|
Name |
Accession |
Description |
Interval |
E-value |
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
5-315 |
0e+00 |
|
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440587 [Multi-domain] Cd Length: 315 Bit Score: 649.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 5 YLDFELPIAELEAKIEALRS-ASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIFTDFQ 83
Cdd:COG0825 2 YLDFEKPIAELEAKIEELRAlAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 84 ELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDTPGAY 163
Cdd:COG0825 82 ELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGAY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 164 PGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTA 243
Cdd:COG0825 162 PGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPEA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491967586 244 AEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYGYC 315
Cdd:COG0825 242 AEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
1-315 |
0e+00 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 637.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 1 MSQEYLDFELPIAELEAKIEALRS-ASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIF 79
Cdd:PRK05724 1 MMLNYLDFEKPIAELEAKIEELRAvAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 80 TDFQELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDT 159
Cdd:PRK05724 81 TDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITFIDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 160 PGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEK 239
Cdd:PRK05724 161 PGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKDASK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491967586 240 ASTAAEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYGYC 315
Cdd:PRK05724 241 APEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316
|
|
| accA |
TIGR00513 |
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ... |
1-315 |
0e+00 |
|
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273113 [Multi-domain] Cd Length: 316 Bit Score: 567.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 1 MSQEYLDFELPIAELEAKIEALRSAS-DDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIF 79
Cdd:TIGR00513 1 MMANYLDFEKPIAELEAKIESLRARSrDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 80 TDFQELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDT 159
Cdd:TIGR00513 81 DDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFIDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 160 PGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEK 239
Cdd:TIGR00513 161 PGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDASK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491967586 240 ASTAAEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYGYC 315
Cdd:TIGR00513 241 APKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
|
|
| AccA_sub |
NF041504 |
carboxyltransferase subunit alpha; |
57-308 |
2.43e-159 |
|
carboxyltransferase subunit alpha;
Pssm-ID: 469391 [Multi-domain] Cd Length: 257 Bit Score: 444.59 E-value: 2.43e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 57 WQVSRMARHPNRPYTLDYIEHIFTDFQELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGY 136
Cdd:NF041504 1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 137 RKALRLMQMAERFNLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNML 216
Cdd:NF041504 81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 217 QYSTYSVISPEGCASILWKSAEKASTAAEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTF 296
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240
|
250
....*....|..
gi 491967586 297 DKDGLLERRYER 308
Cdd:NF041504 241 SADELIAQRREK 252
|
|
| ACCA |
pfam03255 |
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ... |
5-147 |
4.10e-95 |
|
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A carboxylase carboxyltransferase is composed of an alpha and beta subunit.
Pssm-ID: 427221 [Multi-domain] Cd Length: 144 Bit Score: 277.75 E-value: 4.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 5 YLDFELPIAELEAKIEALRS-ASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIFTDFQ 83
Cdd:pfam03255 1 YLDFEKPIAELEAKIEELRKlAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491967586 84 ELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAE 147
Cdd:pfam03255 81 ELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
5-315 |
0e+00 |
|
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440587 [Multi-domain] Cd Length: 315 Bit Score: 649.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 5 YLDFELPIAELEAKIEALRS-ASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIFTDFQ 83
Cdd:COG0825 2 YLDFEKPIAELEAKIEELRAlAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 84 ELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDTPGAY 163
Cdd:COG0825 82 ELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGAY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 164 PGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTA 243
Cdd:COG0825 162 PGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWKDASKAPEA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491967586 244 AEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYGYC 315
Cdd:COG0825 242 AEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
1-315 |
0e+00 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 637.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 1 MSQEYLDFELPIAELEAKIEALRS-ASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIF 79
Cdd:PRK05724 1 MMLNYLDFEKPIAELEAKIEELRAvAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 80 TDFQELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDT 159
Cdd:PRK05724 81 TDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITFIDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 160 PGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEK 239
Cdd:PRK05724 161 PGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKDASK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491967586 240 ASTAAEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYGYC 315
Cdd:PRK05724 241 APEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316
|
|
| accA |
TIGR00513 |
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ... |
1-315 |
0e+00 |
|
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273113 [Multi-domain] Cd Length: 316 Bit Score: 567.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 1 MSQEYLDFELPIAELEAKIEALRSAS-DDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIF 79
Cdd:TIGR00513 1 MMANYLDFEKPIAELEAKIESLRARSrDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 80 TDFQELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDT 159
Cdd:TIGR00513 81 DDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFIDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 160 PGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEK 239
Cdd:TIGR00513 161 PGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDASK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491967586 240 ASTAAEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYGYC 315
Cdd:TIGR00513 241 APKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
|
|
| AccA_sub |
NF041504 |
carboxyltransferase subunit alpha; |
57-308 |
2.43e-159 |
|
carboxyltransferase subunit alpha;
Pssm-ID: 469391 [Multi-domain] Cd Length: 257 Bit Score: 444.59 E-value: 2.43e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 57 WQVSRMARHPNRPYTLDYIEHIFTDFQELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGY 136
Cdd:NF041504 1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 137 RKALRLMQMAERFNLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNML 216
Cdd:NF041504 81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 217 QYSTYSVISPEGCASILWKSAEKASTAAEVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTF 296
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGL 240
|
250
....*....|..
gi 491967586 297 DKDGLLERRYER 308
Cdd:NF041504 241 SADELIAQRREK 252
|
|
| accA |
CHL00198 |
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional |
6-314 |
3.14e-134 |
|
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
Pssm-ID: 214393 [Multi-domain] Cd Length: 322 Bit Score: 383.78 E-value: 3.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 6 LDFELPIAELEAKIEAL-RSASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIFTDFQE 84
Cdd:CHL00198 9 PDFMKPLAELESQVEELsKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIPYILDEWIE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 85 LAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDTPGAYP 164
Cdd:CHL00198 89 LHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTFIDTPGAWA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 165 GIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTAA 244
Cdd:CHL00198 169 GVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKDSKKSLDAA 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 245 EVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYGY 314
Cdd:CHL00198 249 EALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGA 318
|
|
| PLN03230 |
PLN03230 |
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional |
6-313 |
8.33e-120 |
|
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
Pssm-ID: 178769 [Multi-domain] Cd Length: 431 Bit Score: 351.17 E-value: 8.33e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 6 LDFELPIAELEAKIEALRS-ASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIFTDFQE 84
Cdd:PLN03230 76 LPFEKPIVDLENRIDEVRElANKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTDKWVE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 85 LAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDTPGAYP 164
Cdd:PLN03230 156 LHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPGAYA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 165 GIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTAA 244
Cdd:PLN03230 236 GIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSAAAAPKAA 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491967586 245 EVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERRYERLMSYG 313
Cdd:PLN03230 316 EALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIG 384
|
|
| PRK12319 |
PRK12319 |
acetyl-CoA carboxylase subunit alpha; Provisional |
55-312 |
1.97e-114 |
|
acetyl-CoA carboxylase subunit alpha; Provisional
Pssm-ID: 183435 [Multi-domain] Cd Length: 256 Bit Score: 330.97 E-value: 1.97e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 55 DAWQVSRMARHPNRPYTLDYIEHIFTDFQELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPE 134
Cdd:PRK12319 3 DVARILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 135 GYRKALRLMQMAERFNLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVN 214
Cdd:PRK12319 83 GYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 215 MLQYSTYSVISPEGCASILWKSAEKASTAAEVMGLTAARLKELGLIDNIVPEplggAHRNYHEMARNLKHCLVEELNELD 294
Cdd:PRK12319 163 MLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPE----HGYFSSEIIDMIKKNLIEELAQLS 238
|
250
....*....|....*...
gi 491967586 295 TFDKDGLLERRYERLMSY 312
Cdd:PRK12319 239 QKPLEQLLEERYQRFRKY 256
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
6-305 |
1.19e-106 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 327.58 E-value: 1.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 6 LDFELPIAELEAKI-EALRSASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIFTDFQE 84
Cdd:PLN03229 97 LDFEKPLVDLEKKIvDVRKMANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRPTFLDHIFNITDKFVE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 85 LAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAERFNLPIITFIDTPGAYP 164
Cdd:PLN03229 177 LHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPGAYA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 165 GIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSAEKASTAA 244
Cdd:PLN03229 257 DLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAKAAPKAA 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491967586 245 EVMGLTAARLKELGLIDNIVPEPLGGAHRNYHEMARNLKHCLVEELNELDTFDKDGLLERR 305
Cdd:PLN03229 337 EKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHR 397
|
|
| ACCA |
pfam03255 |
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ... |
5-147 |
4.10e-95 |
|
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A carboxylase carboxyltransferase is composed of an alpha and beta subunit.
Pssm-ID: 427221 [Multi-domain] Cd Length: 144 Bit Score: 277.75 E-value: 4.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 5 YLDFELPIAELEAKIEALRS-ASDDKIDLHDEIKRLQKKSDELTKKTFANLDAWQVSRMARHPNRPYTLDYIEHIFTDFQ 83
Cdd:pfam03255 1 YLDFEKPIAELEAKIEELRKlAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491967586 84 ELAGDRAFADDKAIVGGLARLDGRAVMVIGHQKGRTVKDKVTRNFGMPAPEGYRKALRLMQMAE 147
Cdd:pfam03255 81 ELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLAE 144
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
66-260 |
9.47e-16 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 77.30 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 66 PNRPYTL-DYIEHIFT--DFQELAGDRAfaddKAIVGGLARLDGRAVMVIGHQkgrtvkdkvTRNF-GMPAPEGYRKALR 141
Cdd:pfam01039 252 PKKPYDVrEVIAGIVDegEFFEIKPGYA----KTVVTGFARLGGIPVGVVANQ---------PRVGaGVLFPDSADKAAR 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 142 LMQMAERFNLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAIG----VGDKVNMLQ 217
Cdd:pfam01039 319 FIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskinGADINFAWP 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491967586 218 YSTYSVISPEGCASILWKSAEKAST------AAEVMGLTAARLKELGLI 260
Cdd:pfam01039 399 TARIAVMGPEGAVEIKFRKEKAAAEmrgkdlAATRKQKIAEYEEELSPP 447
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
66-265 |
5.88e-14 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 71.98 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 66 PNRPY-TLDYIEHIF--TDFQELAGDRAfaddKAIVGGLARLDGRAVMVIGHQkgrtvkdkvtrnfgmPA-------PEG 135
Cdd:COG4799 274 PRKPYdMREVIARLVdgGSFFEFKPLYG----PNIVTGFARIDGRPVGIVANQ---------------PMvlagvldIDA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 136 YRKALRLMQMAERFNLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIGeGGSGGAlAIGVGDKvnm 215
Cdd:COG4799 335 ADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILR-KAYGAG-YYAMCGK--- 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 216 lQYST----------YSVISPEGCASILWKSA-EKASTAAEVMGLTAARLKE---------LGLIDNIVP 265
Cdd:COG4799 410 -ALGPdflfawptaeIAVMGGEGAANVLYRRElAAAEDPEALRAELIAEYEEqanpyyaaaRGWIDDVID 478
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
82-204 |
5.39e-09 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 56.96 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 82 FQE---LAGDRAFADDK-----AIVGGLARLDGRAVMVIGHQKgrTVKDkvtrnfGMPAPEGYRKALRLMQMAERFNLPI 153
Cdd:COG4799 49 FLElgaLAGHRMYDDDDrvpgdGVVTGIGTVDGRPVVVVANDF--TVKG------GSLGPMTAKKILRAQDIALENGLPV 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491967586 154 ITFIDTPGAYPGIGAEERGQSEAIARNLREMStLKVPVICTVIGEGGSGGA 204
Cdd:COG4799 121 IYLVDSGGARLQEGVESFAGYGRIFYRNARSS-GGIPQISVIMGPCAAGGA 170
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
62-217 |
2.46e-06 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 48.65 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 62 MARHPNRPYTL--DYIEHI------FTDFQELAGDRAFADD---KAIVGGLARLDGRAVMVIGHQKgrTVKDkvtrnfGM 130
Cdd:PLN02820 73 VKRHRSRNKLLprERIDRLldpgspFLELSQLAGHELYGEDlpsGGIVTGIGPVHGRLCMFVANDP--TVKG------GT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 131 PAPEGYRKALRLMQMAERFNLPIITFIDTPGAYPGIGAE---ERGQSEAIARNLREMSTLKVPVICTVIGEGGSGGALAI 207
Cdd:PLN02820 145 YYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEvfpDRDHFGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVP 224
|
170
....*....|
gi 491967586 208 GVGDKVNMLQ 217
Cdd:PLN02820 225 AMADESVIVK 234
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
69-277 |
5.67e-06 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 47.64 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 69 PYTLDyiEHIFTDFQELAGDRA-------FADDkAIVGGLARLDGRAVMVIGHQKgrTVkdkvtrnFGMPAPEGY-RKAL 140
Cdd:pfam01039 15 DLLLD--PGSFGELEDLFFHRAtefgrkrIPRD-GVVTGSGAVIGRAVEVVAQDF--TV-------FGGSLGPAKgEKIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 141 RLMQMAERFNLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMSTlKVPVICTVIGEGGSGGALAIGVGDKVNMlqyst 220
Cdd:pfam01039 83 RAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVIM----- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491967586 221 ysvispegcasilwksAEKASTaaevMGLTAARLKELGLIDNIVPEPLGGAHRNYHE 277
Cdd:pfam01039 157 ----------------VEGTSP----MFLTGPPVIKKVTGEEVTSEELGGATQHMTI 193
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
79-204 |
1.37e-03 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 40.18 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491967586 79 FTDFQELAGDrafaddkAIVGGLARLDGRAVMVIGhqkgrtvkdkvtrNFGMPAPEGYRKALRLMQMAERFNLPIITFID 158
Cdd:PLN02820 350 FDEFKKNYGT-------TLVTGFARIYGQPVGIIG-------------NNGILFTESALKGAHFIELCAQRGIPLLFLQN 409
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 491967586 159 TPGAYPGIGAEERGQSEAIARNLREMSTLKVPVICTVIgeGGSGGA 204
Cdd:PLN02820 410 ITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITIIV--GGSFGA 453
|
|
|