREP----ARLSGGQKQRVAIAGVVALRPKIIILDE 166
Cdd:PRK13549 357 GVG-----KNITLAALdrftgGSRIDDAAELKTILESiqrlkvKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251820877 167 ATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-231 |
1.05e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.96 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPdNQFVGAtvedd 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP-VLFSGT----- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLEnqgiPLEEMR-SRVDEALELVGMTDFKTREPARL-----------SGGQKQRVAIAGVVALRPKIIILDEATSM 170
Cdd:PLN03232 1326 VRFNID----PFSEHNdADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 171 LDPegRLDLIkIVREIKER-HGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMRE 231
Cdd:PLN03232 1402 VDV--RTDSL-IQRTIREEfKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-218 |
1.54e-20 |
|
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: 86.81 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKynqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAESGDIYIDGDALTIDNVWDKRRL 82
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 -IGMVFQNPdnqfvgatveddvafgLENQGIPLEEMRSRVDEAlelvgmtdfktreparLSGGQKQRVAIAGVVALRPKI 161
Cdd:cd03217 78 gIFLAFQYP----------------PEIPGVKNADFLRYVNEG----------------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITH--DLDEVALSDRVIVMKNGQV 218
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-232 |
1.59e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 91.24 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 15 NQEDEQYTlNDVSFHVKQGEWLSIIGHNGSGKSTTVRlidglleAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPdnQF 94
Cdd:PTZ00265 1238 NEQDYQGD-EEQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--ML 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 95 VGATVEDDVAFGLENQgipleeMRSRVDEALELVGMTDFKTREPAR-----------LSGGQKQRVAIAGVVALRPKIII 163
Cdd:PTZ00265 1308 FNMSIYENIKFGKEDA------TREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILL 1381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQ-----VESISTPNELFMRED 232
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQD 1455
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-228 |
1.92e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.67 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGDIYIDGDALTIDNVWDKRRLIGMVFQNPdnQFVGATVEDDVAF 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNP--QLPHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 106 GleNQGIPLEEmrsrVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDpe 174
Cdd:PRK11174 446 G--NPDASDEQ----LQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD-- 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 175 gRLDLIKIVREIKE-RHGMTVISITHDLDEVALSDRVIVMKNGQV------ESISTPNELF 228
Cdd:PRK11174 518 -AHSEQLVMQALNAaSRRQTTLMVTHQLEDLAQWDQIWVMQDGQIvqqgdyAELSQAGGLF 577
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-229 |
2.74e-20 |
|
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: 90.25 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAESGDI-----------YID---- 67
Cdd:TIGR03269 1 IEVKNLTKKF---DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 68 --------GDALTIDNV--WDK--------RRLIGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMrsrVDEALELVG 129
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVdfWNLsdklrrriRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEA---VGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 130 MTDFKTR--EPAR-LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVIsITHDLDEVA- 205
Cdd:TIGR03269 155 MVQLSHRitHIARdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV-LTSHWPEVIe 233
|
250 260
....*....|....*....|....*...
gi 251820877 206 -LSDRVIVMKNGQVESISTPNEL---FM 229
Cdd:TIGR03269 234 dLSDKAIWLENGEIKEEGTPDEVvavFM 261
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-232 |
3.32e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.18 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:PLN03130 1238 IKFEDVVLRYRPELPP-VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGAtveddVAFGLEnqgiPLEEmRSRVD--EALELVGMTDFKTREPARL-----------SGGQKQRVAI 151
Cdd:PLN03130 1317 IIPQAP-VLFSGT-----VRFNLD----PFNE-HNDADlwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSL 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 152 AGVVALRPKIIILDEATSMLDPegRLD-LI-KIVREikERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFM 229
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDV--RTDaLIqKTIRE--EFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
...
gi 251820877 230 RED 232
Cdd:PLN03130 1462 NEG 1464
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-227 |
3.35e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.18 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVwDKRRLIG-M-----------VFQNPD 91
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDI-ATRRRVGyMsqafslygeltVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 92 nqfvgatveddvafgLENQ--GIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAgvVAL--RPKIIILDEA 167
Cdd:NF033858 362 ---------------LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA--VAVihKPELLILDEP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 168 TSMLDPEGRlD-----LIKIVREikerHGMTV-ISiTHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:NF033858 425 TSGVDPVAR-DmfwrlLIELSRE----DGVTIfIS-THFMNEAERCDRISLMHAGRVLASDTPAAL 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-220 |
4.64e-20 |
|
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: 89.50 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGDIYIDGDALTIDNVWDK-RR 81
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAiRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVfqnPDNQFVGATVEDdVAFGlenQGIPLEEM-----RSRVDEALEL------VGMTDFKTREP----ARLSGGQK 146
Cdd:TIGR02633 337 GIAMV---PEDRKRHGIVPI-LGVG---KNITLSVLksfcfKMRIDAAAELqiigsaIQRLKVKTASPflpiGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 147 QRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQVES 220
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVlGLSDRVLVIGEGKLKG 483
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-227 |
6.04e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTiDNVWDKRRLIGMV--FQNPDNQFvgaTV- 99
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-ARARLARARIGVVpqFDNLDLEF---TVr 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGlENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDL 179
Cdd:PRK13536 133 ENLLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 251820877 180 IKIVREIKERhGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNEL 227
Cdd:PRK13536 212 WERLRSLLAR-GKTILLTTHFMEEAErLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-230 |
6.32e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.29 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEA----ESGDIYIDGDALTIDNVwdKRRLIGMVFQNPDNQFvgatve 100
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAL--RGRKIATIMQNPRSAF------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 101 ddvafgleNqgiPLEEMRSRVDE----------------ALELVGMTDFKT---REPARLSGGQKQRVAIAGVVALRPKI 161
Cdd:PRK10418 93 --------N---PLHTMHTHAREtclalgkpaddatltaALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQVESISTPNELFMR 230
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVArLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-234 |
1.01e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-IGMVFQN----PDnqfvgA 97
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgVAIIYQElhlvPE-----M 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 98 TVEDDVAFG-LENQG--IPLEEMRSRVDEALELVGMtDFKTREP-ARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDP 173
Cdd:PRK11288 95 TVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGV-DIDPDTPlKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 174 EGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQ-VESISTPNELfMREDLV 234
Cdd:PRK11288 174 REIEQLFRVIRELRAE-GRVILYVSHRMEEIfALCDAITVFKDGRyVATFDDMAQV-DRDQLV 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-227 |
1.10e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.93 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDgDALTIDNVWDK--RRL 82
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-DSHNLKDINLKwwRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNP-------------------DNQFVGATVEDDVAFGLENQGIP----------------------LEEMR--- 118
Cdd:PTZ00265 462 IGVVSQDPllfsnsiknnikyslyslkDLEALSNYYNEDGNDSQENKNKRnscrakcagdlndmsnttdsneLIEMRkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 119 -----SRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKI 182
Cdd:PTZ00265 542 qtikdSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 251820877 183 VREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDII 666
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-227 |
1.69e-19 |
|
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: 88.08 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:TIGR00957 1285 VEFRNYCLRY-REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGATVEDDVAFGLENQgiplEEmrsrVDEALELVGMTDFKTREPAR-----------LSGGQKQRVAIAG 153
Cdd:TIGR00957 1364 IIPQDP-VLFSGSLRMNLDPFSQYSD----EE----VWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRlDLIK-IVREIKErhGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETD-NLIQsTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-220 |
2.26e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.47 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 38 IIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAL--TIDNVW---DKRRlIGMVFQnpDNQ-FVGATVEDDVAFGLENQg 111
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGIClppEKRR-IGYVFQ--DARlFPHYKVRGNLRYGMAKS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 112 ipleeMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLD-PEGR--LD-LIKIVREIK 187
Cdd:PRK11144 105 -----MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRelLPyLERLAREIN 179
|
170 180 190
....*....|....*....|....*....|....
gi 251820877 188 erhgMTVISITHDLDEV-ALSDRVIVMKNGQVES 220
Cdd:PRK11144 180 ----IPILYVSHSLDEIlRLADRVVVLEQGKVKA 209
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-227 |
2.67e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 15 NQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGDIYIDGDALtidNVWDKRRLIGMVFQnpD 91
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQ--D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 92 NQFVGA-TVEDDVAFGLE---NQGIPLEEMRSRVDEALELVGMTDF-KTR--EPAR---LSGGQKQRVAIAGVVALRPKI 161
Cdd:TIGR00955 108 DLFIPTlTVREHLMFQAHlrmPRRVTKKEKRERVDEVLQALGLRKCaNTRigVPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITH----DLDEvaLSDRVIVMKNGQVESISTPNEL 227
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHqpssELFE--LFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-216 |
3.76e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALT-IDNVWDKRRLIGMVFQN---------PDN 92
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkLDHKLAAQLGIGIIYQElsvideltvLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 93 QFVGATVEDDVAfglenqGIPL---EEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATS 169
Cdd:PRK09700 101 LYIGRHLTKKVC------GVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 251820877 170 MLDPEGRLDLIKIVREIKeRHGMTVISITHDLDEV-ALSDRVIVMKNG 216
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIrRICDRYTVMKDG 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-217 |
4.24e-19 |
|
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: 86.42 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE--AESGDIYIDGDALTIDNVWDKRRLiGMVFQNPDNQFV-GATV 99
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERA-GIVIIHQELTLVpELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLE---NQGI-PLEEMRSRVDEALELVGMTDFK-TREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE 174
Cdd:TIGR02633 96 AENIFLGNEitlPGGRmAYNAMYLRAKNLLRELQLDADNvTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 251820877 175 GRLDLIKIVREIKeRHGMTVISITHDLDEV-ALSDRVIVMKNGQ 217
Cdd:TIGR02633 176 ETEILLDIIRDLK-AHGVACVYISHKLNEVkAVCDTICVIRDGQ 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-218 |
1.16e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnVWDK---RR 81
Cdd:PRK11160 339 LTLNNVSFTY-PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA---DYSEaalRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQNPDnqFVGATVEDDVAFGLENqgIPLEEMRsrvdEALELVGMTDFKTREPA----------RLSGGQKQRVAI 151
Cdd:PRK11160 415 AISVVSQRVH--LFSATLRDNLLLAAPN--ASDEALI----EVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 152 AGVVaLRPK-IIILDEATSMLDPEGRLDLIKIVREIKErhGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:PRK11160 487 ARAL-LHDApLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-212 |
1.27e-18 |
|
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: 82.46 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 21 YTLNDVSFHVKQG-----EWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIdnvwdKRRLIGMVFQNPDNQFV 95
Cdd:cd03237 8 KTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-----KPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 96 GATVEDdvaFGLENQgipleeMRSRVDEALELVGMTDfktREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEG 175
Cdd:cd03237 83 SSITKD---FYTHPY------FKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 251820877 176 RLDLIKIVREIKERHGMTVISITHD-LDEVALSDRVIV 212
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAFVVEHDiIMIDYLADRLIV 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-214 |
2.66e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 17 EDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLidgLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPDnqfvg 96
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRL---LAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 97 atveddvafglenqgipleemrsrVDEALEL---VGMTD--FKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSML 171
Cdd:COG2401 112 ------------------------FKDAVELlnaVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 251820877 172 DPEGRLDLIKIVREIKERHGMTVISITHDLD-EVALSDRVIVMK 214
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATHHYDvIDDLQPDLLIFV 211
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-218 |
2.80e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGDIYIDGDALtidNVWDKRRLI---GMVFQNPDNQFVgATV 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPL---SDWSAAELArhrAYLSQQQSPPFA-MPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLEnQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVV-----ALRP--KIIILDEATSMLD 172
Cdd:COG4138 87 FQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251820877 173 PEGRLDLIKIVREIKERhGMTVISITHDLDEVAL-SDRVIVMKNGQV 218
Cdd:COG4138 166 VAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRhADRVWLLKQGKL 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-232 |
3.70e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAeSGDIYIDGDALTidnVWDKRRLIGM----------VFQNPDNQFV 95
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLE---AWSAAELARHraylsqqqtpPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 96 GATVEDdvafglenqGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVV-----ALRP--KIIILDEAT 168
Cdd:PRK03695 91 TLHQPD---------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 169 SMLD--PEGRLDliKIVREIKeRHGMTVISITHDLDEVAL-SDRVIVMKNGQVESISTPNELfMRED 232
Cdd:PRK03695 162 NSLDvaQQAALD--RLLSELC-QQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGRRDEV-LTPE 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-232 |
4.34e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPdNQFVGaTVEDD 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP-VLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 V-AFglenqgipLEEMRSRVDEALELVGMTDFKTREP----ARL-------SGGQKQRVAIAGvvALRPK---IIILDEA 167
Cdd:PTZ00243 1404 VdPF--------LEASSAEVWAALELVGLRERVASESegidSRVleggsnySVGQRQLMCMAR--ALLKKgsgFILMDEA 1473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 168 TSMLDPEgrLDlikivREIKER-----HGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMRED 232
Cdd:PTZ00243 1474 TANIDPA--LD-----RQIQATvmsafSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-218 |
6.94e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRlIGMVFQNPDNQfvgatvEDD 102
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLA-NGIVYISEDRK------RDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGL---ENQGIP-LEEMRS---RVDEALELVGMTDFKT----REPAR------LSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:PRK10762 341 LVLGMsvkENMSLTaLRYFSRaggSLKHADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVlGMSDRILVMHEGRI 473
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
1.85e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDI----------------YID 67
Cdd:COG0488 315 VLELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigyfdqhqeELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 68 GDALTIDNVWDkrrligmVFQNPDNQFVGATVEDdvaFGLenqgipleemrsRVDEALELVGmtdfktrepaRLSGGQKQ 147
Cdd:COG0488 392 PDKTVLDELRD-------GAPGGTEQEVRGYLGR---FLF------------SGDDAFKPVG----------VLSGGEKA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKerhGmTVISITHD---LDEVAlsDRVIVMKNGQVE 219
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDryfLDRVA--TRILEFEDGGVR 508
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-218 |
2.36e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.68 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDeqyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:PRK10789 316 VNIRQFTYPQTDHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdnqFVGA-TVEDDVAFGLENQgipleeMRSRVDEALELVGMTDFKTREP-----------ARLSGGQKQRVAIA 152
Cdd:PRK10789 393 VVSQTP---FLFSdTVANNIALGRPDA------TQQEIEHVARLASVHDDILRLPqgydtevgergVMLSGGQKQRISIA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 153 GVVALRPKIIILDEATSMLDpeGRLDLiKIVREIKE-RHGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:PRK10789 464 RALLLNAEILILDDALSAVD--GRTEH-QILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-258 |
4.15e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.56 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYN-QEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeaeSGDIYIDGDALTIDNV---- 76
Cdd:COG4170 1 MPLLDIRNLTIEIDtPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGIT---KDNWHVTADRFRWNGIdllk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 ---WDKRRLIG----MVFQNPD-----NQFVGATVEddvafglenQGIPLEEMRS--------RVDEALEL---VGMTDF 133
Cdd:COG4170 78 lspRERRKIIGreiaMIFQEPSscldpSAKIGDQLI---------EAIPSWTFKGkwwqrfkwRKKRAIELlhrVGIKDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 134 K---TREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDR 209
Cdd:COG4170 149 KdimNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISqWADT 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 251820877 210 VIVMKNGQ-VESISTpnelfmrEDLVDLDLdRPFTTELASSLRQTGLDLP 258
Cdd:COG4170 229 ITVLYCGQtVESGPT-------EQILKSPH-HPYTKALLRSMPDFRQPLP 270
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-218 |
4.24e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLiGMVFQNPDNQFVGATVE---- 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-GLVYLPEDRQSSGLYLDapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 101 -DDVAFGLENQGIPLEEMRSR--VDEALELVGMTDFKTREPAR-LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGR 176
Cdd:PRK15439 360 wNVCALTHNRRGFWIKPARENavLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 251820877 177 LDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:PRK15439 440 NDIYQLIRSIAAQ-NVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-227 |
7.99e-17 |
|
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: 80.44 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALtIDNVWDKRRLIGMVfqnpdNQFVGAtveDDVAFGLEN 109
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYC-----PQFDAI---DDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 -------QGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKI 182
Cdd:TIGR01257 2033 lylyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 251820877 183 VREIKeRHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:TIGR01257 2113 IVSII-REGRAVVLTSHSMEECeALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-218 |
8.60e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKynQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLi 83
Cdd:COG3845 257 VLEVENLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 84 GMVFQNPDNQFVGA----TVEDDVAFGLENQG-------IPLEEMRSRvdeALELVGMTDFKTREP----ARLSGGQKQR 148
Cdd:COG3845 334 GVAYIPEDRLGRGLvpdmSVAENLILGRYRRPpfsrggfLDRKAIRAF---AEELIEEFDVRTPGPdtpaRSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 149 VAIAGVVALRPKIIILDEATsmldpegR-LDL--IKIVRE--IKER-HGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:COG3845 411 VILARELSRDPKLLIAAQPT-------RgLDVgaIEFIHQrlLELRdAGAAVLLISEDLDEIlALSDRIAVMYEGRI 480
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-218 |
1.00e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.23 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidnVWDKRRL----IGMVfqnPDNQ--FVG 96
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKImreaVAIV---PEGRrvFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 97 ATVEDDVAFGleNQGIPLEEMRSRVDEALELVG-MTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEG 175
Cdd:PRK11614 95 MTVEENLAMG--GFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 251820877 176 RLDLIKIVREIKERhGMTVISITHDLDE-VALSDRVIVMKNGQV 218
Cdd:PRK11614 173 IQQIFDTIEQLREQ-GMTIFLVEQNANQaLKLADRGYVLENGHV 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-258 |
1.94e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.92 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 2 MNIIEVKNLKYKYNQEDEQYTLND-VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEaesGDIYIDGDALTIDNV---- 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDrVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK---DNWRVTADRMRFDDIdllr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 77 ---WDKRRLIG----MVFQNPDN-----QFVGATVEDDVAfGLENQGIPLEEMRSRVDEALEL---VGMTDFK---TREP 138
Cdd:PRK15093 78 lspRERRKLVGhnvsMIFQEPQScldpsERVGRQLMQNIP-GWTYKGRWWQRFGWRKRRAIELlhrVGIKDHKdamRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 139 ARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVA-LSDRVIVMKNGQ 217
Cdd:PRK15093 157 YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSqWADKINVLYCGQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 251820877 218 VESISTPNELFMREdlvdldlDRPFTTELASSLRQTGLDLP 258
Cdd:PRK15093 237 TVETAPSKELVTTP-------HHPYTQALIRAIPDFGSAMP 270
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-234 |
1.95e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIEVKNLKYKYNQedeQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDgdaltidnvwDKR 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQ---RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----------GKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RlIGMVfqnPDNQFVGATVEDDVA-FGLENQGIpleeMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRP 159
Cdd:PRK09544 68 R-IGYV---PQKLYLDTTLPLTVNrFLRLRPGT----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 160 KIIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMkNGQVESISTPNELFMREDLV 234
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL-NHHICCSGTPEVVSLHPEFI 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-218 |
2.96e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRlIGMVFQNPDNQFVG----ATV 99
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIR-AGIMLCPEDRKAEGiipvHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFGLENQGIPLEEMRSRVDE---ALELVGMTDFKTREPAR----LSGGQKQRVAIAGVVALRPKIIILDEATSMLD 172
Cdd:PRK11288 349 ADNINISARRHHLRAGCLINNRWEaenADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251820877 173 PEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVlGVADRIVVMREGRI 474
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-201 |
3.36e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALtidnvwdkRRLIGMVFQNPdnQFVG--ATVEDD 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQRDEYHQDL--LYLGhqPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAfGLEN----QGIPLEEMRSRVDEALELVGMTDFktrE--PAR-LSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEG 175
Cdd:PRK13538 89 LT-ALENlrfyQRLHGPGDDEALWEALAQVGLAGF---EdvPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|....*.
gi 251820877 176 RLDLIKIVREIKERHGMTVISITHDL 201
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTHQDL 190
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
6-227 |
6.00e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.24 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIdnvwdkrrligM 85
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI-----------A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQNPDNQFVGatVEDDVAFGLEnQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:PRK13545 92 ISSGLNGQLTG--IENIELKGLM-MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNEL 227
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVkSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-201 |
7.55e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.22 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 1 MMNIIevkNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKR 80
Cdd:PRK13540 1 MLDVI---ELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNPDNQFVgaTVEDDVAFGLENQGIPLEemrsrVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPK 160
Cdd:PRK13540 75 QLCFVGHRSGINPYL--TLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 251820877 161 IIILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDL 201
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-216 |
6.20e-15 |
|
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: 71.51 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYN-QEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLEaesGDIYIDGDALTIdnvw 77
Cdd:cd03232 3 VLTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGRPLDK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DKRRLIGMVFQNpdnqfvgatvedDVAFGLenqgipleemrSRVDEALELVGmtdfKTREparLSGGQKQRVAIAGVVAL 157
Cdd:cd03232 76 NFQRSTGYVEQQ------------DVHSPN-----------LTVREALRFSA----LLRG---LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 158 RPKIIILDEATSMLDPEGRLDLIKIVREIKErHGMTVISITHDLDEVALS--DRVIVMKNG 216
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-212 |
6.46e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDgdaLTIDnvwdkrrligmvfQNPdnQFVGATVEDDVAFGLEN 109
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKIS-------------YKP--QYIKPDYDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 QGIPLEE--MRSRVDEALELVGMTDFKTREparLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIK 187
Cdd:PRK13409 424 ITDDLGSsyYKSEIIKPLQLERLLDKNVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
170 180
....*....|....*....|....*...
gi 251820877 188 ERHGMTVISITHDL---DevALSDRVIV 212
Cdd:PRK13409 501 EEREATALVVDHDIymiD--YISDRLMV 526
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-237 |
6.61e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.06 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES--GDIYIDGDALTIDNVWDKRRL-IGMVFQN----P----- 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALgIVIIHQElaliPylsia 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 91 DNQFVGatvEDDVAFGLenqgIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSM 170
Cdd:NF040905 97 ENIFLG---NERAKRGV----IDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251820877 171 L---DPEGRLDLIkivREIKErHGMTVISITHDLDEVA-LSDRVIVMKNGQveSISTpneLFMREDLVDLD 237
Cdd:NF040905 170 LneeDSAALLDLL---LELKA-QGITSIIISHKLNEIRrVADSITVLRDGR--TIET---LDCRADEVTED 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-175 |
6.88e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.80 E-value: 6.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 18 DEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDnvwDKRRLIGMVFQNPDNQFVGA 97
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 98 TVEdDVAFGLENQGIPLEEMRSrvdEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEG 175
Cdd:PRK13543 99 TLE-NLHFLCGLHGRRAKQMPG---SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-234 |
8.84e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEdeqytLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDK-RRL 82
Cdd:PRK09700 265 VFEVRNVTSRDRKK-----VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNP-DNQFVGAtveddvaFGL-ENQGIPLEEMRSRVDEALELVG-MTDFKTREPAR----------------LSG 143
Cdd:PRK09700 340 MAYITESRrDNGFFPN-------FSIaQNMAISRSLKDGGYKGAMGLFHeVDEQRTAENQRellalkchsvnqniteLSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 144 GQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQVESIS 222
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIiTVCDRIAVFCEGRLTQIL 491
|
250
....*....|..
gi 251820877 223 TPNELFMREDLV 234
Cdd:PRK09700 492 TNRDDMSEEEIM 503
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-218 |
1.34e-14 |
|
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: 70.75 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 17 EDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGDIYIDGdaLTIDNVWDK-RRLIGMVFQNpDN 92
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEKyPGEIIYVSEE-DV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 93 QFVGATVEDDVAFGLENQGiplEEMrSRVdealelvgmtdfktreparLSGGQKQRVAIAGVVALRPKIIILDEATSMLD 172
Cdd:cd03233 94 HFPTLTVRETLDFALRCKG---NEF-VRG-------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 251820877 173 PEGRLDLIKIVREI-KERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:cd03233 151 SSTALEILKCIRTMaDVLKTTTFVSLYQASDEIyDLFDKVLVLYEGRQ 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-234 |
1.35e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE--------SGDIYIDGDALTIDNVWDKRRLIGMVFQNPDNQF 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 95 vGATVEDDVAFG----LENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVA---------LRPKI 161
Cdd:PRK13547 97 -AFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 162 IILDEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEVAL-SDRVIVMKNGQVESISTPNELfMREDLV 234
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADV-LTPAHI 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-212 |
5.80e-14 |
|
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: 71.35 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDgdaLTIDnvwdkrrligmvfQNPdnQFVGATVEDDVAFGLEN 109
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKIS-------------YKP--QYISPDYDGTVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 ---QGIPLEEMRSRVDEALELVGMTDFKTREparLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREI 186
Cdd:COG1245 425 antDDFGSSYYKTEIIKPLGLEKLLDKNVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*....
gi 251820877 187 KERHGMTVISITHDL---DevALSDRVIV 212
Cdd:COG1245 502 AENRGKTAMVVDHDIyliD--YISDRLMV 528
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-218 |
5.96e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.67 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDG--LLEAESGDIYIDG-DALTIDNVWDK 79
Cdd:CHL00131 6 PILEIKNLHASVN---ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGeSILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 RRLIGMVFQNPdNQFVGATVED--DVAFGLENQGIPLEEMR-----SRVDEALELVGMTD-FKTREPAR-LSGGQKQRVA 150
Cdd:CHL00131 83 HLGIFLAFQYP-IEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 151 IAGVVALRPKIIILDEATSMLDpegrLDLIKIVRE---IKERHGMTVISITH--DLDEVALSDRVIVMKNGQV 218
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLD----IDALKIIAEginKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKI 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-217 |
1.23e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNvwDKRRL---IGMVFQNPdNQFVGATV 99
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKS--SKEALengISMVHQEL-NLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVAFG-------LENQGIPLEEMRSRVDEaLELvgmtDFKTREP-ARLSGGQKQRVAIAGVVALRPKIIILDEATSML 171
Cdd:PRK10982 91 MDNMWLGryptkgmFVDQDKMYRDTKAIFDE-LDI----DIDPRAKvATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251820877 172 DPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQ 217
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-216 |
1.46e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.52 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKY--KYNQEDEQyTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAESGDIYIDGDALTIDNVWDK- 79
Cdd:TIGR00956 758 DIFHWRNLTYevKIKKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVNGRPLDSs 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 80 -RRLIGMVFQNpDNQFVGATVEDDV---AFGLENQGIPLEEMRSRVDEALELVGMTDFKTR---EPAR-LSGGQKQRVAI 151
Cdd:TIGR00956 834 fQRSIGYVQQQ-DLHLPTSTVRESLrfsAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvgVPGEgLNVEQRKRLTI 912
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 152 AGVVALRPKIII-LDEATSMLDPEGRLDLIKIVREIKErHGMTVISITHDLDEVALS--DRVIVMKNG 216
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-231 |
2.45e-13 |
|
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: 69.97 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYNQeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGD-ALTIDNVWdkrr 81
Cdd:TIGR00957 635 NSITVHNATFTWAR-DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvAYVPQQAW---- 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 ligmvFQNpdnqfvgATVEDDVAFGLenqgiPLEEMRSR-VDEA------LELVGMTDfKTR---EPARLSGGQKQRVAI 151
Cdd:TIGR00957 710 -----IQN-------DSLRENILFGK-----ALNEKYYQqVLEAcallpdLEILPSGD-RTEigeKGVNLSGGQKQRVSL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 152 AGVVALRPKIIILDEATSMLDPE-GRLDLIKIVREIKERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMR 230
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
.
gi 251820877 231 E 231
Cdd:TIGR00957 852 D 852
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-217 |
3.49e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-IGMVFQN---------PDN 92
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQElnlipqltiAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 93 QFVGAtvEDDVAFGlenqGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLD 172
Cdd:PRK10762 100 IFLGR--EFVNRFG----RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 251820877 173 PEGRLDLIKIVREIKErHGMTVISITHDLDEV-ALSDRVIVMKNGQ 217
Cdd:PRK10762 174 DTETESLFRVIRELKS-QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-235 |
4.90e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRL-IGMVFQNPdNQFVGATVED 101
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEP-LLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAFGLENQgiplEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIK 181
Cdd:PRK15439 106 NILFGLPKR----QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFS 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 182 IVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQVeSISTPNELFMREDLVD 235
Cdd:PRK15439 182 RIRELLAQ-GVGIVFISHKLPEIrQLADRISVMRDGTI-ALSGKTADLSTDDIIQ 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-216 |
1.21e-12 |
|
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: 65.43 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIY----IDGDALTIDNVWDKRRLIGMVFQNPdnQFVGA 97
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKP--WLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 98 TVEDDVAFGlenqgIPLEEMRSR-VDEALELVGMTDF-----KTREPAR---LSGGQKQRVAIAGVVALRPKIIILDEAT 168
Cdd:cd03290 94 TVEENITFG-----SPFNKQRYKaVTDACSLQPDIDLlpfgdQTEIGERginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 169 SMLD--------PEGrldLIKIVREIKErhgmTVISITHDLDEVALSDRVIVMKNG 216
Cdd:cd03290 169 SALDihlsdhlmQEG---ILKFLQDDKR----TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-201 |
1.81e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.47 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIyidGDALTIDNVWDKRRliGMVFQNpdnqFVGATVEDDVAFGLEN 109
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---DDPPDWDEILDEFR--GSELQN----YFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 QG---IP------LEEMRSRVDE---------ALELVGMTDfktREPARLSGGQKQRVAIAGVVALRPKIIILDEATSML 171
Cdd:cd03236 94 QYvdlIPkavkgkVGELLKKKDErgkldelvdQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 251820877 172 DPEGRLDLIKIVREIKErHGMTVISITHDL 201
Cdd:cd03236 171 DIKQRLNAARLIRELAE-DDNYVLVVEHDL 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-213 |
3.52e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDiyiDGDALTIDNVWDKRRliGMVFQNpdnqFVGATVEDDVAFGLEN 109
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEEPSWDEVLKRFR--GTELQN----YFKKLYNGEIKVVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 QGIPL---------EEMRSRVDEA------LELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE 174
Cdd:PRK13409 167 QYVDLipkvfkgkvRELLKKVDERgkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 251820877 175 GRLDLIKIVREIKErhGMTVISITHD---LDevALSDRVIVM 213
Cdd:PRK13409 247 QRLNVARLIRELAE--GKYVLVVEHDlavLD--YLADNVHIA 284
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-199 |
3.74e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.31 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaltidnvwdkrrliGMVFQNPDNQFVG-ATVED 101
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK--------------GKLFYVPQRPYMTlGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAFglenqgiP--LEEMRSR------VDEALELVGMTDFKTREPA---------RLSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:TIGR00954 534 QIIY-------PdsSEDMKRRglsdkdLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*..
gi 251820877 165 DEATSML--DPEGRLdlikivREIKERHGMTVISITH 199
Cdd:TIGR00954 607 DECTSAVsvDVEGYM------YRLCREFGITLFSVSH 637
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-221 |
4.73e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKynqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDAL-------TIDN- 75
Cdd:PRK10982 250 ILEVRNLTSL-----RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhnaneAINHg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 76 ---VWDKRRLIGmVFQNPD---NQFVGATVEDDVAFGLenqgipLEEMRSRVDEALELVGMtdfKTREPAR------LSG 143
Cdd:PRK10982 325 falVTEERRSTG-IYAYLDigfNSLISNIRNYKNKVGL------LDNSRMKSDTQWVIDSM---RVKTPGHrtqigsLSG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 144 GQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDE-VALSDRVIVMKNGQVESI 221
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPElLGITDRILVMSNGLVAGI 472
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-221 |
7.77e-12 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 63.01 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 38 IIGHNGSGKSTtvrLIDGLLEAESGDIYIDGDALTIDN----VWDKRRLIGMVFQNPDNQFVGAT----VEDDVAFglen 109
Cdd:cd03240 27 IVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPklirEGEVRAQVKLAFENANGKKYTITrslaILENVIF---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 qgIPLEEMRSRVdealelvgmtdfkTREPARLSGGQKQ------RVAIAGVVALRPKIIILDEATSMLDPEGR-LDLIKI 182
Cdd:cd03240 100 --CHQGESNWPL-------------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 251820877 183 VREIKERHGMTVISITHDLDEVALSDRVI-VMKNGQVESI 221
Cdd:cd03240 165 IEERKSQKNFQLIVITHDEELVDAADHIYrVEKDGRQKSR 204
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-227 |
1.03e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI-------DGLLEAESGDIyidGDAltidnvwDKRRLIG-----M----- 85
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkiqQGRVEVLGGDM---ADA-------RHRRAVCpriayMpqglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 --------VFQNPDnqFVGATveddvaFGLENQgipleEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGvvAL 157
Cdd:NF033858 87 knlyptlsVFENLD--FFGRL------FGQDAA-----ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC--AL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 158 --RPKIIILDEATSMLDPEGR---LDLIKIVREikERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:NF033858 152 ihDPDLLILDEPTTGVDPLSRrqfWELIDRIRA--ERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAEL 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-213 |
1.61e-11 |
|
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: 64.04 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 31 KQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaltidnvWDK--RRLIGMVFQNpdnqFVGATVEDDVAFGLE 108
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPS-------WDEvlKRFRGTELQD----YFKKLANGEIKVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 109 NQ---GIP----------LEEM--RSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDP 173
Cdd:COG1245 166 PQyvdLIPkvfkgtvrelLEKVdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 251820877 174 EGRLDLIKIVREIKERhGMTVISITHD---LDevALSDRVIVM 213
Cdd:COG1245 246 YQRLNVARLIRELAEE-GKYVLVVEHDlaiLD--YLADYVHIL 285
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-256 |
1.66e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.60 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 115 EEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKeRHGMTV 194
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATV 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 195 ISITHDLDEV-ALSDRVIVMKNGQVESISTPNELFMREDLVDLDLDRPFTTEL---ASSLRQTGLD 256
Cdd:NF000106 198 LLTTQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELdrmVGAIAQAGLD 263
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-233 |
3.22e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDiyidgdaltidnVWDKRRlIGMVFQNPdnQFVGATVEDD 102
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR------------VWAERS-IAYVPQQA--WIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLENQGIPLEEMrSRV-----DEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPE-GR 176
Cdd:PTZ00243 741 ILFFDEEDAARLADA-VRVsqleaDLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGE 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 177 ldliKIVRE--IKERHGMTVISITHDLDEVALSDRVIVMKNGQVEsISTPNELFMREDL 233
Cdd:PTZ00243 820 ----RVVEEcfLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE-FSGSSADFMRTSL 873
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-204 |
4.27e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 7 VKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTID-NVWDKRRLIGM 85
Cdd:PRK13546 24 MKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAiSAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 vfqnpdnqfvgatveDDVAFGLENQGIPLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILD 165
Cdd:PRK13546 104 ---------------ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 251820877 166 EATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV 204
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQV 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-228 |
5.55e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDG-LLEAESGDIYIDGDALTIDNV-Wdkrrl 82
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGSVAYVPQVsW----- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 igmVFQnpdnqfvgATVEDDVAFGLENQGipleemrSRVDEALELVGMTDFKTREPAR-----------LSGGQKQRVAI 151
Cdd:PLN03232 690 ---IFN--------ATVRENILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSM 751
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251820877 152 AGVVALRPKIIILDEATSMLDPE-GRLDLIKIVREikERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNELF 228
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKD--ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-193 |
7.42e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYNqedEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDG-LLEAESGDIYI----DGDALTIdnvW 77
Cdd:PRK10938 259 PRIVLNNGVVSYN---DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLfgrrRGSGETI---W 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 78 DKRRLIGMVfqnpDNQF-----VGATVEDDVAFGLEN-----QGIPlEEMRSRVDEALELVGMTDFKTREPAR-LSGGQK 146
Cdd:PRK10938 333 DIKKHIGYV----SSSLhldyrVSTSVRNVILSGFFDsigiyQAVS-DRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQ 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251820877 147 QRVAIAGVVALRPKIIILDEATSMLDPEGRLdLIKIVREIKERHGMT 193
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQ-LVRRFVDVLISEGET 453
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-232 |
1.40e-10 |
|
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: 60.31 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYnQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:cd03288 20 IKIHDLCVRY-ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGAtveddVAFGLENQGIPLEemrSRVDEALELVGMTDFKTREPARL-----------SGGQKQRVAIAG 153
Cdd:cd03288 99 IILQDP-ILFSGS-----IRFNLDPECKCTD---DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 154 VVALRPKIIILDEATSMLDPEGRLDLIKIV-REIKERhgmTVISITHDLDEVALSDRVIVMKNGQVESISTPNELFMRED 232
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVmTAFADR---TVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQED 246
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-218 |
1.86e-10 |
|
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: 59.87 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGDIYIDGDALTIDNVWDKRRLIG 84
Cdd:cd03289 3 MTVKDLTAKYT-EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 85 MVFQNPdNQFVGATVEDDVAFGLENQgiplEEMRSRVDE-ALELV-----GMTDFKTREPA-RLSGGQKQRVAIAGVVAL 157
Cdd:cd03289 81 VIPQKV-FIFSGTFRKNLDPYGKWSD----EEIWKVAEEvGLKSVieqfpGQLDFVLVDGGcVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 158 RPKIIILDEATSMLDPEgrldLIKIVREIKER--HGMTVISITHDLDEVALSDRVIVMKNGQV 218
Cdd:cd03289 156 KAKILLLDEPSAHLDPI----TYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-227 |
1.88e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-GDIYIDGDALTIDNV-Wdkrrl 82
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVsW----- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 igmVFQnpdnqfvgATVEDDVAFGLenqgiPLEEMR-------SRVDEALELV---GMTDFKTREpARLSGGQKQRVAIA 152
Cdd:PLN03130 690 ---IFN--------ATVRDNILFGS-----PFDPERyeraidvTALQHDLDLLpggDLTEIGERG-VNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 153 GVVALRPKIIILDEATSMLDPE-GRLDLIKIVREikERHGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKD--ELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-212 |
2.13e-10 |
|
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: 58.35 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNvwdkrrligmvfqnpdnQFVgatveddvafglen 109
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-----------------QYI-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 qgipleemrsrvdealelvgmtdfktrepaRLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKER 189
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....
gi 251820877 190 HGMTVISITHDLDEVA-LSDRVIV 212
Cdd:cd03222 121 GKKTALVVEHDLAVLDyLSDRIHV 144
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-205 |
2.46e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIdGDalTIDnvwdkrrl 82
Cdd:TIGR03719 321 KVIEAENLTKAF---GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE--TVK-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVdealeLVGMTDFKTREPAR----LSGGQKQRVAIAGVVALR 158
Cdd:TIGR03719 387 LAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKGSDQQKkvgqLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 251820877 159 PKIIILDEATSMLDPEgrlDLIKIVREIKERHGMTVIsITHD---LDEVA 205
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE---TLRALEEALLNFAGCAVV-ISHDrwfLDRIA 507
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-173 |
3.08e-10 |
|
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: 60.69 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 5 IEVKNLKYKYNqEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGDIYIDG---DALTIDNvWdkRR 81
Cdd:TIGR01271 1218 MDVQGLTAKYT-EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQT-W--RK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LIGMVFQ-------------NPDNQFVGA---TVEDDVafGLENQgipLEEMRSRVDEALELVGMTdfktreparLSGGQ 145
Cdd:TIGR01271 1293 AFGVIPQkvfifsgtfrknlDPYEQWSDEeiwKVAEEV--GLKSV---IEQFPDKLDFVLVDGGYV---------LSNGH 1358
|
170 180
....*....|....*....|....*...
gi 251820877 146 KQRVAIAGVVALRPKIIILDEATSMLDP 173
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-200 |
3.76e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 6 EVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIdGDALTIdNVWDKRRLIgm 85
Cdd:PRK11147 321 EMENVNYQI---DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEV-AYFDQHRAE-- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 vfQNPDNqfvgaTVEDDVAFGleNQGIPLEEMRSRVdealeLVGMTDF-----KTREPAR-LSGGQKQRVAIAGVVaLRP 159
Cdd:PRK11147 394 --LDPEK-----TVMDNLAEG--KQEVMVNGRPRHV-----LGYLQDFlfhpkRAMTPVKaLSGGERNRLLLARLF-LKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 251820877 160 -KIIILDEATSMLDPEgRLDLIKivrEIKERHGMTVISITHD 200
Cdd:PRK11147 459 sNLLILDEPTNDLDVE-TLELLE---ELLDSYQGTVLLVSHD 496
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-217 |
5.24e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 13 KYNQEDEQYT---LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI----DGLLEAESGDIYIDGdaLTIDNVwdKRRLIGM 85
Cdd:TIGR00956 64 KLKKFRDTKTfdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDG--ITPEEI--KKHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQNP--DNQFVGATVEDDVAF-------GLENQGIPLEEMRSRV-DEALELVGMTD-FKTR---EPAR-LSGGQKQRVA 150
Cdd:TIGR00956 140 VVYNAetDVHFPHLTVGETLDFaarcktpQNRPDGVSREEYAKHIaDVYMATYGLSHtRNTKvgnDFVRgVSGGERKRVS 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251820877 151 IAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERHGMTV-ISITH-DLDEVALSDRVIVMKNGQ 217
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPlVAIYQcSQDAYELFDKVIVLYEGY 288
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-205 |
1.05e-09 |
|
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: 58.79 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgDIYIDGDALTIDNVwdkrrLIGMVFQNP---DNQFVGA 97
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARPQPGI-----KVGYLPQEPqldPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 98 TVEDDVA---------------FGLENQGIP--LEEMrSRVDEALELVGMTDFKT---------REP------ARLSGGQ 145
Cdd:TIGR03719 88 NVEEGVAeikdaldrfneisakYAEPDADFDklAAEQ-AELQEIIDAADAWDLDSqleiamdalRCPpwdadvTKLSGGE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 146 KQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKErhgmTVISITHD---LDEVA 205
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHDryfLDNVA 225
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-199 |
1.26e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 38 IIGHNGSGKSTTVRLIDGLLEAESGDIYIDGdaLTIDNVwdkrrligmvfQNPDNQFVG--------ATVEDDVAFGLEn 109
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKN--CNINNI-----------AKPYCTYIGhnlglkleMTVFENLKFWSE- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 110 qgipLEEMRSRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRlDLIKIVREIKER 189
Cdd:PRK13541 97 ----IYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLNNLIVMKAN 171
|
170
....*....|
gi 251820877 190 HGMTVISITH 199
Cdd:PRK13541 172 SGGIVLLSSH 181
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-185 |
2.66e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE--SGDIYIDG-DALTIDNVWDKR 80
Cdd:PRK09580 1 MLSIKDLHVSV---EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGkDLLELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 81 RLIGMVFQNP------DNQFVGATVEDDVAFGLENQGIPLEEMRSRVDEALELVGM-TDFKTRE-PARLSGGQKQRVAIA 152
Cdd:PRK09580 78 EGIFMAFQYPveipgvSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMpEDLLTRSvNVGFSGGEKKRNDIL 157
|
170 180 190
....*....|....*....|....*....|...
gi 251820877 153 GVVALRPKIIILDEATSMLDpegrLDLIKIVRE 185
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD----IDALKIVAD 186
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
136-217 |
4.40e-09 |
|
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: 54.64 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 136 REPARLSGGQKQRVAIAGVVALRPK--IIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVM 213
Cdd:cd03238 83 QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDF 161
|
....
gi 251820877 214 KNGQ 217
Cdd:cd03238 162 GPGS 165
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-216 |
4.65e-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: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 38 IIGHNGSGKSTTVRLIDGLLEAESGD-IYIDGDALTIDNVWDKRRLIGmvfqnpdnqfvgatveddvafglenqgiplee 116
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIV-------------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 117 mrsrvdealelvgmtdfkTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVR-----EIKERHG 191
Cdd:smart00382 55 ------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKN 116
|
170 180 190
....*....|....*....|....*....|.
gi 251820877 192 MTVISITHDLDE------VALSDRVIVMKNG 216
Cdd:smart00382 117 LTVILTTNDEKDlgpallRRRFDRRIVLLLI 147
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-217 |
1.15e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 16 QEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES--GDIYIDGDALTIDNVwdkrRLIGMVFQNpDNQ 93
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQD-DIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 94 FVGATVEDDVAF----GLENQgIPLEEMRSRVDEALELVGMTDFKTREPAR-----LSGGQKQRVAIAGVVALRPKIIIL 164
Cdd:PLN03211 152 YPHLTVRETLVFcsllRLPKS-LTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 251820877 165 DEATSMLDPEGRLDLIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQ 217
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyQMFDSVLVLSEGR 284
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-218 |
1.43e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYidgdaltidnvWDKRRL 82
Cdd:PRK15064 318 NALEVENLTKGF---DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-----------WSENAN 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPDNQFvgatvEDDVAFglenqgipLEEM---RSRVDEALELVGM------TDFKTREPAR-LSGGQKQRVAIA 152
Cdd:PRK15064 384 IGYYAQDHAYDF-----ENDLTL--------FDWMsqwRQEGDDEQAVRGTlgrllfSQDDIKKSVKvLSGGEKGRMLFG 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251820877 153 GVVALRPKIIILDEATSMLDPEGrldlIKIVREIKERHGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDREFVsSLATRIIEITPDGV 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-227 |
7.73e-08 |
|
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: 53.38 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaltidnvwdkrrligMVFQNPDNQFVGATVEDD 102
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLEN---------QGIPLEEMRSRVDEALELVGMTDFKTreparLSGGQKQRVAIAGVVALRPKIIILDEATSMLDp 173
Cdd:TIGR01271 507 IIFGLSYdeyrytsviKACQLEEDIALFPEKDKTVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDSPFTHLD- 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 174 egrldlIKIVREIKER------HGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:TIGR01271 581 ------VVTEKEIFESclcklmSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-216 |
8.60e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 16 QEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAESGDiYIDGDaLTIDNVWDKR----RLIGMVFQNpD 91
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTT---LMDVLAGRKTGG-YIEGD-IRISGFPKKQetfaRISGYCEQN-D 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 92 NQFVGATVEDDV---AFGLENQGIPLEEMRSRVDEALELVGMTDFKTR-----EPARLSGGQKQRVAIAGVVALRPKIII 163
Cdd:PLN03140 963 IHSPQVTVRESLiysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 251820877 164 LDEATSMLDPEGRLDLIKIVREIKERhGMTVISITH--DLDEVALSDRVIVMKNG 216
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHqpSIDIFEAFDELLLMKRG 1096
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-227 |
1.39e-07 |
|
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: 51.40 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaltidnvwdkrrligMVFQNPDNQFVGATVEDD 102
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLEN---------QGIPLEEMRSRVDEALELV----GMTdfktreparLSGGQKQRVAIAGVVALRPKIIILDEats 169
Cdd:cd03291 118 IIFGVSYdeyryksvvKACQLEEDITKFPEKDNTVlgegGIT---------LSGGQRARISLARAVYKDADLYLLDS--- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 170 mldPEGRLDLIKiVREIKER------HGMTVISITHDLDEVALSDRVIVMKNGQVESISTPNEL 227
Cdd:cd03291 186 ---PFGYLDVFT-EKEIFEScvcklmANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-214 |
1.71e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.67 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 24 NDVSFHvkQGEWLSIIGHNGSGKSTTVRLIdglleaesgdiyidGDALTIDNVWDKRRLigmvfqnpdnqfvgatveddv 103
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTILDAI--------------GLALGGAQSATRRRS--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 104 aFGLENQGIPLEEmrsrvdeaLELVGMTDfktrepaRLSGGQKQRVAIAGVVALRPK----IIILDEATSMLDPEGRLdl 179
Cdd:cd03227 57 -GVKAGCIVAAVS--------AELIFTRL-------QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQ-- 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 251820877 180 iKIVREIKER--HGMTVISITHDLDEVALSDRVIVMK 214
Cdd:cd03227 119 -ALAEAILEHlvKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-219 |
2.99e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 19 EQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIyidGDALTIDnvwdkrrligmvfqnpdnqfVGAT 98
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGIK--------------------LGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 99 VEDDVAFgLENQGIPLEEMRSRVDEALE-----LVGMTDFK----TREPARLSGGQKQRVAIAGVVALRPKIIILDEATS 169
Cdd:PRK10636 381 AQHQLEF-LRADESPLQHLARLAPQELEqklrdYLGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 251820877 170 MLDpegrLDLIKIVRE-IKERHGMTVIsITHDLDEV-ALSDRVIVMKNGQVE 219
Cdd:PRK10636 460 HLD----LDMRQALTEaLIDFEGALVV-VSHDRHLLrSTTDDLYLVHDGKVE 506
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-172 |
4.20e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDaLTIDnvwdkrRLIgmvfQNPDNQFVGaTVEDD 102
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD-LIVA------RLQ----QDPPRNVEG-TVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 103 VAFGLENQGIPLEE----------------------------------MRSRVDEALELVGMT-DFKTREparLSGGQKQ 147
Cdd:PRK11147 87 VAEGIEEQAEYLKRyhdishlvetdpseknlnelaklqeqldhhnlwqLENRINEVLAQLGLDpDAALSS---LSGGWLR 163
|
170 180
....*....|....*....|....*
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLD 172
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-205 |
5.99e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgDIYIDGDAltidnVWDKRRLIGMVFQNP---DNQFVGATV 99
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKEFEGEA-----RPAPGIKVGYLPQEPqldPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 100 EDDVA--FGL--------ENQGIP-------LEEMrSRVDEALELVGMTDFKTR-EPA--------------RLSGGQKQ 147
Cdd:PRK11819 92 EEGVAevKAAldrfneiyAAYAEPdadfdalAAEQ-GELQEIIDAADAWDLDSQlEIAmdalrcppwdakvtKLSGGERR 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251820877 148 RVAIAGVVALRPKIIILDEATSMLDPEGRLDLikivreikERH-----GmTVISITHD---LDEVA 205
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWL--------EQFlhdypG-TVVAVTHDryfLDNVA 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-174 |
9.33e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 3 NIIEVKNLKYKYnqeDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIdGDalTIDnvwdkrrl 82
Cdd:PRK11819 323 KVIEAENLSKSF---GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TVK-------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 83 IGMVFQNPDNQFVGATVEDDVAFGLENQGIPLEEMRSRVdealeLVGMTDFKTREPAR----LSGGQKQRVAIAGVVALR 158
Cdd:PRK11819 389 LAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRA-----YVGRFNFKGGDQQKkvgvLSGGERNRLHLAKTLKQG 463
|
170
....*....|....*.
gi 251820877 159 PKIIILDEATSMLDPE 174
Cdd:PRK11819 464 GNVLLLDEPTNDLDVE 479
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-258 |
1.63e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPDNQFVGATvED 101
Cdd:PRK10938 18 TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLSPG-ED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DvaFGLENQGIPLEEMR--SRVDEALELVGMTDFKTREPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGRLDL 179
Cdd:PRK10938 97 D--TGRTTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 180 IKIVREIkERHGMTVISITHDLDEV-ALSDRVIVMKNGQVESISTPNELfMREDLVdldldrpftTELASSLRQTGLDLP 258
Cdd:PRK10938 175 AELLASL-HQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEI-LQQALV---------AQLAHSEQLEGVQLP 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-218 |
1.74e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 4 IIEVKNLKYKYNQEDEQYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL--EAESGDIYIDGDALTIDNVwdkRR 81
Cdd:NF040905 257 VFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTV---SD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 82 LI--GMVFQNPDNQFVGATVEDDVAfglENQGIP-LEEMRSR--VDEALELVGMTDFKTR----------EPARLSGGQK 146
Cdd:NF040905 334 AIdaGLAYVTEDRKGYGLNLIDDIK---RNITLAnLGKVSRRgvIDENEEIKVAEEYRKKmniktpsvfqKVGNLSGGNQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251820877 147 QRVAIAGVVALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEV-ALSDRVIVMKNGQV 218
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELlGMCDRIYVMNEGRI 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-172 |
1.83e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 36 LSIIGHNGSGKSTTVRLIDGLLEAESGDIY--------------IDGDALTIDNvwdkrrLIGMVFQNPdnqfvgatved 101
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNP------LLYMMRCFP----------- 600
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251820877 102 dvafglenqGIPLEEMRSRvdeaLELVGMTDFKTREPA-RLSGGQKQRVAIAGVVALRPKIIILDEATSMLD 172
Cdd:PLN03073 601 ---------GVPEQKLRAH----LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
135-213 |
2.44e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 135 TREPARLSGGQKQRVAIAGVV--ALRPKIIILDEATSMLDPEGRLDLIKIVREIKErHGMTVISITHDLDEVALSDRVIV 212
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDTIRAADHVID 210
|
.
gi 251820877 213 M 213
Cdd:cd03270 211 I 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-232 |
1.46e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 136 REPARLSGGQKQRVAIAGVVA--LRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVM 213
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMISLADRIIDI 550
|
90 100
....*....|....*....|....*
gi 251820877 214 K------NGQVESISTPNELFMRED 232
Cdd:PRK00635 551 GpgagifGGEVLFNGSPREFLAKSD 575
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-227 |
4.26e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 119 SRVDEALELVGMTDFKTREPA-RLSGGQKQRVAIAGVVALR---PKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTV 194
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTV 885
|
90 100 110
....*....|....*....|....*....|....*....
gi 251820877 195 ISITHDLDEVALSDRVIVM------KNGQVESISTPNEL 227
Cdd:TIGR00630 886 VVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
119-224 |
6.40e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 43.37 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 119 SRVDEALELVGMTDFKTREPA-RLSGGQKQRVAIAGVVALR---PKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTV 194
Cdd:cd03271 147 ARKLQTLCDVGLGYIKLGQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTV 225
|
90 100 110
....*....|....*....|....*....|....*.
gi 251820877 195 ISITHDLDEVALSDRVIVM------KNGQVESISTP 224
Cdd:cd03271 226 VVIEHNLDVIKCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
38-201 |
8.55e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 38 IIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTidNVWDKRRLIGMVFQN---------PDNQF-------------- 94
Cdd:COG0419 28 IVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLI--NVGSEEASVELEFEHggkryrierRQGEFaefleakpserkea 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 95 ----VGATVEDDVAFGLENQGIPLEEMRSRVDEALELVG-----MTDFKtrEPARLSGGQKQRVAIAGVVALrpkiiILD 165
Cdd:COG0419 106 lkrlLGLEIYEELKERLKELEEALESALEELAELQKLKQeilaqLSGLD--PIETLSGGERLRLALADLLSL-----ILD 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 251820877 166 eaTSMLDPEGRLDLIKIVREIKErhgmtvisITHDL 201
Cdd:COG0419 179 --FGSLDEERLERLLDALEELAI--------ITHVI 204
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-202 |
1.13e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGDIYIDG--------------DALTIDNVWDKRRligmVFQ 88
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalPQPALEYVIDGDR----EYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 89 NPDNQFVGATVEDD---VAFgLENQ--GIPLEEMRSRVDEALELVGMTDFKTREPAR-LSGGQKQRVAIAGVVALRPKII 162
Cdd:PRK10636 93 QLEAQLHDANERNDghaIAT-IHGKldAIDAWTIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 251820877 163 ILDEATSMLDpegrLD-LIKIVREIKERHGmTVISITHDLD 202
Cdd:PRK10636 172 LLDEPTNHLD----LDaVIWLEKWLKSYQG-TLILISHDRD 207
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
114-213 |
2.46e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 114 LEEMRSRVdEALELVGMtDFKT--REPARLSGGQKQRVAIAGVV--ALRPKIIILDEATSMLDPEGRLDLIKIVREIKER 189
Cdd:TIGR00630 462 LKEIRERL-GFLIDVGL-DYLSlsRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDL 539
|
90 100
....*....|....*....|....
gi 251820877 190 hGMTVISITHDLDEVALSDRVIVM 213
Cdd:TIGR00630 540 -GNTLIVVEHDEDTIRAADYVIDI 562
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
38-223 |
5.58e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.76 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 38 IIGHNGSGKSTTVRLIDGLLEAESGDIYIDGDALTIDNVWDKRRLIGMVFQNPDNQFVGATVEDDVAFGLENQ------- 110
Cdd:COG3593 28 LVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLLSRLLRLLLKEEDKEELEEAleelnee 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 111 -GIPLEEMRSRVDEALEL------------------------VGMTDFKTREPARLSGGQKQRVAIAGVVAL-------R 158
Cdd:COG3593 108 lKEALKALNELLSEYLKElldgldlelelsldeledllkslsLRIEDGKELPLDRLGSGFQRLILLALLSALaelkrapA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251820877 159 PKIIILDEatsmldPEGRL------DLIKIVREIKERHGMTVISiTHD---LDEVALsDRVIVMKNGQVESIST 223
Cdd:COG3593 188 NPILLIEE------PEAHLhpqaqrRLLKLLKELSEKPNQVIIT-THSphlLSEVPL-ENIRRLRRDSGGTTST 253
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-172 |
8.87e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVR-----LIDGL------LEAESGDIYIDGDAL--TIDNVWDKRRL----IGM 85
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIpkncqiLHVEQEVVGDDTTALqcVLNTDIERTQLleeeAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 86 VFQNPDNQFVGATVEDDVAfglENQGIPLEEMRSRVDEA---LELV--------------GMT---DFKTREPARLSGGQ 145
Cdd:PLN03073 273 VAQQRELEFETETGKGKGA---NKDGVDKDAVSQRLEEIykrLELIdaytaearaasilaGLSftpEMQVKATKTFSGGW 349
|
170 180
....*....|....*....|....*..
gi 251820877 146 KQRVAIAGVVALRPKIIILDEATSMLD 172
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-258 |
1.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 141 LSGGQKQRVAIAGVV---ALRPKIIILDEATSMLDPEGRLDLIKIVREIKERhGMTVISITHDLDEVALSDRVIVM---- 213
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKVADYVLELgpeg 888
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 251820877 214 --KNGQVESISTPNELfmredlvdLDLDRPFTTELASSLRQTgLDLP 258
Cdd:PRK00635 889 gnLGGYLLASCSPEEL--------IHLHTPTAKALRPYLSSP-QELP 926
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
38-220 |
2.48e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.40 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 38 IIGHNGSGKSTtvrlidgLLEAESGDIYidGDALTIDNVWDKRRLIgmvfqnpdnqfvgATVED--DVAFGLENQGIPLE 115
Cdd:cd03279 33 ICGPTGAGKST-------ILDAITYALY--GKTPRYGRQENLRSVF-------------APGEDtaEVSFTFQLGGKKYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 116 EMRSR---VDEALELV-----GMTDFKTREPARLSGGQKQRVAIA------GVVALRPKI----IILDEATSMLDPEGRL 177
Cdd:cd03279 91 VERSRgldYDQFTRIVllpqgEFDRFLARPVSTLSGGETFLASLSlalalsEVLQNRGGArleaLFIDEGFGTLDPEALE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 251820877 178 DLIKIVREIKERHGMTVIsITH--DLDEvALSDRVIVMKNGQVES 220
Cdd:cd03279 171 AVATALELIRTENRMVGV-ISHveELKE-RIPQRLEVIKTPGGSR 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
127-209 |
2.65e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.26 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 127 LVGMTDFKTRepARLSGGQKQ------RVAIAGVVALRPKIIILDEATSMLDPEG----RLDLIKIVREIKERHGMTVIS 196
Cdd:TIGR00606 1188 LKGDTALDMR--GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLV 1265
|
90
....*....|...
gi 251820877 197 ITHDLDEVALSDR 209
Cdd:TIGR00606 1266 ITHDEDFVELLGR 1278
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
36-213 |
9.28e-03 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 37.28 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 36 LSIIGHNGSGKSTTVR-LIDGLLEAESGDIYID--GDALTIDNVWDKRRLIGMVFQNPDNQF------VGATVED----- 101
Cdd:COG0433 50 ILILGATGSGKSNTLQvLLEELSRAGVPVLVFDphGEYSGLAEPGAERADVGVFDPGAGRPLpinpwdLFATASElgpll 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 102 DVAFGL-ENQGIPLEEM-RSRVDEALELVGMTDFKTR-EPARLSGGQKQRVAIAGVVALRPKIIILDEATSMLDPEGrLD 178
Cdd:COG0433 130 LSRLDLnDTQRGVLREAlRLADDKGLLLLDLKDLIALlEEGEELGEEYGNVSAASAGALLRRLESLESADGLFGEPG-LD 208
|
170 180 190
....*....|....*....|....*....|....*
gi 251820877 179 LIKIvreIKERHGMTVIsithDLDEVALSDRVIVM 213
Cdd:COG0433 209 LEDL---LRTDGRVTVI----DLSGLPEELQSTFV 236
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
139-185 |
9.96e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.52 E-value: 9.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 251820877 139 ARLSGGQKQR---VAI-AGVVAL---------RPKIIILDEATSMLDPEGRLDLIKIVRE 185
Cdd:pfam13558 31 GGLSGGEKQLlayLPLaAALAAQygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
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