|
Name |
Accession |
Description |
Interval |
E-value |
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-269 |
0e+00 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 513.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK 80
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALN 160
Cdd:PRK13648 81 LRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTTIG 240
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELTRIG 240
|
250 260
....*....|....*....|....*....
gi 613389154 241 LDLPFPIKINQMLGHQTSFLTYEGLVDQL 269
Cdd:PRK13648 241 LDLPFPIKINQMLGHQTSFLTYEGLVDQL 269
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-269 |
4.94e-139 |
|
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: 391.79 E-value: 4.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNN-QTITDDNFEKLRKDIG 86
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIIL 166
Cdd:TIGR04520 81 MVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDLPFP 246
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVELLKEIGLDVPFI 240
|
250 260
....*....|....*....|....*...
gi 613389154 247 IKINQMLGHQ-----TSFLTYEGLVDQL 269
Cdd:TIGR04520 241 TELAKALKKRgiplpPDILTEEELVDEL 268
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-269 |
6.74e-131 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 371.66 E-value: 6.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 3 DKNSVIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLR 82
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPS 162
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLD 242
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQEIGLD 240
|
250 260 270
....*....|....*....|....*....|..
gi 613389154 243 LPFPIKINQMLGHQ-----TSFLTYEGLVDQL 269
Cdd:PRK13635 241 VPFSVKLKELLKRNgillpNTYLTMESLVDEL 272
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-269 |
4.31e-109 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 316.16 E-value: 4.31e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK 80
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALN 160
Cdd:PRK13632 81 IRKKIGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTTIG 240
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILEKAK 240
|
250 260
....*....|....*....|....*....
gi 613389154 241 LDLPFPIKINQMLGHQTSFLTYEGLVDQL 269
Cdd:PRK13632 241 IDSPFIYKLSKKLKGIDPTYNEEELIEQI 269
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-236 |
4.68e-109 |
|
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: 314.27 E-value: 4.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:COG1122 80 VFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEEL 236
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-269 |
1.15e-104 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 305.12 E-value: 1.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDA-SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKD 84
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVI 164
Cdd:PRK13650 83 IGMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDLP 244
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLGLDIP 242
|
250 260 270
....*....|....*....|....*....|
gi 613389154 245 FPIKINQMLGHQ-----TSFLTYEGLVDQL 269
Cdd:PRK13650 243 FTTSLVQSLRQNgydlpEGYLTEKELEEQL 272
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-253 |
5.81e-100 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 293.24 E-value: 5.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 4 KNSVIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI----ENVKSgEIFYNNQTITDDNFE 79
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNS-KITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 80 KLRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLAL 159
Cdd:PRK13640 81 DIREKVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTTI 239
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEI 240
|
250
....*....|....
gi 613389154 240 GLDLPFPIKINQML 253
Cdd:PRK13640 241 GLDIPFVYKLKNKL 254
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-219 |
3.35e-96 |
|
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: 281.28 E-value: 3.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 9 VFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIV 88
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 89 FQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:cd03225 81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613389154 169 ATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGT 219
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-269 |
2.08e-88 |
|
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: 263.93 E-value: 2.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDD---NFEKL 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDIGIVFQNPDNQ-FVGSIVKyDVAFGLENHAVPHDEMHRRVSEALKQV----DMLERAdyePNALSGGQKQRVAIASV 156
Cdd:TIGR04521 81 RKKVGLVFQFPEHQlFEETVYK-DIAFGPKNLGLSEEEAEERVKEALELVgldeEYLERS---PFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEE 235
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEyADRVIVMHKGKIVLDGTPREVFSDVDE 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 613389154 236 LTTIGLDLPFPIKINQML---GHQ--TSFLTYEGLVDQL 269
Cdd:TIGR04521 237 LEKIGLDVPEITELARKLkekGLPvpKDPLTVEEAADEI 275
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-244 |
2.07e-86 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 258.86 E-value: 2.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 4 KNSVIVFKNVSFQYQSDASFT----LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNN-QTITDDNF 78
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 79 EKLRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTT 238
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMMKK 240
|
....*.
gi 613389154 239 IGLDLP 244
Cdd:PRK13633 241 IGLDVP 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-245 |
9.38e-79 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 239.22 E-value: 9.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRK 83
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:PRK13642 82 KIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDL 243
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDV 241
|
..
gi 613389154 244 PF 245
Cdd:PRK13642 242 PF 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-238 |
1.00e-77 |
|
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: 244.04 E-value: 1.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASFT---LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITD---DNFEK 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQF-----VGSIVkydvAFGLENHAV-PHDEMHRRVSEALKQVDMLER-ADYEPNALSGGQKQRVAI 153
Cdd:COG1123 340 LRRRVQMVFQDPYSSLnprmtVGDII----AEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
....*.
gi 613389154 233 AEELTT 238
Cdd:COG1123 496 PQHPYT 501
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-236 |
3.52e-77 |
|
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: 242.50 E-value: 3.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI---ENVKSGEIFYNNQTITDDNFEKL 81
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNP 161
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEEL 236
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-269 |
4.70e-75 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 230.29 E-value: 4.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT----DDNFEK 80
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQV----DMLERADYEpnaLSGGQKQRVAIASV 156
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVglpeELLARSPFE---LSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEE 235
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 613389154 236 LTTIGLDLPFPIKINQMLGHQTSF------LTYEGLVDQL 269
Cdd:PRK13634 240 LEAIGLDLPETVKFKRALEEKFGIsfpkpcLTLEELAHEV 279
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-232 |
2.46e-64 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 204.95 E-value: 2.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnfekL---R 82
Cdd:COG3842 4 PALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LppeK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQN----P-----DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
Cdd:COG3842 77 RNVGMVFQDyalfPhltvaEN----------VAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-232 |
6.12e-63 |
|
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: 197.42 E-value: 6.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITD-DNFE--KL 81
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDIGIVFQNPdNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNP 161
Cdd:cd03258 81 RRRIGMIFQHF-NLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDlseaME-----ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHE----MEvvkriCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-220 |
9.18e-63 |
|
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: 196.20 E-value: 9.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnFEKLRKDIGI 87
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG--VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:cd03259 77 VFQDYalfphltvaEN----------IAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-220 |
2.12e-62 |
|
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: 195.80 E-value: 2.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT---DDNFEKLRKDIGIV 88
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsRRLRKIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 89 FQNPDNQF-----VGSIVkydvAFGLENHAVPHDEMH--RRVSEALKQVDMLE-RADYEPNALSGGQKQRVAIASVLALN 160
Cdd:cd03257 88 FQDPMSSLnprmtIGEQI----AEPLRIHGKLSKKEArkEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-236 |
1.22e-61 |
|
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: 194.43 E-value: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYqsdASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT---DDNFEKLR 82
Cdd:COG1127 5 MIEVRNLTKSF---GDRVvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglsEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQNP---------DNqfvgsivkydVAFGL-ENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVA 152
Cdd:COG1127 82 RRIGMLFQGGalfdsltvfEN----------VAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFD 231
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
....*
gi 613389154 232 HAEEL 236
Cdd:COG1127 232 SDDPW 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
1.50e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 194.54 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQYQS-DASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITddnf 78
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTgGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 79 eKLRKDIGIVFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQ 149
Cdd:COG1116 77 -GPGPDRGVVFQEPallpwltvlDN----------VALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 150 RVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA--MeADHVIVMNKG 218
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAvfL-ADRVVVLSAR 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-244 |
2.11e-61 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 195.27 E-value: 2.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDD--NFEKLR 82
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQV--DMLERADYEPNALSGGQKQRVAIASVLALN 160
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE-AMEADHVIVMNKGTVYKEGTATEIFDHAEELTTI 239
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPREVFKEVETLESI 242
|
....*
gi 613389154 240 GLDLP 244
Cdd:PRK13637 243 GLAVP 247
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-233 |
2.11e-60 |
|
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: 191.41 E-value: 2.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIG 86
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNPDNQF---VgsivkYD-VAFGLENH----AVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:COG1120 79 YVPQEPPAPFgltV-----RElVALGRYPHlglfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHA 233
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEVLTPE 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-263 |
3.19e-59 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 189.43 E-value: 3.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnFEKL---RK 83
Cdd:PRK13644 1 MIRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD--FSKLqgiRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:PRK13644 78 LVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAeELTTIGLDL 243
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV-SLQTLGLTP 235
|
250 260
....*....|....*....|
gi 613389154 244 PFPIKINQMLGHQTSFLTYE 263
Cdd:PRK13644 236 PSLIELAENLKMHGVVIPWE 255
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
4.28e-59 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 189.29 E-value: 4.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDknSVIVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTI--TDDNF 78
Cdd:PRK13636 1 MED--YILKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 79 EKLRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:PRK13636 78 MKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE-AMEADHVIVMNKGTVYKEGTATEIFDHAEELT 237
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
....*..
gi 613389154 238 TIGLDLP 244
Cdd:PRK13636 238 KVNLRLP 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-244 |
4.44e-59 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 189.13 E-value: 4.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN--FEKLRKDIGIV 88
Cdd:PRK13639 5 RDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 89 FQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:PRK13639 84 FQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 169 ATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDLP 244
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRLP 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-238 |
1.09e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 189.90 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQS-DASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL---R 82
Cdd:COG1135 2 IELENLSKTFPTkGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
Cdd:COG1135 82 RKIGMIFQHFnllssrtvaEN----------VALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDlseaME-----ADHVIVMNKGTVYKEGTATE 228
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE----MDvvrriCDRVAVLENGRIVEQGPVLD 227
|
250
....*....|
gi 613389154 229 IFDHAEELTT 238
Cdd:COG1135 228 VFANPQSELT 237
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-220 |
4.61e-58 |
|
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: 184.23 E-value: 4.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDA--SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL---- 81
Cdd:cd03255 1 IELKNLSKTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDIGIVFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVA 152
Cdd:cd03255 81 RRHIGFVFQSFnllpdltalEN----------VELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-223 |
4.60e-57 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 182.17 E-value: 4.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL- 81
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 ---RKDIGIVFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQ 149
Cdd:COG1136 82 rlrRRHIGFVFQFFnllpeltalEN----------VALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 150 RVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-238 |
9.00e-57 |
|
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: 181.92 E-value: 9.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQN 91
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 PDnqfvGSI-----VKYDVAFGLENHAVPHDEmhRRVSEALKQVDMLER-ADYEPNALSGGQKQRVAIASVLALNPSVII 165
Cdd:COG1124 88 PY----ASLhprhtVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTATEIFDHAEELTT 238
Cdd:COG1124 162 LDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAvvAHL-CDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-218 |
1.35e-56 |
|
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: 179.12 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIvkydvafglenhavphdemhrrvsealkqvdmleradyEPNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:cd03228 81 VPQDP-FLFSGTI--------------------------------------RENILSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKG 218
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-228 |
1.84e-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: 1.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQ---TITDDNFEKLRK 83
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQnpDNQF-----VgsivkYD-VAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVL 157
Cdd:COG2884 80 RIGVVFQ--DFRLlpdrtV-----YEnVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLS--EAMEAdHVIVMNKGTVYKEGTATE 228
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLElvDRMPK-RVLELEDGRLVRDEARGV 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-256 |
2.34e-56 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 181.92 E-value: 2.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIG 86
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIIL 166
Cdd:PRK13652 82 LVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDLPF 245
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPS 241
|
250
....*....|.
gi 613389154 246 PIKINQMLGHQ 256
Cdd:PRK13652 242 LPKLIRSLQAQ 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-223 |
4.36e-56 |
|
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: 179.59 E-value: 4.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQS-DASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnfekLRKDI 85
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASV 156
Cdd:cd03293 76 GYVFQQDallpwltvlDN----------VALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNK--GTVYKE 223
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-257 |
6.15e-56 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 180.70 E-value: 6.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKD 84
Cdd:PRK13647 2 DNIIEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVI 164
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGtATEIFDHAEELTTIGLDL 243
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEwADQVIVLKEGRVLAEG-DKSLLTDEDIVEQAGLRL 238
|
250
....*....|....
gi 613389154 244 PFPIKINQMLGHQT 257
Cdd:PRK13647 239 PLVAQIFEDLPELG 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-232 |
2.92e-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: 180.63 E-value: 2.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE---NVKSGEIFYNNQTIT---DDNFEKLR-KDIGIVFQNPDNQF--- 96
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLklsEKELRKIRgREIQMIFQDPMTSLnpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 97 --VGSIVkydvAFGLENHA-VPHDEMHRRVSEALKQV---DMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:COG0444 103 mtVGDQI----AEPLRIHGgLSKAEARERAIELLERVglpDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG0444 179 TALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-241 |
5.80e-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: 5.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDnQFVGSIvkYD-VAFGleNHAVPHDEMHrrvsEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAS 155
Cdd:COG2274 554 VLQDVF-LFSGTI--REnITLG--DPDATDEEII----EAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTateifdHAEE 235
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT------HEEL 696
|
....*.
gi 613389154 236 LTTIGL 241
Cdd:COG2274 697 LARKGL 702
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-229 |
6.74e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 176.79 E-value: 6.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsdASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIG 86
Cdd:COG1131 1 IEVRGLTKRY---GDKTaLDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNP---------DN-QFVGSIvkydvafglenHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASV 156
Cdd:COG1131 77 YVPQEPalypdltvrENlRFFARL-----------YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-236 |
1.82e-54 |
|
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: 175.77 E-value: 1.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFE---KLRKD 84
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQnpDNQFVGSIVKYD-VAFGL-ENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPS 162
Cdd:cd03261 79 MGMLFQ--SGALFDSLTVFEnVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEEL 236
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-224 |
2.89e-53 |
|
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: 170.69 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQ 90
Cdd:cd03214 3 ENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 91 npdnqfvgsivkydvafglenhavphdemhrrvseALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:cd03214 81 -----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
25-235 |
4.18e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.49 E-value: 4.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDD--NFEKLRKDIGIVFQNPdNQF----Vg 98
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkDINKLRRKVGMVFQQF-NLFphltV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 sivkydvafgLEN--------HAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:COG1126 95 ----------LENvtlapikvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEE 235
Cdd:COG1126 165 SALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-232 |
4.46e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.58 E-value: 4.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 3 DKNSVIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDnfeklR 82
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQNP--DNQF---VgsivkYD-VAFGLENH----AVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVA 152
Cdd:COG1121 75 RRIGYVPQRAevDWDFpitV-----RDvVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYkEGTATEIFD 231
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREyFDRVLLLNRGLVA-HGPPEEVLT 227
|
.
gi 613389154 232 H 232
Cdd:COG1121 228 P 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-232 |
6.60e-53 |
|
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: 171.65 E-value: 6.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITddNFEKLRKDIGI 87
Cdd:cd03300 1 IELENVSKFYGGFVA--LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:cd03300 77 VFQNY-ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-232 |
6.81e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 175.26 E-value: 6.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnFEKLRKDIGI 87
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD--LPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:COG3839 80 VFQSYalyphmtvyEN----------IAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-256 |
1.09e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 172.62 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK---- 80
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQV----DMLERADYEpnaLSGGQKQRVAIASV 156
Cdd:PRK13649 83 IRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVgiseSLFEKNPFE---LSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSE-AMEADHVIVMNKGTVYKEGTATEIFDHAEE 235
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDvANYADFVYVLEKGKLVLSGKPKDIFQDVDF 238
|
250 260
....*....|....*....|.
gi 613389154 236 LTTIGLDLPFPIKINQMLGHQ 256
Cdd:PRK13649 239 LEEKQLGVPKITKFAQRLADR 259
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-232 |
1.85e-52 |
|
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: 170.98 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsdASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKlrKDIG 86
Cdd:cd03296 3 IEVRNVSKRF---GDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNPdNQFVGSIVKYDVAFGLE----NHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPS 162
Cdd:cd03296 78 FVFQHY-ALFRHMTVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-229 |
4.32e-52 |
|
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: 169.28 E-value: 4.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKST----IAKLMIGIENVK-SGEIFYNNQTITDDNF--EK 80
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTllrlLNRLNDLIPGAPdEGEVLLDGKDIYDLDVdvLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPdNQFVGSIvkYD-VAFGLENHAV-PHDEMHRRVSEALKQVDMLERADYEPNA--LSGGQKQRVAIASV 156
Cdd:cd03260 79 LRRRVGMVFQKP-NPFPGSI--YDnVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-219 |
1.06e-51 |
|
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: 165.88 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 10 FKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVF 89
Cdd:cd00267 2 IENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 90 QnpdnqfvgsivkydvafglenhavphdemhrrvsealkqvdmleradyepnaLSGGQKQRVAIASVLALNPSVIILDEA 169
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 170 TSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEA-DHVIVMNKGT 219
Cdd:cd00267 108 TSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-244 |
1.22e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.91 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQY-QSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT---DDNFEKL 81
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDIGIVFQNpdnqF--VGSIVKYD-VAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:PRK11153 81 RRQIGMIFQH----FnlLSSRTVFDnVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDlseaME-----ADHVIVMNKGTVYKEGTATEIFDHA 233
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE----MDvvkriCDRVAVIDAGRLVEQGTVSEVFSHP 232
|
250
....*....|....*...
gi 613389154 234 -EELT------TIGLDLP 244
Cdd:PRK11153 233 kHPLTrefiqsTLHLDLP 250
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-232 |
1.35e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 171.87 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsdASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItddnFEKL---RK 83
Cdd:COG1118 3 IEVRNISKRF---GSFTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLpprER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQNP---------DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
Cdd:COG1118 76 RVGFVFQHYalfphmtvaEN----------IAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-234 |
3.65e-51 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 175.74 E-value: 3.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG1132 340 IEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQnpDNQ-FVGSIvKYDVAFGLENhaVPHDEmhrrVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAS 155
Cdd:COG1132 419 VPQ--DTFlFSGTI-RENIRYGRPD--ATDEE----VEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 156 VLALNPSVIILDEATSMLDPDA----RQNLLDLVRkvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTateifd 231
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETealiQEALERLMK------GRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT------ 557
|
...
gi 613389154 232 HAE 234
Cdd:COG1132 558 HEE 560
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-232 |
2.74e-50 |
|
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: 172.56 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENvKSGEIFYNNQTITDDNFEK---LRKDIGIVFQNPdnqF----- 96
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP---Fgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 97 ---VGSIVkydvAFGLENHAVPHD--EMHRRVSEALKQV----DMLERadYePNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:COG4172 378 rmtVGQII----AEGLRVHGPGLSaaERRARVAEALEEVgldpAARHR--Y-PHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAvvRAL-AHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-206 |
1.37e-49 |
|
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: 161.82 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 17 YQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDD--NFEKLRKDIGIVFQNPDN 94
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSrkGLLERRQRVGLVFQDPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|..
gi 613389154 175 PDARQNLLDLVRKVKSEHNITIISiTHDLSEA 206
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVIS-THDVDLA 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-219 |
9.04e-49 |
|
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: 159.27 E-value: 9.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQY-QSDAsftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFE--KLRKD 84
Cdd:cd03229 1 LELKNVSKRYgQKTV---LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPdNQFVGSIVKYDVAFGLenhavphdemhrrvsealkqvdmleradyepnalSGGQKQRVAIASVLALNPSVI 164
Cdd:cd03229 78 IGMVFQDF-ALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGT 219
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-228 |
1.26e-48 |
|
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: 160.86 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQnpDNQFVGSIVKYDVAFGLENHAvphDEmhrRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIASV 156
Cdd:cd03253 80 VPQ--DTVLFNDTIGYNIRYGRPDAT---DE---EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATE 228
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEE 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-228 |
1.67e-48 |
|
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: 168.40 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 3 DKNSVIVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLR 82
Cdd:COG4988 332 AGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQNP--------DNqfvgsivkydVAFGleNHAVPHDEMHRrvseALKQVDMLERADYEPN-----------AL 143
Cdd:COG4988 411 RQIAWVPQNPylfagtirEN----------LRLG--RPDASDEELEA----ALEAAGLDEFVAALPDgldtplgeggrGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 144 SGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKE 223
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQ 552
|
....*
gi 613389154 224 GTATE 228
Cdd:COG4988 553 GTHEE 557
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
11-230 |
2.38e-48 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 161.16 E-value: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYQSDASF-------TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRK 83
Cdd:COG4167 8 RNLSKTFKYRTGLfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQNPDNQF-----VGSIvkydvafgLE-----NHAVPHDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVA 152
Cdd:COG4167 88 HIRMIFQDPNTSLnprlnIGQI--------LEeplrlNTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSeAME--ADHVIVMNKGTVYKEGTATEIF 230
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLG-IVKhiSDKVLVMHQGEVVEYGKTAEVF 238
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-238 |
4.05e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 159.84 E-value: 4.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRK-- 83
Cdd:COG3638 1 PMLELRNLSKRYPGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 -DIGIVFQNP---DNQFVgsivkydvafgLEN------HAVP---------HDEMHRRVSEALKQVDMLERADYEPNALS 144
Cdd:COG3638 80 rRIGMIFQQFnlvPRLSV-----------LTNvlagrlGRTStwrsllglfPPEDRERALEALERVGLADKAYQRADQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 145 GGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVyke 223
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRV--- 225
|
250
....*....|....*.
gi 613389154 224 gtateIFD-HAEELTT 238
Cdd:COG3638 226 -----VFDgPPAELTD 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-220 |
4.57e-48 |
|
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: 158.46 E-value: 4.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDD--NFEKLRKDIGIVFQNpDNQFVGSIVK 102
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkkNINELRQKVGMVFQQ-FNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVAFGLEN-HAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNL 181
Cdd:cd03262 95 ENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 613389154 182 LDLVRKVKSEHnITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03262 175 LDVMKDLAEEG-MTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-230 |
9.73e-48 |
|
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: 159.73 E-value: 9.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL----RKDIGIVFQN-- 91
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSfa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 --P-----DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVI 164
Cdd:cd03294 113 llPhrtvlEN----------VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-220 |
1.90e-47 |
|
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: 156.65 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItddNFEKLRKDIGIVFQ 90
Cdd:cd03226 3 ENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 91 NPDNQFVGSIVKYDVAFGLENHavphDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:cd03226 79 DVDYQLFTDSVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
8-244 |
8.20e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 157.63 E-value: 8.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT----DDNFEK 80
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQV----DMLERAdyePNALSGGQKQRVAIASV 156
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLgfsrDVMSQS---PFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE-AMEADHVIVMNKGTVYKEGTATEIFDHAEE 235
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
....*....
gi 613389154 236 LTTIGLDLP 244
Cdd:PRK13646 240 LADWHIGLP 248
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-231 |
1.46e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 155.30 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSdasFTLKdVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKlRKdIGI 87
Cdd:COG3840 2 LRLDDLTYRYGD---FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNpDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:COG3840 76 LFQE-NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFD 231
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-228 |
3.72e-46 |
|
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: 154.62 E-value: 3.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIG 86
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNPdNQFVGSIvKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERAdYEPNA------LSGGQKQRVAIASVLALN 160
Cdd:cd03249 81 LVSQEP-VLFDGTI-AENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDG-YDTLVgergsqLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 161 PSVIILDEATSMLDPDAR---QNLLDLVRKvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATE 228
Cdd:cd03249 158 PKILLLDEATSALDAESEklvQEALDRAMK-----GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-221 |
5.72e-46 |
|
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: 153.07 E-value: 5.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 10 FKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQtitddNFEKLRKDIGIVF 89
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 90 QNP--DNQFVGSiVKYDVAFGLENHAVPHDEMHR----RVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:cd03235 75 QRRsiDRDFPIS-VRDVVLMGLYGHKGLFRRLSKadkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVY 221
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-171 |
6.20e-46 |
|
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: 150.88 E-value: 6.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPdNQFVGSIVKYD 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDP-QLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 105 VAFGLENHAVPHDEMHRRVSEALKQVDML----ERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATS 171
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-235 |
9.13e-46 |
|
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: 153.65 E-value: 9.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKlrKDIGIVFQNpDNQFVGSIVK 102
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQN-YALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLL 182
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613389154 183 DLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTATEIFDHAEE 235
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-232 |
1.45e-45 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 156.42 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 2 EDKNSVIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKl 81
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 rKDIGIVFQN----P-----DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVA 152
Cdd:PRK11432 78 -RDICMVFQSyalfPhmslgEN----------VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFD 231
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYR 226
|
.
gi 613389154 232 H 232
Cdd:PRK11432 227 Q 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-232 |
1.52e-45 |
|
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: 153.23 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKlMIG--IENvKSGEIFYNNQTITDDNFEKLRKDI 85
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINrlIEP-TSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQNpdnqfVGSI----VKYDVAFGLENHAVPHDEMHRRVSEALKQVDM--LERADYEPNALSGGQKQRVAIASVLAL 159
Cdd:cd03295 78 GYVIQQ-----IGLFphmtVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-220 |
1.75e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG4619 1 LELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdnQFVGSIVKYDVAFGLENHAVPHDEMhrRVSEALKQV----DMLERadyEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:COG4619 79 VPQEP--ALWGGTVRDNLPFPFQLRERKFDRE--RALELLERLglppDILDK---PVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
27-232 |
2.57e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 154.89 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFE---KLRKDIGIVFQNPD---N--QFVG 98
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrPLRRRMQMVFQDPYaslNprMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SIvkydVAFGLENHAV-PHDEMHRRVSEALKQVDmLERADYE--PNALSGGQKQRVAIASVLALNPSVIILDEATSMLDP 175
Cdd:COG4608 116 DI----IAEPLRIHGLaSKAERRERVAELLELVG-LRPEHADryPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 176 DARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG4608 191 SIQAQVLNLLEDLQDELGLTYLFISHDLSvvRHI-SDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-220 |
3.98e-45 |
|
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: 149.86 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdNFEKLRKDIGI 87
Cdd:cd03230 1 IEVRNLSKRYGKKTA--LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDnqfvgsivkydvafglenhavPHDEMhrRVSEALKqvdmleradyepnaLSGGQKQRVAIASVLALNPSVIILD 167
Cdd:cd03230 78 LPEEPS---------------------LYENL--TVRENLK--------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-244 |
6.86e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 152.85 E-value: 6.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDD-----NFE 79
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 80 KLRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLER-ADYEPNALSGGQKQRVAIASVLA 158
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEELT 237
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
....*..
gi 613389154 238 TIGLDLP 244
Cdd:PRK13645 247 KIEIDPP 253
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 |
7.14e-45 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 151.73 E-value: 7.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQY-QSDAsftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKL---MI-GIENVK-SGEIFYNNQTIT 74
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYgDKQA---LKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNdLIPGARvEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 75 DDNF--EKLRKDIGIVFQNPdNQFVGSIvkYD-VAFGLENHAV-PHDEMHRRVSEALKQV-------DMLERAdyePNAL 143
Cdd:COG1117 82 DPDVdvVELRRRVGMVFQKP-NPFPKSI--YDnVAYGLRLHGIkSKSELDEIVEESLRKAalwdevkDRLKKS---ALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 144 SGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAME-ADHVIVMNKGTVYK 222
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARvSDYTAFFYLGELVE 233
|
250
....*....|....*.
gi 613389154 223 EGTATEIFDH-AEELT 237
Cdd:COG1117 234 FGPTEQIFTNpKDKRT 249
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-229 |
1.71e-44 |
|
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: 150.39 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIG 86
Cdd:COG4555 1 MIEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQN---PDNQFVGSIVKYdvaFGlENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:COG4555 78 VLPDErglYDRLTVRENIRY---FA-ELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFS-SHIMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
8-269 |
4.79e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 150.75 E-value: 4.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFT---LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT----DDNFEK 80
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLER-ADYEPNALSGGQKQRVAIASVLAL 159
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEELTT 238
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWLKK 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 613389154 239 IGLDLPFPIKINQML---GHQTSF--LTYEGLVDQL 269
Cdd:PRK13641 242 HYLDEPATSRFASKLekgGFKFSEmpLTIDELVDGI 277
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-233 |
1.27e-43 |
|
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: 148.22 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRK--- 83
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQ------------NPDNQFVGSIVKYDVAFGLEnhavpHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
Cdd:TIGR02315 80 RIGMIFQhynlierltvleNVLHGRLGYKPTWRSLLGRF-----SEEDKERALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 152 AIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSELD 234
|
...
gi 613389154 231 DHA 233
Cdd:TIGR02315 235 DEV 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-220 |
1.70e-43 |
|
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: 146.78 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITD---DNFEKLRKD 84
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQnpDNQFVGSIVKYD-VAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:cd03292 80 IGVVFQ--DFRLLPDRNVYEnVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHD--LSEAMEaDHVIVMNKGTV 220
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAkeLVDTTR-HRVIALERGKL 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-249 |
3.66e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 149.23 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEI----FYNNQTITDD------------NFEKLRKDIGIV 88
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHelitnpyskkikNFKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 89 FQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQV----DMLERADYEpnaLSGGQKQRVAIASVLALNPSVI 164
Cdd:PRK13631 122 FQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMglddSYLERSPFG---LSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 165 ILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDL 243
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHIINSTSIQV 277
|
....*.
gi 613389154 244 PFPIKI 249
Cdd:PRK13631 278 PRVIQV 283
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-235 |
3.80e-43 |
|
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: 146.94 E-value: 3.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL---RKD 84
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQN---PDNQFV---------GSIVKYDVAFGLenhavPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVA 152
Cdd:cd03256 80 IGMIFQQfnlIERLSVlenvlsgrlGRRSTWRSLFGL-----FPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFD 231
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTD 234
|
....
gi 613389154 232 HAEE 235
Cdd:cd03256 235 EVLD 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-254 |
6.79e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 147.08 E-value: 6.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 15 FQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItddNFEK-----LRKDIGIVF 89
Cdd:PRK13638 9 FRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKrgllaLRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 90 QNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMlERADYEP-NALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:PRK13638 84 QDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA-QHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDLPFPI 247
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQPWLV 241
|
....*..
gi 613389154 248 KINQMLG 254
Cdd:PRK13638 242 KLHTQLG 248
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-231 |
7.76e-43 |
|
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: 145.83 E-value: 7.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03254 3 IEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIvkydvafgLENHAVPHDEMHR-RVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAS 155
Cdd:cd03254 82 VLQDT-FLFSGTI--------MENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFD 231
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
8-234 |
1.06e-42 |
|
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: 153.44 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG5265 358 VRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQnpDNQ-FVGSIvKYDVAFGleNHAVPHDEMHR--------------------RVSE-ALKqvdmleradyepnaLSG 145
Cdd:COG5265 437 VPQ--DTVlFNDTI-AYNIAYG--RPDASEEEVEAaaraaqihdfieslpdgydtRVGErGLK--------------LSG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 146 GQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
....*....
gi 613389154 226 ateifdHAE 234
Cdd:COG5265 576 ------HAE 578
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-230 |
1.96e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 148.56 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 lrKDIGIVFQN----P-----DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
Cdd:PRK09452 86 --RHVNTVFQSyalfPhmtvfEN----------VAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 152 AIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIY 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-229 |
2.79e-42 |
|
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: 144.50 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITD-DNFEKLRKDIGIVFQNP---------DN 94
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIARLGIGRTFQIPrlfpeltvlEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 175 PDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:cd03219 176 PEETEELAELIRELR-ERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEV 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
7-265 |
3.14e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 146.03 E-value: 3.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASFT---LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK--- 80
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 -LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIASVLA 158
Cdd:PRK13643 81 pVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAEELT 237
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEVDFLK 239
|
250 260
....*....|....*....|....*...
gi 613389154 238 TIGLDLPFPIKINQMLgHQTSFLTYEGL 265
Cdd:PRK13643 240 AHELGVPKATHFADQL-QKTGAVTFEKL 266
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-228 |
3.37e-42 |
|
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: 151.46 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDnQFVGSIvkydvafgLEN-----HAVPHDEMHrrvsEALKQVDMLERADYEPN-----------ALSGGQKQRV 151
Cdd:COG4987 414 VPQRPH-LFDTTL--------RENlrlarPDATDEELW----AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 152 AIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTATE 228
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-231 |
7.19e-42 |
|
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: 143.53 E-value: 7.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIvKYDVAFGLenhavpHDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIASV 156
Cdd:cd03251 81 VSQDV-FLFNDTV-AENIAYGR------PGATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 157 LALNPSVIILDEATSMLD---PDARQNLLDLVRKvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFD 231
Cdd:cd03251 153 LLKDPPILILDEATSALDtesERLVQAALERLMK-----NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-229 |
3.90e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 145.63 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL----RKDIGIVFQN----P---- 92
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELrelrRKKMSMVFQHfallPhrtv 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 -DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATS 171
Cdd:COG4175 123 lEN----------VAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 172 MLDPDAR---QN-LLDLVRKVKSehniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:COG4175 193 ALDPLIRremQDeLLELQAKLKK----TIVFITHDLDEALRlGDRIAIMKDGRIVQIGTPEEI 251
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-220 |
6.65e-41 |
|
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: 140.08 E-value: 6.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnFEKLRKDIGI 87
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQN----P-----DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:cd03301 77 VFQNyalyPhmtvyDN----------IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-229 |
7.89e-41 |
|
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: 140.33 E-value: 7.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIGI 87
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQnpdnqfvgsivkYDVAF----GLEN-------HAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASV 156
Cdd:cd03263 80 CPQ------------FDALFdeltVREHlrfyarlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-229 |
2.48e-40 |
|
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: 139.04 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIGI 87
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNP--DNQFVGsivkYDvafGLENHA----VPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNP 161
Cdd:cd03265 78 VFQDLsvDDELTG----WE---NLYIHArlygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-229 |
7.37e-40 |
|
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: 141.53 E-value: 7.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN----FEKLRKDIGIVFQNPdNQFVGSI 100
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpvelREVRRKKIGMVFQQF-ALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 VKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQN 180
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 613389154 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRiGDRIVIMKAGEIVQVGTPDEI 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-220 |
1.94e-39 |
|
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: 135.04 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNpDNQFVGSIvkydvafglenhavphdemhrrvsealkqvdmlerADyepNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:cd03246 81 LPQD-DELFSGSI-----------------------------------AE---NILSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVMNKGTV 220
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
8-225 |
5.67e-39 |
|
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: 143.94 E-value: 5.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNpDNQFVGSIvkydvafgLENHA----VPHDEmhrrVSEALKQVDMLERADYEP-----------NALSGGQKQRVA 152
Cdd:TIGR03797 532 VLQN-GRLMSGSI--------FENIAggapLTLDE----AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLL 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDAR----QNLLDLvrkvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQaivsESLERL--------KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGT 667
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-231 |
1.03e-38 |
|
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: 135.31 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQnpDNQFVGSIVKYDVAfgLENHAVPhdemHRRVSEALKQVDMLE-----RADYEP------NALSGGQKQRVAIASV 156
Cdd:cd03252 81 VLQ--ENVLFNRSIRDNIA--LADPGMS----MERVIEAAKLAGAHDfiselPEGYDTivgeqgAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFD 231
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-224 |
3.09e-38 |
|
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: 133.19 E-value: 3.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDaSFTLKdVSFNIPkGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNqTITDDNFEKL-----RKDIG 86
Cdd:cd03297 3 CVDIEKRLP-DFTLK-IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-TVLFDSRKKInlppqQRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNpdNQ-FVGSIVKYDVAFGLENHAvpHDEMHRRVSE--ALKQVDMLERAdyEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:cd03297 79 LVFQQ--YAlFPHLNVRENLAFGLKRKR--NREDRISVDEllDLLGLDHLLNR--YPAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-232 |
6.76e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 133.29 E-value: 6.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK--LRKD 84
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNpDNQFVGSIVKYDVAFG-LENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSV 163
Cdd:PRK09493 79 AGMVFQQ-FYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-229 |
8.16e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 133.29 E-value: 8.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKdIGIVFQNPdNQFVGSIVKYD 104
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-ARDRK-VGFVFQHY-ALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLE---NHAVPH-DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQN 180
Cdd:PRK10851 95 IAFGLTvlpRRERPNaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 613389154 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK10851 175 LRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-231 |
9.55e-37 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 137.55 E-value: 9.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRK 83
Cdd:TIGR00958 476 EGLIEFQDVSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPHDEM---------HRRVSEALKQVDMleRADYEPNALSGGQKQRVAIA 154
Cdd:TIGR00958 556 QVALVGQEP--VLFSGSVRENIAYGLTD--TPDEEImaaakaanaHDFIMEFPNGYDT--EVGEKGSQLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQnlldLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFD 231
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-228 |
1.10e-36 |
|
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: 129.86 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 2 EDKNSVIVFKNVSFQYQS-DASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT---DD 76
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTgAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 77 NFEKLRKD-IGIVFQNpdNQFVGSIVkydvafGLENHAVP-----HDEMHRRVSEALKQVDMLERADYEPNALSGGQKQR 150
Cdd:COG4181 83 ARARLRARhVGFVFQS--FQLLPTLT------ALENVMLPlelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 151 VAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATE 228
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-220 |
2.28e-36 |
|
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: 126.77 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKDIGIVFQnpdnqfvgsivky 103
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 104 dvafglenhavphdemhrrvsealkqvdmleradyepnaLSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLD 183
Cdd:cd03216 83 ---------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 613389154 184 LVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03216 124 VIRRLRAQ-GVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-224 |
2.33e-36 |
|
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: 128.46 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASftLKDVSFNIPKGQWtSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIGI 87
Cdd:cd03264 1 LQLENLTKRYGKKRA--LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQnpDNQFVGSIVKYD-VAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIIL 166
Cdd:cd03264 77 LPQ--EFGVYPNFTVREfLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 167 DEATSMLDPDARQNLLDLVRKVKSEHnITIISiTHDLSE-AMEADHVIVMNKGTVYKEG 224
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDR-IVILS-THIVEDvESLCNQVAVLNKGKLVFEG 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-229 |
3.10e-36 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 129.91 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPDN-----QFVGS 99
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTslnprQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 100 IVkyDVAFGLeNHAVPHDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDAR 178
Cdd:PRK15112 109 IL--DFPLRL-NTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 179 QNLLDLVRKVKSEHNITIISITHDLSeAME--ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLG-MMKhiSDQVLVMHQGEVVERGSTADV 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-215 |
3.87e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.99 E-value: 3.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKDIGIVFQNP---------DN 94
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELnlvpnlsvaEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGsivKYDVAFGLenhaVPHDEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:COG1129 100 IFLG---REPRRGGL----IDWRAMRRRARELLARLGL----DIDPDTpvgdLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVM 215
Cdd:COG1129 169 ASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEiADRVTVL 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-230 |
5.14e-36 |
|
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: 128.66 E-value: 5.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMigienvkSGEIF--YNN------QTITDD 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-------TGDLPptYGNdvrlfgERRGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 77 NFEKLRKDIGIV-----FQNPDNQFVGSIV---KYDVaFGLENHavPHDEMHRRVSEALKQVDMLERADYEPNALSGGQK 148
Cdd:COG1119 72 DVWELRKRIGLVspalqLRFPRDETVLDVVlsgFFDS-IGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 149 QRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTAT 227
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
...
gi 613389154 228 EIF 230
Cdd:COG1119 229 EVL 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-232 |
9.71e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 130.08 E-value: 9.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK---LRKDIGIVFQNP-----DNQF 96
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPygslnPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 97 VGSIvkydvafgLE-----NHAVPHDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK11308 111 VGQI--------LEeplliNTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSeAME--ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-232 |
1.09e-35 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 130.35 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnFEKLRKDIGI 87
Cdd:PRK11650 4 LKLQAVRKSYDGKT-QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQN----P-----DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEA---LKQVDMLERadyEPNALSGGQKQRVAIAS 155
Cdd:PRK11650 81 VFQNyalyPhmsvrEN----------MAYGLKIRGMPKAEIEERVAEAariLELEPLLDR---KPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 156 VLALNPSVIILDEATSMLDPDAR-QNLLDLvRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRvQMRLEI-QRLHRRLKTTSLYVTHDQVEAMTlADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-230 |
1.37e-35 |
|
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: 128.00 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDASF-------TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNF 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 79 EK---LRKDIGIVFQ------NPDnqfvgSIVKYDVAFGLENH-AVPHDEMHRRVSEALKQVDM-LERADYEPNALSGGQ 147
Cdd:TIGR02769 81 KQrraFRRDVQLVFQdspsavNPR-----MTVRQIIGEPLRHLtSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 148 KQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTA 226
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDV 235
|
....
gi 613389154 227 TEIF 230
Cdd:TIGR02769 236 AQLL 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
25-228 |
1.60e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.58 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPDNQF---VGSIv 101
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFpftVEEV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 kydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA------LNPSVIILDEATSMLDP 175
Cdd:PRK13548 97 ---VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613389154 176 DARQNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGTATE 228
Cdd:PRK13548 174 AHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-232 |
2.26e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 129.96 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnFEKLRKDIGIVFQNPdNQFVGS 99
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSY-ALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 100 IVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQ 179
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 180 NL----LDLVRKVksehNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK11607 187 RMqlevVDILERV----GVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-247 |
2.58e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 126.74 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG4604 2 IEIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQnpDNQFVGSI-VKYDVAFGlenhAVPH------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALN 160
Cdd:COG4604 80 LRQ--ENHINSRLtVRELVAFG----RFPYskgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDhAEELTTI 239
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIIT-PEVLSDI 232
|
....*...
gi 613389154 240 gLDLPFPI 247
Cdd:COG4604 233 -YDTDIEV 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
8-224 |
2.74e-35 |
|
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: 125.78 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIvKYDVAFGlenhAVPHDEmhRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIASV 156
Cdd:cd03245 83 VPQDV-TLFYGTL-RDNITLG----APLADD--ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-229 |
4.80e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 127.51 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLK---DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEI--FYNNQ----------- 71
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 72 TITDDNFEK-----------LRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDM----LERA 136
Cdd:PRK13651 83 VLEKLVIQKtrfkkikkikeIRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdesyLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 137 dyePNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVM 215
Cdd:PRK13651 163 ---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEwTKRTIFF 238
|
250
....*....|....
gi 613389154 216 NKGTVYKEGTATEI 229
Cdd:PRK13651 239 KDGKIIKDGDTYDI 252
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-220 |
2.77e-34 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 123.35 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDI 85
Cdd:cd03248 11 IVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQNPdNQFVGSIvKYDVAFGLENhaVPHDEM---------HRRVSEALKQVDmlERADYEPNALSGGQKQRVAIASV 156
Cdd:cd03248 91 SLVGQEP-VLFARSL-QDNIAYGLQS--CSFECVkeaaqkahaHSFISELASGYD--TEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTV 220
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-232 |
3.26e-34 |
|
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: 129.42 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKS----TIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRK---- 83
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQ------NPdnqfVGSIVKyDVAFGLENH-AVPHDEMHRRVSEALKQV---DMLERADYEPNALSGGQKQRVAI 153
Cdd:COG4172 93 RIAMIFQepmtslNP----LHTIGK-QIAEVLRLHrGLSGAAARARALELLERVgipDPERRLDAYPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTATEIFD 231
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGvvRRF-ADRVAVMRQGEIVEQGPTAELFA 246
|
.
gi 613389154 232 H 232
Cdd:COG4172 247 A 247
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-229 |
3.32e-34 |
|
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: 123.34 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLrkdigIVFQNPdNQFVGSIVKYD 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNY-SLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLE--NHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLL 182
Cdd:TIGR01184 75 IALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 613389154 183 DLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTATEI 229
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNGPAANIGQILEV 202
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-215 |
3.59e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 124.20 E-value: 3.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKlrk 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 diGIVFQN----P-----DNqfvgsivkydVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
Cdd:COG4525 79 --GVVFQKdallPwlnvlDN----------VAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVM 215
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALfLATRLVVM 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-215 |
4.02e-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: 128.94 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDI 85
Cdd:TIGR02857 320 SSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQNPdnQFVGSIVKYDVAFGlENHAVPHDemhrrVSEALKQVDMLE-----------RADYEPNALSGGQKQRVAIA 154
Cdd:TIGR02857 399 AWVPQHP--FLFAGTIAENIRLA-RPDASDAE-----IREALERAGLDEfvaalpqgldtPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVM 215
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
25-224 |
4.64e-34 |
|
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: 122.33 E-value: 4.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQtITDDNFEKLRKdigivfqnpdnqfVGSIVKYD 104
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK-SYQKNIEALRR-------------IGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFG-------LENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDA 177
Cdd:cd03268 82 GFYPnltarenLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613389154 178 RQNLLDLVRKVKSEhNITIISITHDLSEaME--ADHVIVMNKGTVYKEG 224
Cdd:cd03268 162 IKELRELILSLRDQ-GITVLISSHLLSE-IQkvADRIGIINKGKLIEEG 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-225 |
5.15e-34 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 129.45 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PRK10790 341 IDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdnqfvgsIVKYDVAFGleNHAVPHDEMHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIASV 156
Cdd:PRK10790 420 VQQDP-------VVLADTFLA--NVTLGRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 157 LALNPSVIILDEATSMLDP---DARQNLLDLVRKvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
Cdd:PRK10790 491 LVQTPQILILDEATANIDSgteQAIQQALAAVRE-----HTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-233 |
5.94e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 123.64 E-value: 5.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYQSDASF-------TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK--- 80
Cdd:PRK10419 7 SGLSHHYAHGGLSgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQ------NPdNQFVGSIVKYDVafgleNHAVPHDEMHR--RVSEALKQVDM-LERADYEPNALSGGQKQRV 151
Cdd:PRK10419 87 FRRDIQMVFQdsisavNP-RKTVREIIREPL-----RHLLSLDKAERlaRASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 152 AIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI- 229
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKl 240
|
....*
gi 613389154 230 -FDHA 233
Cdd:PRK10419 241 tFSSP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-232 |
1.21e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 128.21 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIVKyDVAFGLENHAVPHD-EMHRRVSEALKQVDMLERA-DY---EPNA-LSGGQKQRVAIASVLALNP 161
Cdd:PRK11176 422 VSQNV-HLFNDTIAN-NIAYARTEQYSREQiEEAARMAYAMDFINKMDNGlDTvigENGVlLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 162 SVIILDEATSMLDPD---ARQNLLDLVRKvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK11176 500 PILILDEATSALDTEserAIQAALDELQK-----NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-244 |
1.29e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.48 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnfekLRKDIGI 87
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNP---------DNqfvgsivkydVAFGLENHAVPhdemhrRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA 158
Cdd:PRK11247 86 MFQDArllpwkkviDN----------VGLGLKGQWRD------AALQALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGtvykegtateifdhaeelt 237
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAmADRVLLIEEG------------------- 210
|
....*..
gi 613389154 238 TIGLDLP 244
Cdd:PRK11247 211 KIGLDLT 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-230 |
1.78e-33 |
|
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: 124.44 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 21 ASFTLkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNF------EKLRkdIGIVFQNP-- 92
Cdd:COG4148 12 GGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgiflppHRRR--IGYVFQEArl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 -------DNqfvgsivkydVAFGLenHAVPHDEMHRRVSEAlkqVDM------LERAdyePNALSGGQKQRVAIASVLAL 159
Cdd:COG4148 89 fphlsvrGN----------LLYGR--KRAPRAERRISFDEV---VELlgighlLDRR---PATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-230 |
2.40e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 121.76 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPDNQF---VGSIV 101
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAFpftVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 kydvAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLA-------LNPSVIILDEATSMLD 174
Cdd:COG4559 97 ----ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 175 PDARQNLLDLVRKVkSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGTATEIF 230
Cdd:COG4559 173 LAHQHAVLRLARQL-ARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-224 |
2.54e-33 |
|
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: 120.68 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 13 VSFQYQsDASFTLkDVSFniPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITddNFEKLRKDIGIVFQNp 92
Cdd:cd03298 6 IRFSYG-EQPMHF-DLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 DNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSM 172
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-230 |
4.11e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 121.27 E-value: 4.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PRK11231 3 LRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQN---PDnqfvGSIVKYDVAFGLEnhavPH--------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASV 156
Cdd:PRK11231 81 LPQHhltPE----GITVRELVAYGRS----PWlslwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-229 |
5.04e-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: 119.85 E-value: 5.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITD-DNFEKLRKDIGIVFQNPDNqfvgsivky 103
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHERARAGIGYVPEGRRI--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 104 dvaFG----LEN-----HAVPHDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:cd03224 87 ---FPeltvEENlllgaYARRRAKRKARLERVYELFPRLkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 174 DPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:cd03224 164 APKIVEEIFEAIRELRDE-GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-232 |
5.43e-33 |
|
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: 126.37 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIVKyDVAFGlenhaVPHDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIASV 156
Cdd:TIGR02203 411 VSQDV-VLFNDTIAN-NIAYG-----RTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 157 LALNPSVIILDEATSMLDPDAR---QNLLDLVRKvksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESErlvQAALERLMQ-----GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-235 |
5.84e-33 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 120.56 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEN--VKSGEIFYNNQTITD-DNFEKLRKDIGIVFQNPD-------N 94
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILElSPDERARAGIFLAFQYPVeipgvsvS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIVKydvAFGLENHAVPhdEMHRRVSEALKQV----DMLERadyEPNA-LSGGQKQRVAIASVLALNPSVIILDEA 169
Cdd:COG0396 96 NFLRTALN---ARRGEELSAR--EFLKLLKEKMKELgldeDFLDR---YVNEgFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 170 TSMLDPDARQNLLDLVRKVKSEHNiTIISITH--DLSEAMEADHVIVMNKGTVYKEGTAtEIFDHAEE 235
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSPDR-GILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALELEE 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-238 |
1.94e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 119.47 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-------- 77
Cdd:PRK11264 2 SAIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 78 FEKLRKDIGIVFQN----PDNQFVGSIVKYDVAFGLEnhavPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
Cdd:PRK11264 80 IRQLRQHVGFVFQNfnlfPHRTVLENIIEGPVIVKGE----PKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
....*.
gi 613389154 233 AEELTT 238
Cdd:PRK11264 235 PQQPRT 240
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-232 |
2.87e-32 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 119.13 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT-------------DDNFEKLRKDIGIVFQN 91
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpadRRQLQRIRTRLGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 pdnqfvgsivkydvaFGLENH---------------AVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASV 156
Cdd:COG4598 104 ---------------FNLWSHmtvlenvieapvhvlGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDvSSHVVFLHQGRIEEQGPPAEVFGN 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-232 |
4.77e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 121.68 E-value: 4.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 22 SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNN---QTITDDNFEKLR-KDIGIVFQNPDNQFV 97
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRrKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 98 GSIVKyDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDA 177
Cdd:PRK10070 121 MTVLD-NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-225 |
5.09e-32 |
|
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: 117.21 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDNqFVGSIvkydvAFGLENHAVPHDEMhrrVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIASV 156
Cdd:cd03244 83 IPQDPVL-FSGTI-----RSNLDPFGEYSDEE---LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-238 |
7.94e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.89 E-value: 7.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENvKSGEIFYNNQTITDDNFEKL---RKDIGIVFQNPDNQF----- 96
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSSLnprln 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 97 VGSIVkydvAFGLENHAvPH---DEMHRRVSEALKQV--DMLERADYePNALSGGQKQRVAIASVLALNPSVIILDEATS 171
Cdd:PRK15134 381 VLQII----EEGLRVHQ-PTlsaAQREQQVIAVMEEVglDPETRHRY-PAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTATEIFDHAEELTT 238
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHqVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
25-215 |
1.14e-31 |
|
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: 116.04 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDnFEKLRKDIGIVFQNP---------DNq 95
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLAYLGHADglkpeltvrEN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 96 fvgsivkydVAFGLENHAVPHDEMhrRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDP 175
Cdd:COG4133 96 ---------LRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 613389154 176 DARQNLLDLVRKVKSEHNITIISiTHDLSEAmEADHVIVM 215
Cdd:COG4133 165 AGVALLAELIAAHLARGGAVLLT-THQPLEL-AAARVLDL 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-247 |
1.43e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 122.66 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQ---TITDDNFEKLRKDIGIVFQNP-----DNQF 96
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasldPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 97 VGsivkYDVAFGLENHAVPH-DEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:PRK10261 420 VG----DSIMEPLRVHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTATEIFDHAEELTTIGLDLPFPI 247
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-229 |
2.55e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 121.61 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PRK13657 335 VEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNP--------DNQFVGsivKYDVAfglenhavpHDEMhRRVSEALKQVDMLERAD--YEPNA------LSGGQKQRV 151
Cdd:PRK13657 414 VFQDAglfnrsieDNIRVG---RPDAT---------DEEM-RAAAERAQAHDFIERKPdgYDTVVgergrqLSGGERQRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 152 AIASVLALNPSVIILDEATSMLD--PDAR-QNLLDLVRkvkseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATE 228
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDveTEAKvKAALDELM-----KGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555
|
.
gi 613389154 229 I 229
Cdd:PRK13657 556 L 556
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-215 |
3.26e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.89 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI--ENVK-SGEIFYNNQTITDDNFEKLRkdIGIVFQNP---DNQFVG 98
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRR--IGILFQDDllfPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SivkyDVAFGLENhAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDAR 178
Cdd:COG4136 95 E----NLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 613389154 179 QNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVM 215
Cdd:COG4136 170 AQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-232 |
8.84e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.72 E-value: 8.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEI------FYNNQTITDDNFEKL 81
Cdd:COG4161 3 IQLKNINCFYGSHQA--LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqFDFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDIGIVFQNpdnqfvgsivkYdvafglenHAVPH-------------------DEMHRRVSEALKQVDMLERADYEPNA 142
Cdd:COG4161 81 RQKVGMVFQQ-----------Y--------NLWPHltvmenlieapckvlglskEQAREKAMKLLARLRLTDKADRFPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 143 LSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVY 221
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
250
....*....|.
gi 613389154 222 KEGTAtEIFDH 232
Cdd:COG4161 221 EQGDA-SHFTQ 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-230 |
1.36e-30 |
|
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: 119.47 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDnQFVGSIVkydvafglENHA---VPHDEmhrRVSEALKQV---DMLER-AD-YE------PNALSGGQKQRVAI 153
Cdd:COG4618 411 LPQDVE-LFDGTIA--------ENIArfgDADPE---KVVAAAKLAgvhEMILRlPDgYDtrigegGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIF 230
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-230 |
4.43e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.90 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnFEKLRKDIGIVFQnpdnqfvgSIVKY-- 103
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMVFQ--------SYALYph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 104 -----DVAFGLENHAVPHDEMHRRV---SEALKQVDMLERadyEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDP 175
Cdd:PRK11000 90 lsvaeNMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDR---KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK11000 167 ALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-229 |
6.56e-30 |
|
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: 112.23 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKDIGIVFQNPDnqfvg 98
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGRE----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SIVKYDVAFGLENHAVPHDEMHRRVSE-------ALKqvDMLER--ADyepnaLSGGQKQRVAIASVLALNPSVIILDEA 169
Cdd:TIGR03410 86 IFPRLTVEENLLTGLAALPRRSRKIPDeiyelfpVLK--EMLGRrgGD-----LSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-232 |
1.25e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.65 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKN--VSFQYQSDASF------TLK---DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYN 69
Cdd:PRK15079 2 TEGKKVLLEVADlkVHFDIKDGKQWfwqppkTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 70 NQTIT---DDNFEKLRKDIGIVFQNP-----DNQFVGSIVkydvAFGLENH--AVPHDEMHRRVSEALKQVDMLERA-DY 138
Cdd:PRK15079 82 GKDLLgmkDDEWRAVRSDIQMIFQDPlaslnPRMTIGEII----AEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLiNR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 139 EPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNK 217
Cdd:PRK15079 158 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYL 237
|
250
....*....|....*
gi 613389154 218 GTVYKEGTATEIFDH 232
Cdd:PRK15079 238 GHAVELGTYDEVYHN 252
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-229 |
1.29e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.89 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYqsdASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfeklRKDI 85
Cdd:COG4152 1 MLELKGLTKRF---GDKTaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVfqnPD------NQFVGSIVKYdvaFGlENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLAL 159
Cdd:COG4152 74 GYL---PEerglypKMKVGEQLVY---LA-RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-227 |
1.78e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 111.06 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQ---TITDDNFEKLR-KDI 85
Cdd:PRK11629 10 NLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQN----PDnqFVGsivkydvafgLENHAVP-------HDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
Cdd:PRK11629 90 GFIYQFhhllPD--FTA----------LENVAMPlligkkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTAT 227
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-230 |
3.26e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.91 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLM---IGIENVK---SGEIFYNNQTITDDNFEKLRKDIGIVFQNPdNQFVG 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQP-NPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SIVKYDVAFGLENHAVPHD-EMHRRVSEALKQV----DMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 174 DPDARQNLLDLVRKVKSEhnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-237 |
3.37e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.77 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLM-----IGIENVKSGEIFYNNQTITDDNFEK 80
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPDNQFVGSIVKyDVAFGLE-NHAVPHD-EMHRRVSEALKQVDMLE----RADYEPNALSGGQKQRVAIA 154
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFE-NVALGLKlNRLVKSKkELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHA 233
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVFTNP 236
|
....*
gi 613389154 234 E-ELT 237
Cdd:PRK14247 237 RhELT 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-220 |
4.82e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK-LRKDIGIVFQNP---------DN 94
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFmlvpnltvaEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 qfvgsivkydVAFGLENHA---VPHDEMHRRVSEALKQ----VDmleradyePNA----LSGGQKQRVAIASVLALNPSV 163
Cdd:COG3845 101 ----------IVLGLEPTKggrLDRKAARARIRELSERygldVD--------PDAkvedLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-229 |
6.42e-29 |
|
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: 112.51 E-value: 6.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 21 ASFTLkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKL-----RKDIGIVFQNPdNQ 95
Cdd:TIGR02142 10 GDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSR-KGIflppeKRRIGYVFQEA-RL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 96 FVGSIVKYDVAFGLENHAVPHDEMH-RRVSEALKQVDMLERAdyePNALSGGQKQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:TIGR02142 87 FPHLSVRGNLRYGMKRARPSERRISfERVIELLGIGHLLGRL---PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 175 PDARQNLLDLVRKVKSEHNITIISITHDLSE-AMEADHVIVMNKGTVYKEGTATEI 229
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-203 |
1.98e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.04 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT---DDNFEKLRK 83
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQnpDNQFVGSIVKYD-VAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPS 162
Cdd:PRK10908 80 QIGMIFQ--DHHLLMDRTVYDnVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613389154 163 VIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDL 203
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDI 197
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-227 |
2.45e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEI------FYNNQTITDDNFEKL 81
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDIGIVFQnpdnQFvgsivkydvafglenHAVPH-------------------DEMHRRVSEALKQVDMLERADYEPNA 142
Cdd:PRK11124 81 RRNVGMVFQ----QY---------------NLWPHltvqqnlieapcrvlglskDQALARAEKLLERLRLKPYADRFPLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 143 LSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVY 221
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
....*.
gi 613389154 222 KEGTAT 227
Cdd:PRK11124 221 EQGDAS 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
25-224 |
4.80e-28 |
|
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: 107.07 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKdIGIVfqnPDNQFVgsivkYD 104
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFV---SDSTGL-----YD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLEN-------HAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDA 177
Cdd:cd03266 92 RLTARENleyfaglYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 613389154 178 RQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
Cdd:cd03266 172 TRALREFIRQLRALGK-CILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-229 |
5.48e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.15 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPDNQfvGSI-VKYD 104
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTP--GDItVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGlenhAVPHDEMHRR--------VSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPD 176
Cdd:PRK10253 102 VARG----RYPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613389154 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEI 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-231 |
8.41e-28 |
|
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: 112.14 E-value: 8.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKD 84
Cdd:TIGR01193 471 NGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPdNQFVGSIVKYDVAFGLENhaVPHDEMHRRVSEALKQVDMLE-------RADYEPNALSGGQKQRVAIASVL 157
Cdd:TIGR01193 550 INYLPQEP-YIFSGSILENLLLGAKEN--VSQDEIWAACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFD 231
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-215 |
1.02e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqTITDDnfeklrKDIGIVFQNP--DNQFVGSiVK 102
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----RRAGG------ARVAYVPQRSevPDSLPLT-VR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVAFGLENHAVP---HD-EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDAR 178
Cdd:NF040873 76 DLVAMGRWARRGLwrrLTrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 613389154 179 QNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVM 215
Cdd:NF040873 156 ERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-230 |
1.12e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 108.68 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEN----VKSGEIFYNNQTITDDNFEKLRK----DIGIVFQNPDNQFVGS 99
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 100 -IVKYDVAFGLENH-AVPHDEMHRRVSEALKQV---DMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:PRK11022 106 yTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIF 242
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-241 |
1.72e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.82 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 29 SFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITddNFEKLRKDIGIVFQNpDNQFVGSIVKYDVAFG 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSMLFQE-NNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 109 LENHAVPHDEMHRRVSEALKQV---DMLERAdyePNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLV 185
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQMgieDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 186 RKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG-TATEIFDHAEELTTIGL 241
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGpTDELLSGKASASALLGI 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-215 |
2.61e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.18 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQyqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYL--AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPdnQFVGSIVkYDvafgleNHAVPHDEMHRRVSEAlKQVDMLER-------ADYEPNALSGGQKQRVAI 153
Cdd:PRK10247 79 YRQQVSYCAQTP--TLFGDTV-YD------NLIFPWQIRNQQPDPA-IFLDDLERfalpdtiLTKNIAELSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVM 215
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-219 |
3.08e-27 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 104.47 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSD---ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQtitddnfeklrkd 84
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPDNQFvGSIvKYDVAFGLenhavPHD-EMHRRVSEA--LKQ-VDMLERADyepN--------ALSGGQKQRVA 152
Cdd:cd03250 68 IAYVSQEPWIQN-GTI-RENILFGK-----PFDeERYEKVIKAcaLEPdLEILPDGD---LteigekgiNLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGT 219
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-206 |
4.32e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 105.63 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAK----LMIGIENVK-SGEIFYNNQTITDDNFE 79
Cdd:PRK14243 8 ETVLRTENLNVYYGS--FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrLNDLIPGFRvEGKVTFHGKNLYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 80 --KLRKDIGIVFQNPdNQFVGSIvkYD-VAFGLENHAVPHDeMHRRVSEALKQV-------DMLERADYepnALSGGQKQ 149
Cdd:PRK14243 86 pvEVRRRIGMVFQKP-NPFPKSI--YDnIAYGARINGYKGD-MDELVERSLRQAalwdevkDKLKQSGL---SLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 150 RVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA 206
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQA 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-225 |
5.17e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.53 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDnQFVGSIvKYDVAFGLENhavPHDEmhrRVSEALKQV---DMLEraDYEP-NA--------LSGGQKQRVAIAS 155
Cdd:PRK11160 419 VSQRVH-LFSATL-RDNLLLAAPN---ASDE---ALIEVLQQVgleKLLE--DDKGlNAwlgeggrqLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSeAMEA-DHVIVMNKGTVYKEGT 225
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQfDRICVMDNGQIIEQGT 556
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-229 |
7.16e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.87 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 18 QSDASFTLKDVSFNI-------------PKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKD 84
Cdd:PRK10575 7 HSDTTFALRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQN-PDNQfvGSIVKYDVAFG-------LENHAVphdEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASV 156
Cdd:PRK10575 87 VAYLPQQlPAAE--GMTVRELVAIGrypwhgaLGRFGA---ADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-207 |
7.63e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 104.78 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKlrkdiGIVFQN 91
Cdd:PRK11248 6 HLYADYGGKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 pDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATS 171
Cdd:PRK11248 79 -EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 613389154 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM 207
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAV 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-235 |
8.75e-27 |
|
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: 102.99 E-value: 8.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEN--VKSGEIFYNNQTITD-DNFEKLRKDIGIVFQNPdnqfvgsiv 101
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDlPPEERARLGIFLAFQYP--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 kydvafgLENHAVphdemhrRVSEALKQVDMleradyepnALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNL 181
Cdd:cd03217 87 -------PEIPGV-------KNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 182 LDLVRKVKSEHNITIIsITH--DLSEAMEADHVIVMNKGTVYKEGTAtEIFDHAEE 235
Cdd:cd03217 144 AEVINKLREEGKSVLI-ITHyqRLLDYIKPDRVHVLYDGRIVKSGDK-ELALEIEK 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
6-230 |
1.19e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 104.58 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITddnfEKLRKD- 84
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPDNQFVGSIVKYDVAF-------GLENHAVPHDemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVL 157
Cdd:PRK15056 80 VAYVPQSEEVDWSFPVLVEDVVMmgryghmGWLRRAKKRD--RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYTVMVKGTVLASGPTETTF 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
25-218 |
1.46e-26 |
|
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: 102.74 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfeklRKDIGIVfqnPD------NQFVG 98
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL---PEerglypKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SIVKYdvaFGlENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDAR 178
Cdd:cd03269 89 DQLVY---LA-QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613389154 179 QNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
Cdd:cd03269 165 ELLKDVIRELARA-GKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-234 |
1.98e-26 |
|
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: 103.14 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKDIGIVfqnPDNQFVgsivky 103
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYV---PEGRRI------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 104 dvaFG----LENHAVPhdEMHRRVSEALKQVdmLERAdYE--PN----------ALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:COG0410 90 ---FPsltvEENLLLG--AYARRDRAEVRAD--LERV-YElfPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAE 234
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-224 |
3.73e-26 |
|
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: 100.85 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIGI 87
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIvkydvafgLENhavphdeMHRRvsealkqvdmleradyepnaLSGGQKQRVAIASVLALNPSVIILD 167
Cdd:cd03247 80 LNQRP-YLFDTTL--------RNN-------LGRR--------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-220 |
5.21e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.47 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPdnqFVGSivkyd 104
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDP---MMGT----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 vAFGL---EN--------------HAVPHDEMHRrVSEALKQVDM-LE-RADYEPNALSGGQKQrvAIASVLAL--NPSV 163
Cdd:COG1101 94 -APSMtieENlalayrrgkrrglrRGLTKKRREL-FRELLATLGLgLEnRLDTKVGLLSGGQRQ--ALSLLMATltKPKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDyGNRLIMMHEGRI 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-234 |
6.65e-26 |
|
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: 101.47 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKDIGIVFQNPdNQFVGSIVKY 103
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEA-SIFRKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 104 DVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLD 183
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 184 LVRKVKsEHNITIIsIT-HDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAE 234
Cdd:cd03218 175 IIKILK-DRGIGVL-ITdHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
25-219 |
7.68e-26 |
|
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: 101.36 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQ-------TITDDNFEKLRKD-IGIVfqnpdNQF 96
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaQASPREILALRRRtIGYV-----SQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 97 ------VGSIvkyD-VAFGLENHAVPHDEMHRRVSEALKQVDMLER-ADYEPNALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:COG4778 102 lrviprVSAL---DvVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 169 ATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLsEAME--ADHVIVMNKGT 219
Cdd:COG4778 179 PTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE-EVREavADRVVDVTPFS 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-206 |
8.14e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLM-----IGIENVKSGEIFYNNQTI---TDDNFEkLRKDIGIVFQNPdNQ 95
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQP-NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 96 FVGSIVKyDVAFGLENHAVPHDE-MHRRVSEALKQVDMLE----RADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK14239 98 FPMSIYE-NVVYGLRLKGIKDKQvLDEAVEKSLKGASIWDevkdRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 613389154 171 SMLDPDARQNLLDLVRKVKseHNITIISITHDLSEA 206
Cdd:PRK14239 177 SALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQA 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-205 |
1.67e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 101.27 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKS-----GEIFYNNQTITDD--NFEK 80
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNPdNQFVGSIvkYD-VAFGLENHA-VPHDEMHRRVSEALKQVDMLERADYEPNA----LSGGQKQRVAIA 154
Cdd:PRK14258 86 LRRQVSMVHPKP-NLFPMSV--YDnVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE 205
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQ 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-237 |
1.79e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.07 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAK-----LMIGIENVKSGE--IFYNNQTITDDNFEKLRKDIGIVFQNPdNQFV 97
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEvrLFGRNIYSPDVDPIEVRREVGMVFQYP-NPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 98 GSIVKYDVAFGLE--NHAVPHDEMHRRVSEALKQVDMLERA-----DYePNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK14267 99 HLTIYDNVAIGVKlnGLVKSKKELDERVEWALKKAALWDEVkdrlnDY-PSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHAE-ELT 237
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFENPEhELT 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-255 |
1.85e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.94 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 3 DKNSVIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIA-KLMIGIE----NVKSGEIFY---NNQT 72
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTAlALMRLLEqaggLVQCDKMLLrrrSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 73 I-----TDDNFEKLR-KDIGIVFQNPDNQF-----VGSivkyDVAFGLENH-AVPHDEMHRRVSEALKQV------DMLE 134
Cdd:PRK10261 88 IelseqSAAQMRHVRgADMAMIFQEPMTSLnpvftVGE----QIAESIRLHqGASREEAMVEAKRMLDQVripeaqTILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 135 RAdyePNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVI 213
Cdd:PRK10261 164 RY---PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 613389154 214 VMNKGTVYKEGTATEIFDHAEELTTIGLDLPFPiKINQMLGH 255
Cdd:PRK10261 241 VMYQGEAVETGSVEQIFHAPQHPYTRALLAAVP-QLGAMKGL 281
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-229 |
1.94e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.38 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK 80
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFD--NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 L---RKDIGIVFQNpDNQFVGSIVKYDVAFGLENHA-VPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASV 156
Cdd:PRK11831 79 LytvRKRMSMLFQS-GALFTDMNVFDNVAYPLREHTqLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-220 |
2.55e-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: 99.16 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDASFT----LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IENVK-SGEIFYNNQTITDDNFe 79
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGvSGEVLINGRPLDKRSF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 80 klRKDIGIVFQnpdnqfvgsivkydvafglENHAVPHDEmhrrVSEALKQVDMLERadyepnaLSGGQKQRVAIASVLAL 159
Cdd:cd03213 81 --RKIIGYVPQ-------------------DDILHPTLT----VRETLMFAAKLRG-------LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAMEA--DHVIVMNKGTV 220
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-220 |
3.40e-25 |
|
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: 99.02 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIvkydvafglENHAVPHDEM-HRRVSEALkqvdmleRADYEPNALSGGQKQRVAIASVLALNPSVIIL 166
Cdd:cd03369 87 IPQDP-TLFSGTI---------RSNLDPFDEYsDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613389154 167 DEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTV 220
Cdd:cd03369 150 DEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-241 |
5.60e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 101.34 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI---ENVKSGEIFYNNQTI---TDDNFEKLR-KD 84
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREIlnlPEKELNKLRaEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPdnqfVGSIVKY-DVAFGLENHAVPHDEMHRrvSEALKQ-VDMLE---------RADYEPNALSGGQKQRVAI 153
Cdd:PRK09473 99 ISMIFQDP----MTSLNPYmRVGEQLMEVLMLHKGMSK--AEAFEEsVRMLDavkmpearkRMKMYPHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
....*....
gi 613389154 233 AEELTTIGL 241
Cdd:PRK09473 253 PSHPYSIGL 261
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-230 |
1.15e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.89 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTIT-------------DDNFEKLRKDIGIVFQN 91
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 PDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERA-DYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK10619 101 FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 171 SMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK10619 181 SALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-203 |
2.68e-24 |
|
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: 101.28 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:TIGR02868 335 LELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdnQFVGSIVKYDVAFGLENhaVPHDEMhrrvSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIASV 156
Cdd:TIGR02868 414 CAQDA--HLFDTTVRENLRLARPD--ATDEEL----WAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDL 203
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-224 |
2.13e-23 |
|
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: 95.09 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQtITDDNFEKLRKDIGIVFQNpDNQFVGSIvkyD 104
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFGQ-KTQLWWDL---P 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLENHA----VPHDEMHRRVSEAlkqVDMLERAD--YEP-NALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDA 177
Cdd:cd03267 112 VIDSFYLLAaiydLPPARFKKRLDEL---SELLDLEEllDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613389154 178 RQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEG 224
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKdiEAL-ARRVLVIDKGRLLYDG 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-232 |
2.31e-23 |
|
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: 98.96 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQn 91
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQ- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 pDNQ-FVGSIVKYDVAFGlENhAVPhdemhRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIASVLAL 159
Cdd:TIGR01842 400 -DVElFPGTVAENIARFG-EN-ADP-----EKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-236 |
3.28e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 98.51 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PRK10522 323 LELRNVTFAYQ-DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNpdnqfvgsIVKYDVAFGLENHAVPHDemhrRVSEALKQVDMLERADYEPN-----ALSGGQKQRVAIASVLALNPS 162
Cdd:PRK10522 402 VFTD--------FHLFDQLLGPEGKPANPA----LVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 163 VIILDEATSMLDPDAR----QNLLDLVRkvksEHNITIISITHDLSEAMEADHVIVMNKGTVykegtaTEIFDHAEEL 236
Cdd:PRK10522 470 ILLLDEWAADQDPHFRrefyQVLLPLLQ----EMGKTIFAISHDDHYFIHADRLLEMRNGQL------SELTGEERDA 537
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-225 |
4.68e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 97.86 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 14 SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPd 93
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 94 nqFVGS-IVKYDVAFGLENH-----------AVPHDEMHRRVSEALKQVDmlERAdyepNALSGGQKQRVAIASVLALNP 161
Cdd:PRK10789 399 --FLFSdTVANNIALGRPDAtqqeiehvarlASVHDDILRLPQGYDTEVG--ERG----VMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 162 SVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISiTHDLSEAMEADHVIVMNKGTVYKEGT 225
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIIS-AHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-223 |
1.23e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.92 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFE---KLR-KDIGIVFQnpdnqfvgSI 100
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQ--------SF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 VKYDVAFGLENHAVP-------HDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:PRK10584 98 MLIPTLNALENVELPallrgesSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 613389154 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-231 |
1.54e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 93.07 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL---------RKDIGIVFQNPDNQF- 96
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPRDGLr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 97 --V---GSIVKYDVAFGlENHavpHDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK11701 104 mqVsagGNIGERLMAVG-ARH---YGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTATEIFD 231
Cdd:PRK11701 180 GGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVArLLAHRLLVMKQGRVVESGLTDQVLD 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-234 |
1.58e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.62 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENV-----KSGEIFYNNQTITD-DNFEKLRKDIGIVFQNPdNQFVG 98
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNyRDVLEFRRRVGMLFQRP-NPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SIVKyDVAFGLENHA-VPHDEMHRRVSEALKQVDMLE----RADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:PRK14271 116 SIMD-NVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 174 DPDARQNLLDLVRKVKSEhnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFD---HAE 234
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSspkHAE 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
25-229 |
2.97e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.01 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQwtsIV---GHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKDIGIVFQNPdnqfvgSI 100
Cdd:COG1137 19 VKDVSLEVNQGE---IVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHKRARLGIGYLPQEA------SI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 vkydvaFG-----------LENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEA 169
Cdd:COG1137 90 ------FRkltvednilavLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 170 TSMLDPDARQNLLDLVRKVKsEHNITIIsIT-HDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLK-ERGIGVL-ITdHNVRETLGiCDRAYIISEGKVLAEGTPEEI 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-220 |
5.15e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 91.18 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEN--VKSGEIFYNNQTITDDNFeklRKDIGIVFQnpDNQFVGSI- 100
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGggTTSGQILFNGQPRKPDQF---QKCVAYVRQ--DDILLPGLt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 VKYDVAFglenhaVPHDEMHRRVSEALKQV---DMLER-------ADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:cd03234 98 VRETLTY------TAILRLPRKSSDAIRKKrveDVLLRdlaltriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTV 220
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLfDRILLLSSGEI 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-237 |
6.87e-22 |
|
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: 94.48 E-value: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQYQSDASFTLK---DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynNQTITDD- 76
Cdd:TIGR03269 273 VEVGEPIIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV---NVRVGDEw 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 77 -NFEKLRKD--------IGIVFQN----PDNQFVGSIVKydvAFGLEnhaVPHDEMHRRVSEALKQVDMLERA-----DY 138
Cdd:TIGR03269 350 vDMTKPGPDgrgrakryIGILHQEydlyPHRTVLDNLTE---AIGLE---LPDELARMKAVITLKMVGFDEEKaeeilDK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 139 EPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNK 217
Cdd:TIGR03269 424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRD 503
|
250 260
....*....|....*....|
gi 613389154 218 GTVYKEGTATEIFdhaEELT 237
Cdd:TIGR03269 504 GKIVKIGDPEEIV---EELT 520
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-219 |
8.14e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.49 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQyQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFynnqtitddnfekLRKDIGI 87
Cdd:COG4178 363 LALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-------------RPAGARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VF--QNP-------DNQfvgsivkydVAFGLENHAVPHDEMHrrvsEALKQV---DMLERADYE---PNALSGGQKQRVA 152
Cdd:COG4178 429 LFlpQRPylplgtlREA---------LLYPATAEAFSDAELR----EALEAVglgHLAERLDEEadwDQVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGT 219
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-220 |
1.12e-21 |
|
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: 89.03 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKdIGIVFqnpdnqfvgsivkyd 104
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR-AGIAY--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 vafglenhaVPHDemhrRVSEALkqvdMLERADYE----PNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQN 180
Cdd:cd03215 80 ---------VPED----RKREGL----VLDLSVAEnialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613389154 181 LLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:cd03215 143 IYRLIRELADA-GKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-218 |
1.24e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI--ENVKSGEIFYNNQTITDDNF-EKLRKDIGIVFQN---------P 92
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIrDTERAGIAIIHQElalvkelsvL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 DNQFVGS-IVKydvaFGLENHavphDEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIASVLALNPSVIILD 167
Cdd:PRK13549 101 ENIFLGNeITP----GGIMDY----DAMYLRAQKLLAQLKL----DINPATpvgnLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKG 218
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
11-224 |
1.60e-21 |
|
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: 89.77 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITddnfEKLRKDIGIVFQ 90
Cdd:TIGR03740 4 KNLSKRFGKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT----RKDLHKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 91 NPdnQFVGSIVKYDvafGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:TIGR03740 78 SP--PLYENLTARE---NLKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVqQLADHIGIISEGVLGYQG 206
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-220 |
3.25e-21 |
|
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: 92.55 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQS---DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKD 84
Cdd:COG4615 328 LELRGVTYRYPGedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQnpDN-QFvgsivkyDVAFGLENHAVPhdemhRRVSEALKQVDMLERADYEPN-----ALSGGQKQRVAIASVLA 158
Cdd:COG4615 408 FSAVFS--DFhLF-------DRLLGLDGEADP-----ARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 159 LNPSVIILDEATSMLDPDAR----QNLL-DLVRKVKsehniTIISITHD-----LseameADHVIVMNKGTV 220
Cdd:COG4615 474 EDRPILVFDEWAADQDPEFRrvfyTELLpELKARGK-----TVIAISHDdryfdL-----ADRVLKMDYGKL 535
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-230 |
6.33e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 13 VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIA----KLMIGIENV-KSGEIFYNNQTITDDNFEKLRK---- 83
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlsilRLLPSPPVVyPSGDIRFHGESLLHASEQTLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQNPdnqfvgsIVKYDVAFGLENHAVPHDEMHRRVS-EALKQ--VDMLER----------ADYePNALSGGQKQR 150
Cdd:PRK15134 93 KIAMIFQEP-------MVSLNPLHTLEKQLYEVLSLHRGMRrEAARGeiLNCLDRvgirqaakrlTDY-PHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 151 VAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
.
gi 613389154 230 F 230
Cdd:PRK15134 245 F 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-218 |
1.30e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQ---TITDDNFEKLRKD- 84
Cdd:PRK10535 8 KDIRRSYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADALAQLRREh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQnpdnqfvgsivKYDVAFGL---ENHAVP-------HDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
Cdd:PRK10535 88 FGFIFQ-----------RYHLLSHLtaaQNVEVPavyagleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVMNKG 218
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-231 |
1.32e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.50 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqTITD----DNFEKLRK 83
Cdd:PRK13536 42 IDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-----TVLGvpvpARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIV--FQNPDNQFV--GSIVKYDVAFGlenhavphdeMHRRVSEA----LKQVDMLER-ADYEPNALSGGQKQRVAIA 154
Cdd:PRK13536 115 RIGVVpqFDNLDLEFTvrENLLVFGRYFG----------MSTREIEAvipsLLEFARLESkADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFD 231
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-230 |
1.43e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 91.24 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLM------------------------------- 55
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 56 ----IGIENVK-------------------SGEIFYNNQTITDDNFEKLRKDIGIVFQNPdNQFVGSIVKyDVAFGLENH 112
Cdd:PTZ00265 1246 eeqnVGMKNVNefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYE-NIKFGKEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 113 AVphdEMHRRVSEALKQVDMLERA--DYEPN------ALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDL 184
Cdd:PTZ00265 1324 TR---EDVKRACKFAAIDEFIESLpnKYDTNvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 185 VRKVKSEHNITIISITHDLSEAMEADHVIVMNK----GT-VYKEGTATEIF 230
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAHGTHEELL 1451
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-229 |
2.69e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL-RKdiGIV--FQNP---------DNQ 95
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRM--GVVrtFQHVrlfremtviENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 96 FVGS--IVKYDVAFGLenHAVP-----HDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:PRK11300 102 LVAQhqQLKTGLFSGL--LKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-223 |
2.82e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.17 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASFT---------------------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKS 63
Cdd:COG2401 5 NPFFVLMRVTKVYSSVLDLServaivleafgvelrvveryvLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 64 GEIFYNnqtITDDNFEKLRKDIGIVFQNPD-NQFVG--SIVKY-DVAFglenhavphdeMHRRVSEalkqvdmleradye 139
Cdd:COG2401 85 VAGCVD---VPDNQFGREASLIDAIGRKGDfKDAVEllNAVGLsDAVL-----------WLRRFKE-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 140 pnaLSGGQKQRVAIASVLALNPSVIILDEATSMLDPD-----ARqNLLDLVRkvksEHNITIISITH--DLSEAMEADHV 212
Cdd:COG2401 137 ---LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrvAR-NLQKLAR----RAGITLVVATHhyDVIDDLQPDLL 208
|
250
....*....|.
gi 613389154 213 IVMNKGTVYKE 223
Cdd:COG2401 209 IFVGYGGVPEE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-218 |
3.21e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIGIVFQNPDNQ----FVGSIV 101
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS-TAQRLARGLVYLPEDRQssglYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 KYDVAfglenhAVPHDEMHRRVSEAlKQVDMLER-----------ADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK15439 359 AWNVC------ALTHNRRGFWIKPA-RENAVLERyrralnikfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613389154 171 SMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKG 218
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQmADRVLVMHQG 479
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-229 |
3.79e-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: 89.48 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVK--SGEIFYN---------------- 69
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIYHvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 70 -------NQTIT----------DDNFEKLRKDIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDM 132
Cdd:TIGR03269 79 gepcpvcGGTLEpeevdfwnlsDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 133 LERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAME--AD 210
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV-LTSHWPEVIEdlSD 237
|
250
....*....|....*....
gi 613389154 211 HVIVMNKGTVYKEGTATEI 229
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV 256
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-243 |
3.83e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdNFEKLRKDI 85
Cdd:PRK13537 6 APIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQ----NPDNQFVGSIVKYDVAFGLENHAVphdemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNP 161
Cdd:PRK13537 83 GVVPQfdnlDPDFTVRENLLVFGRYFGLSAAAA-----RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDHaeeltTIG 240
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIES-----EIG 231
|
...
gi 613389154 241 LDL 243
Cdd:PRK13537 232 CDV 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-219 |
7.51e-20 |
|
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: 83.27 E-value: 7.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGienvksgeifynnqtitddnfeKLRKDIGI 87
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG----------------------ELEPDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDNQFVgsivkYdvafglenhavphdemhrrvseaLKQvdmleradyepnaLSGGQKQRVAIASVLALNPSVIILD 167
Cdd:cd03221 57 VTWGSTVKIG-----Y-----------------------FEQ-------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 168 EATSMLDPDARQNLLDLVRkvksEHNITIISITHD---LSEAmeADHVIVMNKGT 219
Cdd:cd03221 96 EPTNHLDLESIEALEEALK----EYPGTVILVSHDryfLDQV--ATKIIELEDGK 144
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-227 |
8.13e-20 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 85.85 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG--IENVKSGEIFYNNQTITD-DNFEKLRKDIGIVFQNP-------DN 94
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDlEPEERAHLGIFLAFQYPieipgvsNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIVKYDVAFGLENHAVPHdEMHRRVSEALKQVDM----LERADYEpnALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:CHL00131 103 DFLRLAYNSKRKFQGLPELDPL-EFLEIINEKLKLVGMdpsfLSRNVNE--GFSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNiTIISITH--DLSEAMEADHVIVMNKGTVYKEGTAT 227
Cdd:CHL00131 180 SGLDIDALKIIAEGINKLMTSEN-SIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-237 |
1.59e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASFT--------------------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSG 64
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSrslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 65 EIfynnqtitddnfekLRK-------DIGIVFqNPD-----N-QFVGSIvkydvaFGLenhavPHDEMHRRVSEAlkqVD 131
Cdd:COG1134 82 RV--------------EVNgrvsallELGAGF-HPEltgreNiYLNGRL------LGL-----SRKEIDEKFDEI---VE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 132 M--LERADYEP-NALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME 208
Cdd:COG1134 133 FaeLGDFIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGAVRR 211
|
250 260 270
....*....|....*....|....*....|
gi 613389154 209 -ADHVIVMNKGTVYKEGTATEIFDHAEELT 237
Cdd:COG1134 212 lCDRAIWLEKGRLVMDGDPEEVIAAYEALL 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-216 |
1.72e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.16 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNN-QTITDDNFEKLRKDI 85
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQNPdNQFVGSIvKYDVAFGL--------------ENHAVPHDEMHRRVS----------------------EALKQ 129
Cdd:PTZ00265 463 GVVSQDP-LLFSNSI-KNNIKYSLyslkdlealsnyynEDGNDSQENKNKRNScrakcagdlndmsnttdsneliEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 130 VDMLERAD--------------------YE----PNA--LSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLD 183
Cdd:PTZ00265 541 YQTIKDSEvvdvskkvlihdfvsalpdkYEtlvgSNAskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270
....*....|....*....|....*....|....
gi 613389154 184 LVRKVK-SEHNITIIsITHDLSEAMEADHVIVMN 216
Cdd:PTZ00265 621 TINNLKgNENRITII-IAHRLSTIRYANTIFVLS 653
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-243 |
1.86e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.91 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfEKLRKDIGIVFqnpdnqfvG--SIVK 102
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIGVVF--------GqrSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVA----FGL--ENHAVPHDEMHRRVSEAlkqVDMLERADY--EP-NALSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:COG4586 109 WDLPaidsFRLlkAIYRIPDAEYKKRLDEL---VELLDLGELldTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613389154 174 DPDARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTATEIFDHAEELTTIGLDL 243
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL-CDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLEL 256
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-229 |
2.16e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.21 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKsGEIFYNNQTITDDNFEKLRKDIGIVFQNPdNQFVGSIvKYDVAF 107
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNP-QLPHGTL-RDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 108 GleNHAVPHDEMHrrvsEALKQVDMLERADYEPNAL-----------SGGQKQRVAIASVLALNPSVIILDEATSMLDPD 176
Cdd:PRK11174 446 G--NPDASDEQLQ----QALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 177 ARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK11174 520 SEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-219 |
3.12e-19 |
|
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: 83.53 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKL----RK 83
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVFQNPdnQFVGSIVKYDVAFGlenhAVPHDEMHRRVSEALK---QVDMLERADYEPNA-----LSGGQKQRVAIAS 155
Cdd:cd03290 80 SVAYAAQKP--WLLNATVEENITFG----SPFNKQRYKAVTDACSlqpDIDLLPFGDQTEIGerginLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 156 VLALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGT 219
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-229 |
3.19e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEkLRKDIG------------IVFQNpdn 94
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA-TRRRVGymsqafslygelTVRQN--- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 qfvgsivkydvafgLENHA----VPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:NF033858 360 --------------LELHArlfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 171 SMLDPDAR----QNLLDLVRkvksEHNITI-ISiTHDLSEAMEADHVIVMNKGTVYKEGTATEI 229
Cdd:NF033858 426 SGVDPVARdmfwRLLIELSR----EDGVTIfIS-THFMNEAERCDRISLMHAGRVLASDTPAAL 484
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-229 |
3.20e-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: 87.31 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 10 FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVF 89
Cdd:TIGR00957 1287 FRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIP 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 90 QNPdNQFVGSI----------VKYDVAFGLEnhaVPHdeMHRRVSEALKQVDMlERADYEPNaLSGGQKQRVAIASVLAL 159
Cdd:TIGR00957 1367 QDP-VLFSGSLrmnldpfsqySDEEVWWALE---LAH--LKTFVSALPDKLDH-ECAEGGEN-LSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 160 NPSVIILDEATSMLDPDArQNLLDLVRKVKSEhNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEI 229
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLET-DNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-219 |
4.01e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqTITDDNFEKL------RKDIGIVFQN------- 91
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----TINNINYNKLdhklaaQLGIGIIYQElsvidel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 --PDNQFVGSIVKYDVaFGLEnhAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEA 169
Cdd:PRK09700 96 tvLENLYIGRHLTKKV-CGVN--IIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 170 TSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGT 219
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRiCDRYTVMKDGS 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-225 |
2.02e-18 |
|
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: 85.07 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 34 KGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItDDNFEKLRKDIGIVFQNpDNQFVGSIVKYDVAFGLENHA 113
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH-NILFHHLTVAEHILFYAQLKG 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 114 VPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHn 193
Cdd:TIGR01257 1033 RSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR- 1111
|
170 180 190
....*....|....*....|....*....|...
gi 613389154 194 iTIISITHDLSEA-MEADHVIVMNKGTVYKEGT 225
Cdd:TIGR01257 1112 -TIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-239 |
2.02e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKdIGI--VFQNPdNQFVGSIVK 102
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ-LGIylVPQEP-LLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVAFGLENHAVPhdemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLL 182
Cdd:PRK15439 105 ENILFGLPKRQAS----MQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLF 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 183 DLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGtATEIFDHAEELTTI 239
Cdd:PRK15439 181 SRIRELLAQ-GVGIVFISHKLPEIRQlADRISVMRDGTIALSG-KTADLSTDDIIQAI 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-237 |
2.19e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKDIGIVFQNP-DNQFVG--SIV 101
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITESRrDNGFFPnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 ------------KYDVAFGLENHavpHDEmhRRVSEALKQVDMLERADYEPN--ALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:PRK09700 360 qnmaisrslkdgGYKGAMGLFHE---VDE--QRTAENQRELLALKCHSVNQNitELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 168 EATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEadhviVMNKGTVYKEGTATEIFDHAEELT 237
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIIT-----VCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-202 |
2.38e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 10 FKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTitddnfeklrkDIGIVF 89
Cdd:COG0488 1 LENLSKSFGGRPLL--DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 90 QNP---DNQFVGSIV------------KYDVAfgLENHAVPHDEMHR------------------RVSEALKQVDMLERA 136
Cdd:COG0488 68 QEPpldDDLTVLDTVldgdaelraleaELEEL--EAKLAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 137 DYEP-NALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKvkseHNITIISITHD 202
Cdd:COG0488 146 LDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHD 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-201 |
6.51e-18 |
|
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: 78.73 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQyQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqtitddnfeklrkdigi 87
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 vfqnpdnqfvgsivkydvafglenhavphdEMHRRvsealKQVDMLERADYEP-------------NALSGGQKQRVAIA 154
Cdd:cd03223 59 ------------------------------GMPEG-----EDLLFLPQRPYLPlgtlreqliypwdDVLSGGEQQRLAFA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 613389154 155 SVLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITH 201
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-220 |
8.93e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 8.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNnqtitddnfEKLRkdIG 86
Cdd:COG0488 315 VLELEGLSKSYGDKTLL--DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETVK--IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNPDNqfvgsivkydvafgLENHAVPHDEMhRRVSEALKQV---DMLER-----AD-YEP-NALSGGQKQRVAIASV 156
Cdd:COG0488 382 YFDQHQEE--------------LDPDKTVLDEL-RDGAPGGTEQevrGYLGRflfsgDDaFKPvGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHDlSEAME--ADHVIVMNKGTV 220
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG----TVLLVSHD-RYFLDrvATRILEFEDGGV 507
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-224 |
1.14e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPDNQFVGSiVKYD 104
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFD-VRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLENHAV---PHDEMHRR-VSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQN 180
Cdd:PRK09536 98 VEMGRTPHRSrfdTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 613389154 181 LLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
Cdd:PRK09536 178 TLELVRRL-VDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-229 |
1.27e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.52 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSiVKYDVAFGLEnhAVPHDemhrrVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIASV 156
Cdd:PTZ00243 1389 IPQDP-VLFDGT-VRQNVDPFLE--ASSAE-----VWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARA 1459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 157 LALNPSVIIL-DEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTATEI 229
Cdd:PTZ00243 1460 LLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
25-232 |
1.71e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI---ENVKSGEIFYNNQTITDD-----NFEKLRKDIGIVFQN----- 91
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrlarDIRKSRANTGYIFQQfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 ----PDNQFVGSIVKYDVAFGLENHAVPhdEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:PRK09984 100 rlsvLENVLIGALGSTPFWRTCFSWFTR--EQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTA----TEIFDH 232
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSqqfdNERFDH 247
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-229 |
2.12e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNF------EKLRkdIGIVFQnpDNQ-FVGS 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclppEKRR--IGYVFQ--DARlFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 100 IVKYDVAFGLENHAVPHDEmhrRVSEALKQVDMLERadYePNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQ 179
Cdd:PRK11144 92 KVRGNLRYGMAKSMVAQFD---KIVALLGIEPLLDR--Y-PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-237 |
2.40e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNF-EKLRKDIGIVFQN----PD-----N 94
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQElhlvPEmtvaeN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIVKydvAFGLENHAvphdEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK11288 100 LYLGQLPH---KGGIVNRR----LLNYEAREQLEHLGV----DIDPDTplkyLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNItIISITHDLSEAME-ADHVivmnkgTVYKEGTATEIFDHAEELT 237
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFAlCDAI------TVFKDGRYVATFDDMAQVD 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-218 |
6.90e-17 |
|
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: 79.87 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI--ENVKSGEIFYNNQTITDDNF-EKLRKDIGIVFQN---------P 92
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIrDTERAGIVIIHQEltlvpelsvA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 DNQFVGSIVKydvafgLENHAVPHDEMHRRVSEALKQVdmleRADYEPNA-----LSGGQKQRVAIASVLALNPSVIILD 167
Cdd:TIGR02633 97 ENIFLGNEIT------LPGGRMAYNAMYLRAKNLLREL----QLDADNVTrpvgdYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSE-AMEADHVIVMNKG 218
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEvKAVCDTICVIRDG 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-231 |
8.60e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 8.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKST----IAKLMIGienvkSGEIFYNNQTITDDNFEKLRKDIGIVFQNPDNQFVGSI 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTllarMAGLLPG-----QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 VKYdVAFGLenHAVPHDEMHRRV----SEALKQVDMLERadyeP-NALSGGQKQRVAIASVL-----ALNPS--VIILDE 168
Cdd:COG4138 87 FQY-LALHQ--PAGASSEAVEQLlaqlAEALGLEDKLSR----PlTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 169 ATSMLDPdARQNLLD-LVRKVkSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTATEIFD 231
Cdd:COG4138 160 PMNSLDV-AQQAALDrLLREL-CQQGITVVMSSHDLNHTLrHADRVWLLKQGKLVASGETAEVMT 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
28-232 |
9.43e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.41 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEN----VKSGEIFYNNQTITDDNFEKLRK----DIGIVFQNPD-----N 94
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRKiigrEIAMIFQEPSscldpS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIVKydvafglenHAVPHDEM-----------HRRVSEALKQVDMLERADY---EPNALSGGQKQRVAIASVLALN 160
Cdd:COG4170 106 AKIGDQLI---------EAIPSWTFkgkwwqrfkwrKKRAIELLHRVGIKDHKDImnsYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLeSISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-214 |
1.00e-16 |
|
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: 77.06 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGE-------IFYNNQTITDDnfeklrkdigivFQ 90
Cdd:cd03237 8 KTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDieieldtVSYKPQYIKAD------------YE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 91 NPDNQFVGSIVKydvafGLENHAVPHDEmhrrVSEALKQVDMLERadyEPNALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:cd03237 76 GTVRDLLSSITK-----DFYTHPYFKTE----IAKPLQIEQILDR---EVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIV 214
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIdYLADRLIV 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-229 |
1.30e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTI----------------TDDnfeklRKDIGIV 88
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsprdairagiayvPED-----RKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 89 FQNP--DNQFVGSIVKYdVAFGLenhaVPHDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIASVLALNPSVII 165
Cdd:COG1129 343 LDLSirENITLASLDRL-SRGGL----LDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 166 LDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEI 229
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGlSDRILVMREGRIVGELDREEA 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-237 |
1.72e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.68 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKS--GEIFYNNQTItddNFEKLR--KDIGIVF--QN----P-- 92
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVC---RFKDIRdsEALGIVIihQElaliPyl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 ---DNQFVGS-IVKYDVafglenhaVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:NF040905 94 siaENIFLGNeRAKRGV--------IDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 169 ATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVivmnkgTVYKEGTATEIFD-HAEELT 237
Cdd:NF040905 166 PTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRvADSI------TVLRDGRTIETLDcRADEVT 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-225 |
3.03e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.40 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG--IENVKS------GEIFYNNQTITDDNFEKLRKDIGIVFQN 91
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 PDNQFVGSiVKYDVAFGLENHAVPHDEMHRRVSEALKQVdmLERADYEP------NALSGGQKQRVAIASVLA------- 158
Cdd:PRK13547 92 AQPAFAFS-AREIVLLGRYPHARRAGALTHRDGEIAWQA--LALAGATAlvgrdvTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 159 --LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGT 225
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-225 |
4.94e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEK-LRK 83
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQA--LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 DIGIVfqnPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIASVLALNPS 162
Cdd:PRK11614 81 AVAIV---PEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLhERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 163 VIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKlADRGYVLENGHVVLEDT 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-218 |
6.69e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 20 DASF----TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItddNFEKLRKD----IGIVFQN 91
Cdd:PRK10762 11 DKAFpgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV---TFNGPKSSqeagIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 ---------PDNQFVGSivKYDVAFGlenhAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPS 162
Cdd:PRK10762 88 lnlipqltiAENIFLGR--EFVNRFG----RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 163 VIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKG 218
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-239 |
1.77e-15 |
|
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: 73.79 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIvkydvAFGLENHAVPHDEmhrRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIASV 156
Cdd:cd03288 100 ILQDP-ILFSGSI-----RFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 157 LALNPSVIILDEATSMLDPdARQNLLDLVrKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEEL 236
Cdd:cd03288 171 FVRKSSILIMDEATASIDM-ATENILQKV-VMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGV 248
|
...
gi 613389154 237 TTI 239
Cdd:cd03288 249 FAS 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-203 |
1.96e-15 |
|
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: 72.78 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPdnqfvgsiVKYDVAf 107
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG--------LKPELS- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 108 GLEN----HAVpHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLD 183
Cdd:TIGR01189 90 ALENlhfwAAI-HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170 180
....*....|....*....|
gi 613389154 184 LVRKVKSEHNITIISITHDL 203
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTHQDL 188
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-229 |
2.48e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIeNVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPDNQFVGSIVKYdVAF 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQY-LTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 108 GLENHAVPHDEMH--RRVSEALKQVDMLERAdyePNALSGGQKQRVAIASVL-----ALNPS--VIILDEATSMLDPdAR 178
Cdd:PRK03695 93 HQPDKTRTEAVASalNEVAEALGLDDKLGRS---VNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDV-AQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613389154 179 QNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTATEI 229
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLrHADRVWLLKQGKLLASGRRDEV 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-228 |
1.86e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKST-IAKLMIGIEN--VKSGEIFYNNQTItddNFEKLRKDIGIVFQnpDNQFVGSIV 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlMNALAFRSPKgvKGSGSVLLNGMPI---DAKEMRAISAYVQQ--DDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 KYD-----VAFGLENHaVPHDEMHRRVSEALKQVDMLERADY---EPN---ALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:TIGR00955 116 VREhlmfqAHLRMPRR-VTKKEKRERVDEVLQALGLRKCANTrigVPGrvkGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTATE 228
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELfDKIILMAEGRVAYLGSPDQ 253
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-216 |
5.71e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNnqtitddnfEKLRkdI 85
Cdd:PRK09544 3 SLVSLENVSVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVfqnPDNQFVGSIVKYDVA-FGLENHAVPHDEmhrrVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVI 164
Cdd:PRK09544 70 GYV---PQKLYLDTTLPLTVNrFLRLRPGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMN 216
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLN 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-230 |
6.90e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSiVKYDV-AFGLENHAVPHDEMHRrvsEALKqvDMLERADYEPNA--------LSGGQKQRVAIASVLA 158
Cdd:PLN03232 1315 IPQSP-VLFSGT-VRFNIdPFSEHNDADLWEALER---AHIK--DVIDRNPFGLDAevseggenFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 159 LNPSVIILDEATSMLdpDARQNLLdLVRKVKSE-HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIF 230
Cdd:PLN03232 1388 RRSKILVLDEATASV--DVRTDSL-IQRTIREEfKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-213 |
6.99e-14 |
|
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: 68.40 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 38 TSIVGHNGSGKSTIaklmigIENVK---SGEIFYNN---QTITDDNFEKLRK-DIGIVFQNPDNQFVGSIVKYDVafgLE 110
Cdd:cd03240 25 TLIVGQNGAGKTTI------IEALKyalTGELPPNSkggAHDPKLIREGEVRaQVKLAFENANGKKYTITRSLAI---LE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 111 NHA-VPHDEMHRRVsealkqVDMLERadyepnaLSGGQKQ------RVAIASVLALNPSVIILDEATSMLDPD-ARQNLL 182
Cdd:cd03240 96 NVIfCHQGESNWPL------LDMRGR-------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLA 162
|
170 180 190
....*....|....*....|....*....|.
gi 613389154 183 DLVRKVKSEHNITIISITHDLSEAMEADHVI 213
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-230 |
7.29e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI----ENVKSGEIFYNNQTITDdnfEKLR-KDIGIVFQNPDNQFvgSI 100
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAP---CALRgRKIATIMQNPRSAF--NP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 VKYDVAFGLENHAV---PHDEmhRRVSEALKQVDMLERA---DYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:PRK10418 95 LHTMHTHARETCLAlgkPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 175 PDARQNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRIVEQGDVETLF 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-221 |
7.41e-14 |
|
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: 68.04 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEN--VKSGEIFYNNQTITDDnfek 80
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNpdnqfvgsivkyDVAFGLENhavphdemhrrVSEALKQVDMLEradyepnALSGGQKQRVAIASVLALN 160
Cdd:cd03232 77 FQRSTGYVEQQ------------DVHSPNLT-----------VREALRFSALLR-------GLSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAM--EADHVIVMNKG--TVY 221
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHQPSASIfeKFDRLLLLKRGgkTVY 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-201 |
1.70e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNfeklrkdigivfqnpdnqfVGSIVKY- 103
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD-------------------VAEACHYl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 104 ----------DVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:PRK13539 79 ghrnamkpalTVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*...
gi 613389154 174 DPDARQNLLDLVRkVKSEHNITIISITH 201
Cdd:PRK13539 159 DAAAVALFAELIR-AHLAQGGIVIAATH 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-230 |
1.85e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqTITDDNF------EKLRKDIGIVFQNPDNQFVG 98
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEDIsllplhARARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDAR 178
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613389154 179 QNLLDLVRKVKsEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTATEIF 230
Cdd:PRK10895 174 IDIKRIIEHLR-DSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEIL 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-231 |
2.34e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 40 IVGHNGSGKSTIAKLMIGIENVKSGEIF------YNNQTITDDNFEK----LRKDIGivfqnpdNQFVGSIVKYDVA--F 107
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisYKPQYISPDYDGTveefLRSANT-------DDFGSSYYKTEIIkpL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 108 GLENHavphdeMHRRVSEalkqvdmleradyepnaLSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRK 187
Cdd:COG1245 444 GLEKL------LDKNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 613389154 188 VKSEHNITIISITHDLS-EAMEADHVIVMnKGTVYKEGTATEIFD 231
Cdd:COG1245 501 FAENRGKTAMVVDHDIYlIDYISDRLMVF-EGEPGVHGHASGPMD 544
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-219 |
3.22e-13 |
|
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: 66.19 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKlmigienvksgEIFYNNQTITDDNFEKLRKDIGIVFqnpdnqfVGSIvKYD 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGKARLISFLPKFSRNKLIF-------IDQL-QFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLEnhavphdemhrrvseALKqvdmLERadyEPNALSGGQKQRVAIASVLALNP--SVIILDEATSMLDPDARQNLL 182
Cdd:cd03238 72 IDVGLG---------------YLT----LGQ---KLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLL 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 613389154 183 DLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGT 219
Cdd:cd03238 130 EVIKGLIDLGN-TVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-203 |
3.50e-13 |
|
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: 66.75 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNPdnqfvgsiVKYDVAf 107
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPG--------IKTTLS- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 108 GLEN----HAVPHDEmhrRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLD 183
Cdd:cd03231 90 VLENlrfwHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170 180
....*....|....*....|
gi 613389154 184 LVRKVKSEHNITIISITHDL 203
Cdd:cd03231 167 AMAGHCARGGMVVLTTHQDL 186
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
28-229 |
5.20e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENvksgeifyNNQTITDDNF------------EKLRKDIG----IVFQN 91
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--------DNWRVTADRMrfddidllrlspRERRKLVGhnvsMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 PDN----------QFVGSIVKYDVA------FGLEnhavphdemHRRVSEALKQV------DMLERADYEpnaLSGGQKQ 149
Cdd:PRK15093 98 PQScldpservgrQLMQNIPGWTYKgrwwqrFGWR---------KRRAIELLHRVgikdhkDAMRSFPYE---LTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 150 RVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATE 228
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKE 245
|
.
gi 613389154 229 I 229
Cdd:PRK15093 246 L 246
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-204 |
6.43e-13 |
|
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: 66.62 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 32 IPK-GQWTSIVGHNGSGKSTIAKLMIG--IENVKSGEIFYNNQTITD--------DNFEKLRKDIGIVFQNPdnQFVGSI 100
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGklKPNLGKFDDPPDWDEILDefrgselqNYFTKLLEGDVKVIVKP--QYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 ---VKYDVAFGLENHavphDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDA 177
Cdd:cd03236 100 pkaVKGKVGELLKKK----DERGK-LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*..
gi 613389154 178 RQNLLDLVRKVkSEHNITIISITHDLS 204
Cdd:cd03236 175 RLNAARLIREL-AEDDNYVLVVEHDLA 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-229 |
8.46e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 8.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSivkydVAFGLEnhavPHDEmHRRVS--EALKQV---DMLERADYEPNA--------LSGGQKQRVAIA 154
Cdd:PLN03130 1318 IPQAP-VLFSGT-----VRFNLD----PFNE-HNDADlwESLERAhlkDVIRRNSLGLDAevseagenFSVGQRQLLSLA 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 155 SVLALNPSVIILDEATSMLD--PDArqnlldLVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEI 229
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDvrTDA------LIQKTIREEfkSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-231 |
8.51e-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: 68.05 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IENVK-----SGEIFYNNQTITDDNfEKL 81
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEghvhmKGSVAYVPQQAWIQN-DSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 RKDI--GIVFQNPDNQFVgsivkydvafgLENHAVPHDemhrrvSEALKQVDMLERADYEPNaLSGGQKQRVAIASVLAL 159
Cdd:TIGR00957 716 RENIlfGKALNEKYYQQV-----------LEACALLPD------LEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSE-HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFD 231
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-218 |
1.45e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItddNF----EKLRKDIGIVFQNPdNQFVGSI 100
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFksskEALENGISMVHQEL-NLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 VKYDVAFG---LENHAVPHDEMHRRVSEALKQVDMleraDYEPNA----LSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:PRK10982 90 VMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDI----DIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 613389154 174 DPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKG 218
Cdd:PRK10982 166 TEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-228 |
1.64e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDN-FEKLRKdiGIVFQNPDNQFVGSIVKY 103
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLAN--GIVYISEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 104 DVAfglENHAVPHDEMHRRVSEALKQVD-MLERADY-------EPNA------LSGGQKQRVAIASVLALNPSVIILDEA 169
Cdd:PRK10762 346 SVK---ENMSLTALRYFSRAGGSLKHADeQQAVSDFirlfnikTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 170 TSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTATE 228
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLgMSDRILVMHEGRISGEFTREQ 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-238 |
1.68e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 67.24 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKsGEIFYNNQTITDDNFEKLRKDIGIVfq 90
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVI-- 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 91 nPDNQFV--GSIVKydvafGLENHAVPHDEMHRRVSEALKQVDMLERADYEPN--------ALSGGQKQRVAIASVLALN 160
Cdd:TIGR01271 1298 -PQKVFIfsGTFRK-----NLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDfvlvdggyVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 161 PSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMnkgtvykEGTATEIFDHAEELTT 238
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQ----IIRKTlkQSFSNCTVILSEHRVEALLECQQFLVI-------EGSSVKQYDSIQKLLN 1440
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-231 |
1.86e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 22 SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIF------YNNQTITDDNFEKLRKdigIVFQNPDNq 95
Cdd:PRK13409 352 DFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkisYKPQYIKPDYDGTVED---LLRSITDD- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 96 FVGSIVKYDVAFGLENHAVphdeMHRRVSEalkqvdmleradyepnaLSGGQKQRVAIASVLALNPSVIILDEATSMLDP 175
Cdd:PRK13409 428 LGSSYYKSEIIKPLQLERL----LDKNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 176 DARQNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMnKGTVYKEGTATEIFD 231
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEREATALVVDHDIYmIDYISDRLMVF-EGEPGKHGHASGPMD 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-203 |
2.09e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 22 SFTLkdvsFNIP---KGQWTSIVGHNGSGKSTIAKLMigienvkSGEIF-----YNNQTITD------------DNFEKL 81
Cdd:PRK13409 87 GFKL----YGLPipkEGKVTGILGPNGIGKTTAVKIL-------SGELIpnlgdYEEEPSWDevlkrfrgtelqNYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 R-KDIGIVfQNPdnQFVGSIVKYdvafglenhavphdeMHRRVSEALKQVD-------MLERADYEP------NALSGGQ 147
Cdd:PRK13409 156 YnGEIKVV-HKP--QYVDLIPKV---------------FKGKVRELLKKVDergkldeVVERLGLENildrdiSELSGGE 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 148 KQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDL 203
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVE--HDL 271
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-225 |
5.19e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.81 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 3 DKNSVIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdNFEKLR 82
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIV--FQNPDNQFVGSIVKYDVAfglENHAVPHDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALN 160
Cdd:TIGR01257 2012 QNMGYCpqFDAIDDLLTGREHLYLYA---RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAmEA--DHVIVMNKGTVYKEGT 225
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT-SHSMEEC-EAlcTRLAIMVKGAFQCLGT 2153
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-204 |
5.64e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 12 NVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItDDNFEKLRKDIGIVFQ- 90
Cdd:PRK13540 6 ELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 91 ---NPdNQFVGSIVKYDVAFGLENHAVphDEMHRRVSealkqvdMLERADYEPNALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:PRK13540 83 sgiNP-YLTLRENCLYDIHFSPGAVGI--TELCRLFS-------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 613389154 168 EATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS 204
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLP 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-224 |
6.53e-12 |
|
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: 63.32 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqtitddnfEKLRK-----DIGIVFQNP----DN- 94
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------------TVRGRvssllGLGGGFNPEltgrENi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIvkydvafglenHAVPHDEMHRRV------SEalkqvdmLERADYEP-NALSGGQKQRVAIASVLALNPSVIILD 167
Cdd:cd03220 106 YLNGRL-----------LGLSRKEIDEKIdeiiefSE-------LGDFIDLPvKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 168 EATSMLDPDARQNLLDLVRKvKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-215 |
7.66e-12 |
|
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: 64.81 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 22 SFTLkdvsFNIP---KGQWTSIVGHNGSGKSTIAKLMigienvkSGEIF-----YNNQTITD------------DNFEKL 81
Cdd:COG1245 87 GFRL----YGLPvpkKGKVTGILGPNGIGKSTALKIL-------SGELKpnlgdYDEEPSWDevlkrfrgtelqDYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 82 R-KDIGIVfQNPdnQFVGSIVKY---DVAFGLENHavphDEmHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVL 157
Cdd:COG1245 156 AnGEIKVA-HKP--QYVDLIPKVfkgTVRELLEKV----DE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLseA---MEADHVIVM 215
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDL--AildYLADYVHIL 285
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-229 |
9.46e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-------IENVKSGEIFYN-------NQT 72
Cdd:PLN03130 615 ISIKNGYFSWDSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGelpprsdASVVIRGTVAYVpqvswifNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 73 ITDDnfeklrkdigIVFQNPDNQfvgsiVKYDVAfgLENHAVPHDemhrrvSEALKQVDMLERADYEPNaLSGGQKQRVA 152
Cdd:PLN03130 695 VRDN----------ILFGSPFDP-----ERYERA--IDVTALQHD------LDLLPGGDLTEIGERGVN-ISGGQKQRVS 750
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613389154 153 IASVLALNPSVIILDEATSMLDPDARQNLLDlvRKVKSE-HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEI 229
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-234 |
1.42e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGienvksgEIFYNNQTITDdnfekLRKDIG 86
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------ELSHAETSSVV-----IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 IVFQNPdnQFVGSIVKYDVAFG-----------LENHAVPHDemhrrvSEALKQVDMLERADYEPNaLSGGQKQRVAIAS 155
Cdd:PLN03232 683 YVPQVS--WIFNATVRENILFGsdfeserywraIDVTALQHD------LDLLPGRDLTEIGERGVN-ISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 156 VLALNPSVIILDEATSMLDPDARQNLLDLVrkVKSE-HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAE 234
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVFDSC--MKDElKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-219 |
1.68e-11 |
|
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: 60.85 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 40 IVGHNGSGKSTIAKLMIGIENVKSGEIFYNNqtiTDDNFEKLRKDIGIVFQNPDnqfvgsivkydvafglenhavphdem 119
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIYID---GEDILEEVLDQLLLIIVGGK-------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 120 hrrvsealkqvdmleradyePNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVR-----KVKSEHNI 194
Cdd:smart00382 58 --------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNL 117
|
170 180 190
....*....|....*....|....*....|.
gi 613389154 195 TIISITHDLSEAMEA------DHVIVMNKGT 219
Cdd:smart00382 118 TVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-224 |
1.84e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEN--VKSGEIFYNNQTITD-DNFEKLRKDIGIVFQNP------DNQ 95
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLElSPEDRAGEGIFMAFQYPveipgvSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 96 F-----VGSIVKYDVAFGLENHAVpHDEMHRRVSEALKQVDMLERADYEpnALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK09580 97 FflqtaLNAVRSYRGQEPLDRFDF-QDLMEEKIALLKMPEDLLTRSVNV--GFSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHNITIIsITH--DLSEAMEADHVIVMNKGTVYKEG 224
Cdd:PRK09580 174 SGLDIDALKIVADGVNSLRDGKRSFII-VTHyqRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-220 |
5.21e-11 |
|
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: 61.41 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKsGEIFYNNQTITDDNFEKLRKDIGI 87
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPdNQFVGSIVKydvafGLENHAVPHDEMHRRVSE--ALK--------QVD-MLERADYepnALSGGQKQRVAIASV 156
Cdd:cd03289 82 IPQKV-FIFSGTFRK-----NLDPYGKWSDEEIWKVAEevGLKsvieqfpgQLDfVLVDGGC---VLSHGHKQLMCLARS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 157 LALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQ----VIRKTlkQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-174 |
5.91e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItddnfEKLRKDIgivfqNPDNQFVG--SIVKyD 104
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----RRQRDEY-----HQDLLYLGhqPGIK-T 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 105 VAFGLEN-------HAVPHDEMHRrvsEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:PRK13538 88 ELTALENlrfyqrlHGPGDDEALW---EALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-202 |
9.41e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNnQTITddnfeklrkdIGIVFQNP---DNQFVGSIV 101
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQEPqldPTKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 KYDVAFGL----------ENHAVPHDEMHR------RVSEALKQVDM------LERA---------DYEPNALSGGQKQR 150
Cdd:TIGR03719 90 EEGVAEIKdaldrfneisAKYAEPDADFDKlaaeqaELQEIIDAADAwdldsqLEIAmdalrcppwDADVTKLSGGERRR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613389154 151 VAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHD 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-218 |
1.05e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.58 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSDASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI--ENVK-SGEIFYNNQTItDDNFEK 80
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSvEGDIHYNGIPY-KEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 81 LRKDIGIVFQNpDNQFVGSIVKYDVAFGLENHAvphDEMHRRVsealkqvdmleradyepnalSGGQKQRVAIASVLALN 160
Cdd:cd03233 81 YPGEIIYVSEE-DVHFPTLTVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 161 PSVIILDEATSMLDPDARQNLLDLVRKV-KSEHNITIISITHDLSEAMEA-DHVIVMNKG 218
Cdd:cd03233 137 ASVLCWDNSTRGLDSSTALEILKCIRTMaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-220 |
1.10e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFynnqtitddnfekLRKDIGIVFQNP--DN 94
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQQAwiMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFV-GSIVKYDVafglENHAVPHDEMhrRVSEALKQVDML------ERADYEPNaLSGGQKQRVAIASVLALNPSVIILD 167
Cdd:PTZ00243 735 ATVrGNILFFDE----EDAARLADAV--RVSQLEADLAQLgggletEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 168 EATSMLDPDARQNlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
Cdd:PTZ00243 808 DPLSALDAHVGER---VVEECflGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-241 |
1.25e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKD-IGIVfqnP-DNQFVGSIVK 102
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYI---PeDRLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVA--FGLENHAVP---------HDEMHRRVSEALKQVDMleRA---DYEPNALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:COG3845 351 MSVAenLILGRYRRPpfsrggfldRKAIRAFAEELIEEFDV--RTpgpDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 169 ATSMLDPDA----RQNLLDLVRKvksehNITIISITHDLSEAME-ADHVIVMNKGTVykegtaTEIFDhAEELT--TIGL 241
Cdd:COG3845 429 PTRGLDVGAiefiHQRLLELRDA-----GAAVLLISEDLDEILAlSDRIAVMYEGRI------VGEVP-AAEATreEIGL 496
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-229 |
1.83e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 7 VIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnfEKLRKDIG 86
Cdd:NF033858 1 VARLEGVSHRYGKTVA--LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 87 --I----------------VFQNPDnqFVGSIvkydvaFGLenhavPHDEMHRRVSEALKQVDMLERADYEPNALSGGQK 148
Cdd:NF033858 76 prIaympqglgknlyptlsVFENLD--FFGRL------FGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 149 QRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEH-NITIISITHDLSEAMEADHVIVMNKGTVYKEGTAT 227
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPA 222
|
..
gi 613389154 228 EI 229
Cdd:NF033858 223 EL 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-204 |
2.47e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 19 SDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNnqtiTDDNFEKLRkdigivfQNPDNQFVG 98
Cdd:PRK11147 14 SDAPL-LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLQ-------QDPPRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 99 SIVKYdVAFGLEN--------HAVPHD-----------EMHR---------------RVSEALKQVDMleRADYEPNALS 144
Cdd:PRK11147 82 TVYDF-VAEGIEEqaeylkryHDISHLvetdpseknlnELAKlqeqldhhnlwqlenRINEVLAQLGL--DPDAALSSLS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 145 GGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHDLS 204
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRS 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-174 |
4.42e-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: 59.56 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYnNQTItddnfeklrkD 84
Cdd:TIGR03719 320 DKVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------K 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRR--VSE-ALKQVDMLERADyepnALSGGQKQRVAIASVLALNP 161
Cdd:TIGR03719 387 LAYVDQSRDALDPNKTVWEEISGGLDIIKLGKREIPSRayVGRfNFKGSDQQKKVG----QLSGGERNRVHLAKTLKSGG 462
|
170
....*....|...
gi 613389154 162 SVIILDEATSMLD 174
Cdd:TIGR03719 463 NVLLLDEPTNDLD 475
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-201 |
6.71e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.38 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 1 MEDKNSVIVFKNVSFQYQSdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSG--------EIFYNNQT 72
Cdd:TIGR00954 445 VEYQDNGIKFENIPLVTPN-GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGrltkpakgKLFYVPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 73 ITDDNfEKLRKDIgIVFQNPDNQFVGSIVKYDVAFGLENhavphdemhrrvseaLKQVDMLER-------ADYEpNALSG 145
Cdd:TIGR00954 524 PYMTL-GTLRDQI-IYPDSSEDMKRRGLSDKDLEQILDN---------------VQLTHILEReggwsavQDWM-DVLSG 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 146 GQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITH 201
Cdd:TIGR00954 586 GEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-215 |
1.00e-09 |
|
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: 56.21 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFniPKGQWTSIVGHNGSGKSTIAKlmigienvksgeifynnqtitddnfeklrkDIG-IVFQNPDNQFVGSIVKydv 105
Cdd:cd03227 15 DVTF--GEGSLTIITGPNGSGKSTILD------------------------------AIGlALGGAQSATRRRSGVK--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 106 afglENHAVPHDEMHRRVSeaLKQvdmleradyepnaLSGGQKQRVAIASVLAL---NP-SVIILDEATSMLDPDARQNL 181
Cdd:cd03227 60 ----AGCIVAAVSAELIFT--RLQ-------------LSGGEKELSALALILALaslKPrPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....
gi 613389154 182 LDLVRKvKSEHNITIISITHDLSEAMEADHVIVM 215
Cdd:cd03227 121 AEAILE-HLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-246 |
1.25e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 19 SDASFTLKDV------SFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDDNFEKLRKDIGIVFQNP 92
Cdd:PRK10938 7 SQGTFRLSDTktlqlpSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 DNQFVgSIVKYDvaFGLENHAVPHDEMH-----RRVSEALKQVDMLERA-DYepnaLSGGQKQRVAIASVLALNPSVIIL 166
Cdd:PRK10938 87 NTDML-SPGEDD--TGRTTAEIIQDEVKdparcEQLAQQFGITALLDRRfKY----LSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 167 DEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFD--------HAEELT 237
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQqalvaqlaHSEQLE 238
|
....*....
gi 613389154 238 tiGLDLPFP 246
Cdd:PRK10938 239 --GVQLPEP 245
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-242 |
1.40e-09 |
|
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: 57.56 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQtitddnfeklrkdigIVFQNPDNQFVGSIVKYD 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGlenhaVPHDEM-HRRVSEALK-QVDMLERA--DYEPNA-----LSGGQKQRVAIASVLALNPSVIILDEATSMLDP 175
Cdd:cd03291 118 IIFG-----VSYDEYrYKSVVKACQlEEDITKFPekDNTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 176 DARQNLLD-LVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEIFDHAEELTT--IGLD 242
Cdd:cd03291 193 FTEKEIFEsCVCKLMA--NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSklMGYD 260
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-220 |
1.93e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-ENVKSGEIFYNNQTITDDNFEK-LRKDIGIVfqnPDNQFVGSIVKyD 104
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQaIRAGIAMV---PEDRKRHGIVP-I 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLE-NHAVPHDEMHRRVSEALKQVDMLERA-----------DYEPNALSGGQKQRVAIASVLALNPSVIILDEATSM 172
Cdd:TIGR02633 354 LGVGKNiTLSVLKSFCFKMRIDAAAELQIIGSAiqrlkvktaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613389154 173 LDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-244 |
2.70e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTItddNFEKLRKDI--GIVFQNPDNQFVGSIVKYDV 105
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIraGIMLCPEDRKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 106 AfglENHAVPHDEMHRRVSEALKQVDMLERADYE--------PNA------LSGGQKQRVAIASVLALNPSVIILDEATS 171
Cdd:PRK11288 349 A---DNINISARRHHLRAGCLINNRWEAENADRFirslniktPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613389154 172 MLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMnkgtvyKEGTATEIFDHAE--ELTTIGLDLP 244
Cdd:PRK11288 426 GIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGvADRIVVM------REGRIAGELAREQatERQALSLALP 494
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-202 |
3.51e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVF--KNVSfqYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSG--------EIFYnnqtitddn 77
Cdd:PRK11147 318 IVFemENVN--YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtklEVAY--------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 78 FEKLRKDIgivfqNP-----DNQFVGsivKYDVAF-GLENHAVPHDEmhrrvsealkqvDML---ERADYEPNALSGGQK 148
Cdd:PRK11147 387 FDQHRAEL-----DPektvmDNLAEG---KQEVMVnGRPRHVLGYLQ------------DFLfhpKRAMTPVKALSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 149 QRVAIASVLaLNPS-VIILDEATSMLDPDArqnlLDLVRKVKSEHNITIISITHD 202
Cdd:PRK11147 447 NRLLLARLF-LKPSnLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-202 |
4.80e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIF----YNnqtitddnfeklrkdIGIVFQNP---DNQFV 97
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARpapgIK---------------VGYLPQEPqldPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 98 GSIVKYDVA--FGL--------ENHAVPHDEMHR------RVSEALKQVD------MLERA---------DYEPNALSGG 146
Cdd:PRK11819 88 RENVEEGVAevKAAldrfneiyAAYAEPDADFDAlaaeqgELQEIIDAADawdldsQLEIAmdalrcppwDAKVTKLSGG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 147 QKQRVAIASVLALNPSVIILDEATSMLDPDARQNLldlvrkvksEHNI-----TIISITHD 202
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL---------EQFLhdypgTVVAVTHD 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-229 |
5.84e-09 |
|
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: 56.46 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQtitddnfeklrkdigIVFQNPDNQFVGSIVKYD 104
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFGLEnhavpHDEMhrRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIASVLALNPSVIILDEATSML 173
Cdd:TIGR01271 507 IIFGLS-----YDEY--RYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 174 DPDARQNLLD-LVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTATEI 229
Cdd:TIGR01271 580 DVVTEKEIFEsCLCKLMS--NKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
122-229 |
8.41e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 122 RVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITH 201
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQ 202
|
90 100
....*....|....*....|....*....
gi 613389154 202 DLSEAMEADH-VIVMNKGTVYKEGTATEI 229
Cdd:NF000106 203 YMEEAEQLAHeLTVIDRGRVIADGKVDEL 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-221 |
9.94e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 11 KNVSFQ--YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTI-----AKLMIGIenVKSGEIFYNNQTItDDNFEKLrk 83
Cdd:TIGR00956 763 RNLTYEvkIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLlnvlaERVTTGV--ITGGDRLVNGRPL-DSSFQRS-- 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 84 dIGIVFQNpDNQFVGSIVK----YDVAFGLENHaVPHDEMHRRVSEALKQVDMLERADY---EPN-ALSGGQKQRVAIAS 155
Cdd:TIGR00956 838 -IGYVQQQ-DLHLPTSTVReslrFSAYLRQPKS-VSKSEKMEYVEEVIKLLEMESYADAvvgVPGeGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 156 VLALNPSVII-LDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAM--EADHVIVMNKG--TVY 221
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSAILfeEFDRLLLLQKGgqTVY 984
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-218 |
2.33e-08 |
|
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: 53.03 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-------IENVKSGEIFYNNQTITD--DNFEKLRKDIGI----VFQN 91
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYaegqrryVESLSAYARQFLGQMDKPdvDSIEGLSPAIAIdqktTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 92 PDNQfVGSIVK-YD---VAFGLENhavphdeMHRRVsEALKQVDM----LERadyEPNALSGGQKQRVAIASVL--ALNP 161
Cdd:cd03270 91 PRST-VGTVTEiYDylrLLFARVG-------IRERL-GFLVDVGLgyltLSR---SAPTLSGGEAQRIRLATQIgsGLTG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKG 218
Cdd:cd03270 159 VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVIDIGPG 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-218 |
3.01e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-ENVKSGEIFYNNQTITDDNFEKL-----------RKDIGIVFQNP-- 92
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAiaqgiamvpedRKRDGIVPVMGvg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 DNQFVGSIVKYdVAFGLENHAVPHDEMHRRVSE-ALKQVD-MLERADyepnaLSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PRK13549 360 KNITLAALDRF-TGGSRIDDAAELKTILESIQRlKVKTASpELAIAR-----LSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613389154 171 SMLDPDARQNLLDLVRKVKSEHnITIISITHDLSEAME-ADHVIVMNKG 218
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGlSDRVLVMHEG 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-247 |
3.69e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IE-NVKSGEIFYNNQTITddnfEKLRKDIGIVFQNpDNQFVGSIVK 102
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQgNNFTGTILANNRKPT----KQILKRTGFVTQD-DILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVAF----GLENHAVPHDEMhrRVSEALkqVDMLERADYEPN--------ALSGGQKQRVAIASVLALNPSVIILDEAT 170
Cdd:PLN03211 159 ETLVFcsllRLPKSLTKQEKI--LVAESV--ISELGLTKCENTiignsfirGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 171 SMLDPDAR----QNLLDLVRKVKsehniTIISITHDLSEAMEA--DHVIVMNKGTVYKEGTATEIFDHAEeltTIGLDLP 244
Cdd:PLN03211 235 SGLDATAAyrlvLTLGSLAQKGK-----TIVTSMHQPSSRVYQmfDSVLVLSEGRCLFFGKGSDAMAYFE---SVGFSPS 306
|
...
gi 613389154 245 FPI 247
Cdd:PLN03211 307 FPM 309
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-232 |
3.87e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqtitddnfeklrkDIGivfqnpdnqfvGSIVK 102
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----------------DIK-----------GSAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 103 YDVAFGLENHAVPHDE------MHRRVSEALKQV--DMLERAD-----YEP-NALSGGQKQRVAIASVLALNPSVIILDE 168
Cdd:PRK13545 90 IAISSGLNGQLTGIENielkglMMGLTKEKIKEIipEIIEFADigkfiYQPvKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613389154 169 ATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTATEIFDH 232
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFK-EQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-220 |
1.09e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITD-DNFEKL----------RKDIGIvFQNP 92
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhNANEAInhgfalvteeRRSTGI-YAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 D---NQFVGSIVKYDVAFGL-ENHAVPHDEM----HRRVSEALKQVDMleradyepNALSGGQKQRVAIASVLALNPSVI 164
Cdd:PRK10982 342 DigfNSLISNIRNYKNKVGLlDNSRMKSDTQwvidSMRVKTPGHRTQI--------GSLSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613389154 165 ILDEATSMLDPDAR----QNLLDLVRKVKSehnitIISITHDLSEAME-ADHVIVMNKGTV 220
Cdd:PRK10982 414 MLDEPTRGIDVGAKfeiyQLIAELAKKDKG-----IIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-174 |
1.30e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 5 NSVIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYnNQTItddnfeklrkD 84
Cdd:PRK11819 322 DKVIEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------K 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 85 IGIVFQNPDNQFVGSIVKYDVAFGLENHAVPHDEMHRRV---------SEALKQVDMleradyepnaLSGGQKQRVAIAS 155
Cdd:PRK11819 389 LAYVDQSRDALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVGV----------LSGGERNRLHLAK 458
|
170
....*....|....*....
gi 613389154 156 VLALNPSVIILDEATSMLD 174
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
135-214 |
8.20e-07 |
|
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: 47.95 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 135 RADYEPN--ALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADH 211
Cdd:cd03222 62 TPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLdYLSDR 141
|
...
gi 613389154 212 VIV 214
Cdd:cd03222 142 IHV 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-182 |
1.21e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 6 SVIVFKNVSFQYQSdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMigienvkSGEifynnqtitddnfekLRKDI 85
Cdd:PLN03073 507 PIISFSDASFGYPG-GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------SGE---------------LQPSS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 86 GIVFQNPDNQfVGSIVKYDVAfGLENHAVPHDEMHRRVSEALKQV------------DMLERADYepnALSGGQKQRVAI 153
Cdd:PLN03073 564 GTVFRSAKVR-MAVFSQHHVD-GLDLSSNPLLYMMRCFPGVPEQKlrahlgsfgvtgNLALQPMY---TLSGGQKSRVAF 638
|
170 180
....*....|....*....|....*....
gi 613389154 154 ASVLALNPSVIILDEATSMLDPDARQNLL 182
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-181 |
2.04e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIfynnqtitddnfeKLRKDIGIvfqnpdnqfvGSIVKYD 104
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIKL----------GYFAQHQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 105 VAFgLENHAVPHDEMHRRVSEALKQvdmlERADY------------EPNA-LSGGQKQRVAIASVLALNPSVIILDEATS 171
Cdd:PRK10636 385 LEF-LRADESPLQHLARLAPQELEQ----KLRDYlggfgfqgdkvtEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170
....*....|
gi 613389154 172 MLDPDARQNL 181
Cdd:PRK10636 460 HLDLDMRQAL 469
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-229 |
3.44e-06 |
|
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: 48.09 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 143 LSGGQKQRVAIASVL---ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVM---- 215
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYIIDLgpeg 908
|
90
....*....|....*.
gi 613389154 216 --NKGTVYKEGTATEI 229
Cdd:TIGR00630 909 gdGGGTVVASGTPEEV 924
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
28-201 |
4.29e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.30 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 28 VSFNIPKGqWTSIVGHNGSGKSTIA---KLMIGIENVKS--GE-----IFYNNQTitddnfeklRKDIG-----IVFQNP 92
Cdd:cd03278 16 TTIPFPPG-LTAIVGPNGSGKSNIIdaiRWVLGEQSAKSlrGEkmsdvIFAGSET---------RKPANfaevtLTFDNS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 93 DNQFvgSIVkydvafglenhavphdeMHRRVSEAL----KQVDMLeradyepNALSGGQKQRVAIA---SVLALNPSVI- 164
Cdd:cd03278 86 DGRY--SII-----------------SQGDVSEIIeapgKKVQRL-------SLLSGGEKALTALAllfAIFRVRPSPFc 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 613389154 165 ILDEATSMLDPDARQNLLDLVRKvKSEHNITIIsITH 201
Cdd:cd03278 140 VLDEVDAALDDANVERFARLLKE-FSKETQFIV-ITH 174
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-187 |
7.32e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGieNVKSGeifYNN------------QTITD 75
Cdd:PRK10938 261 IVLNNGVVSYNDRP--ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQG---YSNdltlfgrrrgsgETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 76 dnfekLRKDIGIVfqnpDNQ------------------FVGSIVKYdvafglenHAVPhDEMHRRVSEALKQVDMLER-A 136
Cdd:PRK10938 334 -----IKKHIGYV----SSSlhldyrvstsvrnvilsgFFDSIGIY--------QAVS-DRQQKLAQQWLDILGIDKRtA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 137 DYEPNALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQnlldLVRK 187
Cdd:PRK10938 396 DAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQ----LVRR 442
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-235 |
8.82e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNqtitddnfeklrkDIGIVFQNP--DNQFVGSi 100
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVIAISAglSGQLTGI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 vkYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERAdYEP-NALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQ 179
Cdd:PRK13546 104 --ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFI-YQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 180 NLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVMNKGTVYKE-GTATEIFDHAEE 235
Cdd:PRK13546 181 KCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDyGELDDVLPKYEA 236
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-174 |
9.85e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI--GIENV-KSGEIFYNNQTITDDNFEKLR--------------KDIGI 87
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDGIpKNCQILHVEQEVVGDDTTALQcvlntdiertqlleEEAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 88 VFQNPDNQFVGSIVKYDVAfglENHAVPHDEMHRRVSEALKQVDMLERADYEPNA--------------------LSGGQ 147
Cdd:PLN03073 273 VAQQRELEFETETGKGKGA---NKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAasilaglsftpemqvkatktFSGGW 349
|
170 180
....*....|....*....|....*..
gi 613389154 148 KQRVAIASVLALNPSVIILDEATSMLD 174
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-185 |
1.72e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 38 TSIVGHNGSGKSTIAKLMIGIENVKSGEIFYNNQTITDdnfeklrkdigivFQNPDNQFVGSIVKYDVAFGLENHAVPHD 117
Cdd:PRK13541 29 TYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-------------IAKPYCTYIGHNLGLKLEMTVFENLKFWS 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613389154 118 EMHRRVS------EALKQVDMLERADYepnALSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLV 185
Cdd:PRK13541 96 EIYNSAEtlyaaiHYFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
40-203 |
2.26e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 40 IVGHNGSGKSTI---------------AKLMIGIENVKSGEIF------YNNQTIT----DDNFEKLRKDigivfqNPDN 94
Cdd:COG0419 28 IVGPNGAGKSTIleairyalygkarsrSKLRSDLINVGSEEASvelefeHGGKRYRierrQGEFAEFLEA------KPSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 --QFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERA------DYEP-NALSGGQKQRVAIASVLALnpsviI 165
Cdd:COG0419 102 rkEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEilaqlsGLDPiETLSGGERLRLALADLLSL-----I 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 613389154 166 LDeaTSMLDPDARQNLLDLVRkvksehNITIisITHDL 203
Cdd:COG0419 177 LD--FGSLDEERLERLLDALE------ELAI--ITHVI 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-237 |
3.88e-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: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 133 LERAdyePNALSGGQKQRVAIASVL--ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDlSEAM-EA 209
Cdd:TIGR00630 482 LSRA---AGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHD-EDTIrAA 556
|
90 100 110
....*....|....*....|....*....|....
gi 613389154 210 DHVIVMNKGT------VYKEGTATEIFDHAEELT 237
Cdd:TIGR00630 557 DYVIDIGPGAgehggeVVASGTPEEILANPDSLT 590
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-219 |
6.56e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 142 ALSGGQKQRVAIASVLAL---NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKG 218
Cdd:PRK00635 1699 SLSLSEKIAIKIAKFLYLppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGH-SVIYIDHDPALLKQADYLIEMGPG 1777
|
.
gi 613389154 219 T 219
Cdd:PRK00635 1778 S 1778
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
143-225 |
6.82e-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: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 143 LSGGQKQRVAIASVL---ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVM---- 215
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIKCADWIIDLgpeg 248
|
90
....*....|..
gi 613389154 216 --NKGTVYKEGT 225
Cdd:cd03271 249 gdGGGQVVASGT 260
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-237 |
7.43e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 141 NALSGGQKQRVAIASVLALNPSVI--ILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNK- 217
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMISLADRIIDIGPg 553
|
90 100
....*....|....*....|....*
gi 613389154 218 -----GTVYKEGTATEIFDHAEELT 237
Cdd:PRK00635 554 agifgGEVLFNGSPREFLAKSDSLT 578
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-244 |
1.11e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKST----IAKLMIGIENVKSGEIFYNNqtITDDNFEKLRKdiGIVFQNPDNqfvgsi 100
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDG--ITPEEIKKHYR--GDVVYNAET------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 101 vkyDVAFGlenhavphdemHRRVSEAL-------------KQVDMLERADYEPN----------------------ALSG 145
Cdd:TIGR00956 147 ---DVHFP-----------HLTVGETLdfaarcktpqnrpDGVSREEYAKHIADvymatyglshtrntkvgndfvrGVSG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 146 GQKQRVAIASVLALNPSVIILDEATSMLDPdarQNLLDLVRKVKSEHNIT----IISITHDLSEAMEA-DHVIVMNKGTV 220
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDS---ATALEFIRALKTSANILdttpLVAIYQCSQDAYELfDKVIVLYEGYQ 289
|
250 260
....*....|....*....|....*
gi 613389154 221 YKEGTAteifDHAEE-LTTIGLDLP 244
Cdd:TIGR00956 290 IYFGPA----DKAKQyFEKMGFKCP 310
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-213 |
1.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 121 RRVSEALKQVDMLERADYEPNALSGGQKQRVAIASVLAL------NPSVIILDEATSMLDPDARQNLLDLV----RKVKS 190
Cdd:PRK03918 767 KAEENKVKLFVVYQGKERPLTFLSGGERIALGLAFRLALslylagNIPLLILDEPTPFLDEERRRKLVDIMerylRKIPQ 846
|
90 100
....*....|....*....|....*
gi 613389154 191 ehnitIISITHD--LSEAmeADHVI 213
Cdd:PRK03918 847 -----VIIVSHDeeLKDA--ADYVI 864
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
141-201 |
1.84e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 1.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 141 NALSGGQKQ------RVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVR-KVKSEHNI-TIISITH 201
Cdd:PRK01156 800 DSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIpQVIMISH 868
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
143-218 |
2.49e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 143 LSGGQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITH----DLSEAMeaDHVIVMNKG 218
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT-VDTGRTVVCTIHqpsiDIFEAF--DELLLMKRG 1096
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
142-187 |
2.61e-04 |
|
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: 39.14 E-value: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 142 ALSGGQKQRV-------AIASVLALN------PSVIILDEATSMLDPDARQNLLDLVRK 187
Cdd:pfam13558 32 GLSGGEKQLLaylplaaALAAQYGSAegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
40-207 |
4.13e-04 |
|
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: 40.72 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 40 IVGHNGSGKSTIAKLMigienvkSGEIF-----YNNQTITDDNFEKLRKDIGIVFQnpdnqFVGSIVKYDV--AFGLEnh 112
Cdd:cd03279 33 ICGPTGAGKSTILDAI-------TYALYgktprYGRQENLRSVFAPGEDTAEVSFT-----FQLGGKKYRVerSRGLD-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 113 avpHDEMHRRVSEALKQVDMLERADYEpnALSGGQKQRVAIASVLALNPSV----------IILDEATSMLDPDARQNLL 182
Cdd:cd03279 99 ---YDQFTRIVLLPQGEFDRFLARPVS--TLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVA 173
|
170 180
....*....|....*....|....*..
gi 613389154 183 DLVRKVKSEhNITIISITH--DLSEAM 207
Cdd:cd03279 174 TALELIRTE-NRMVGVISHveELKERI 199
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
40-187 |
4.99e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 40.32 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 40 IVGHNGSGKSTIaklmigienvksgeiFYNNQTITDDNFEKLRKD------------------IGIVFQNPDNQFVgsiv 101
Cdd:cd03272 28 VVGRNGSGKSNF---------------FAAIRFVLSDEYTHLREEqrqallhegsgpsvmsayVEIIFDNSDNRFP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 102 kydvafglenhaVPHDEMHRRVSEALKQ---------------VDMLERA--------------------------DYEP 140
Cdd:cd03272 89 ------------IDKEEVRLRRTIGLKKdeyfldkknvtkndvMNLLESAgfsrsnpyyivpqgkinsltnmkqdeQQEM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613389154 141 NALSGGQKQRVAIASVLALN----PSVIILDEATSMLDPDARQNLLDLVRK 187
Cdd:cd03272 157 QQLSGGQKSLVALALIFAIQkcdpAPFYLFDEIDAALDAQYRTAVANMIKE 207
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
38-201 |
7.98e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.21 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 38 TSIVGHNGSGKSTIA---KLMIGIENVKSgeifyNNQTITDDNFEKLRKDIG-----IVFQNpDNQFVGSivkydvafgl 109
Cdd:cd03239 25 NAIVGPNGSGKSNIVdaiCFVLGGKAAKL-----RRGSLLFLAGGGVKAGINsasveITFDK-SYFLVLQ---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 110 enhavphdemhrrvsEALKQVdmleradyepnaLSGGQKQRVAIASVLAL---NPS-VIILDEATSMLDPDARQNLLDLV 185
Cdd:cd03239 89 ---------------GKVEQI------------LSGGEKSLSALALIFALqeiKPSpFYVLDEIDAALDPTNRRRVSDMI 141
|
170
....*....|....*.
gi 613389154 186 RKvKSEHNITIISITH 201
Cdd:cd03239 142 KE-MAKHTSQFIVITL 156
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
141-209 |
1.17e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 141 NALSGGQKQRVAIASVLAL---NPSVI-ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA 209
Cdd:pfam02463 1076 DLLSGGEKTLVALALIFAIqkyKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADK 1148
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-209 |
1.87e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 1.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613389154 141 NALSGGQKQRVAIA---SVLALNPSVI-ILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDlSEAMEA 209
Cdd:TIGR02168 1088 SLLSGGEKALTALAllfAIFKVKPAPFcILDEVDAPLDDANVERFANLLKEFS--KNTQFIVITHN-KGTMEV 1157
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-217 |
2.45e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 139 EPNALSGGQKQ------RVAIASVLA--------LNPsvIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS 204
Cdd:PRK02224 778 EPEQLSGGERAlfnlslRCAIYRLLAegiegdapLPP--LILDEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDE 855
|
90
....*....|...
gi 613389154 205 EAMEADHVIVMNK 217
Cdd:PRK02224 856 LVGAADDLVRVEK 868
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-51 |
2.65e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 2.65e-03
10 20
....*....|....*....|....*..
gi 613389154 25 LKDVSFNIPKGQWTSIVGHNGSGKSTI 51
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
95-204 |
3.08e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 95 QFVGSIVKYDVAFGLENHAVPHDEMHRRVSEALKQVDMLERADYE--PNALSGGQKQRVAIASVLAL---NPSVIILDEA 169
Cdd:pfam13304 187 RLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElpAFELSDGTKRLLALLAALLSalpKGGLLLIDEP 266
|
90 100 110
....*....|....*....|....*....|....*
gi 613389154 170 TSMLDPDARQNLLDLVRKvKSEHNITIISITHDLS 204
Cdd:pfam13304 267 ESGLHPKLLRRLLELLKE-LSRNGAQLILTTHSPL 300
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
144-202 |
3.14e-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: 38.87 E-value: 3.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613389154 144 SGGQKQ------RVAIASVLALNPSVIILDEATSMLDPDARQN----LLDLVRKVKSEHNITIISITHD 202
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESlahaLVEIIKSRSQQRNFQLLVITHD 1269
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
27-219 |
5.73e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.28 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 27 DVSFNIPKGqWTSIVGHNGSGKST----IAKLMIGIEN-----------VKSGE--------IFYN-NQTITDDNFEKLR 82
Cdd:COG3950 18 EIDFDNPPR-LTVLVGENGSGKTTlleaIALALSGLLSrlddvkfrkllIRNGEfgdsakliLYYGtSRLLLDGPLKKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 83 KDIGIVFQNPDN------------QFVGSIVKYDVAFGLENHAvPHDEMHRRVSEALKQV---------------DMLER 135
Cdd:COG3950 97 RLKEEYFSRLDGydslldedsnlrEFLEWLREYLEDLENKLSD-ELDEKLEAVREALNKLlpdfkdiridrdpgrLVILD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613389154 136 AD---YEPNALSGGQKQRVAIASVLALN--------------PSVIILDEatsmLD----PDARQNLLDLVRKVksEHNI 194
Cdd:COG3950 176 KNgeeLPLNQLSDGERSLLALVGDLARRlaelnpalenplegEGIVLIDE----IDlhlhPKWQRRILPDLRKI--FPNI 249
|
250 260
....*....|....*....|....*..
gi 613389154 195 TIISITHD--LSEAMEADHVIVMNKGT 219
Cdd:COG3950 250 QFIVTTHSplILSSLEDEEVIVLERDE 276
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
146-202 |
5.86e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 5.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 613389154 146 GQKQRVAIASVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHD 211
|
|
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