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Conserved domains on  [gi|90994562|ref|YP_537052|]
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acetyl-CoA carboxylase carboxyltransferase alpha subunit (chloroplast) [Neopyropia yezoensis]

Protein Classification

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha( domain architecture ID 10000156)

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha is a component of the acetyl coenzyme A carboxylase (ACC) complex; first, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA

EC:  2.1.3.15
Gene Ontology:  GO:0003989|GO:0016743|GO:0006633|GO:0009317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 3-324 0e+00

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


:

Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 607.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    3 TSNRKPIVPDFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIP 82
Cdd:CHL00198   1 MSNRKPHVPDFMKPLAELESQVEELSKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   83 GILDEWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTF 162
Cdd:CHL00198  81 YILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  163 IDTPGAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKN 242
Cdd:CHL00198 161 IDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  243 SKESLAAAEALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFY 322
Cdd:CHL00198 241 SKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGAFY 320


                 ..
gi 90994562  323 EI 324
Cdd:CHL00198 321 EI 322
 
Name Accession Description Interval E-value
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 3-324 0e+00

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 607.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    3 TSNRKPIVPDFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIP 82
Cdd:CHL00198   1 MSNRKPHVPDFMKPLAELESQVEELSKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   83 GILDEWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTF 162
Cdd:CHL00198  81 YILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  163 IDTPGAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKN 242
Cdd:CHL00198 161 IDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  243 SKESLAAAEALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFY 322
Cdd:CHL00198 241 SKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGAFY 320


                 ..
gi 90994562  323 EI 324
Cdd:CHL00198 321 EI 322
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 12-323 1.84e-171

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: 477.99  E-value: 1.84e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  12 DFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILDEWIEL 91
Cdd:COG0825   4 DFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDFIEL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  92 HGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTFIDTPGAWAG 171
Cdd:COG0825  84 HGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGAYPG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562 172 LKAEELGQGEAIAVNLREMFSFEVPIVCTIIgeggsggalgigigDSILMLEYAIYTVATPEACAAILWKNSKESLAAAE 251
Cdd:COG0825 164 IGAEERGQSEAIARNLREMARLKVPIISVVIgeggsggalaigvgDRVLMLEHSIYSVISPEGCASILWKDASKAPEAAE 243

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90994562 252 ALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFYE 323
Cdd:COG0825 244 ALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRFLE 315
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 12-321 1.37e-145

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: 412.66  E-value: 1.37e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    12 DFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILDEWIEL 91
Cdd:TIGR00513   7 DFEKPIAELEAKIESLRARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIFDDFFEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    92 HGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTFIDTPGAWAG 171
Cdd:TIGR00513  87 AGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFIDTPGAYPG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   172 LKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKNSKESLAAAE 251
Cdd:TIGR00513 167 IGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDASKAPKAAE 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   252 ALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAF 321
Cdd:TIGR00513 247 AMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
AccA_sub NF041504
carboxyltransferase subunit alpha;
64-319 6.60e-122

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 350.22  E-value: 6.60e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   64 QRLHLVRQSERPTTLDYIPGILDEWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYR 143
Cdd:NF041504   2 QKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  144 KALRLMKHANRFGMPILTFIDTPGAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLE 223
Cdd:NF041504  82 KALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLMLE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  224 YAIYTVATPEACAAILWKNSKESLAAAEALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLD 303
Cdd:NF041504 162 HAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGLS 241

                        250
                 ....*....|....*.
gi 90994562  304 SQTLKKRRYEKFRRMG 319
Cdd:NF041504 242 ADELIAQRREKFLAMG 257
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 12-152 7.59e-75

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: 226.52  E-value: 7.59e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    12 DFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILDEWIEL 91
Cdd:pfam03255   3 DFEKPIAELEAKIEELRKLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFIEL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90994562    92 HGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHA 152
Cdd:pfam03255  83 HGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLA 143
 
Name Accession Description Interval E-value
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 3-324 0e+00

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 607.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    3 TSNRKPIVPDFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIP 82
Cdd:CHL00198   1 MSNRKPHVPDFMKPLAELESQVEELSKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   83 GILDEWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTF 162
Cdd:CHL00198  81 YILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  163 IDTPGAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKN 242
Cdd:CHL00198 161 IDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWKD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  243 SKESLAAAEALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFY 322
Cdd:CHL00198 241 SKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGAFY 320


                 ..
gi 90994562  323 EI 324
Cdd:CHL00198 321 EI 322
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 12-323 1.84e-171

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: 477.99  E-value: 1.84e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  12 DFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILDEWIEL 91
Cdd:COG0825   4 DFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDFIEL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  92 HGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTFIDTPGAWAG 171
Cdd:COG0825  84 HGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIITFIDTPGAYPG 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562 172 LKAEELGQGEAIAVNLREMFSFEVPIVCTIIgeggsggalgigigDSILMLEYAIYTVATPEACAAILWKNSKESLAAAE 251
Cdd:COG0825 164 IGAEERGQSEAIARNLREMARLKVPIISVVIgeggsggalaigvgDRVLMLEHSIYSVISPEGCASILWKDASKAPEAAE 243

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90994562 252 ALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFYE 323
Cdd:COG0825 244 ALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRFLE 315
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 12-323 2.12e-169

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 473.09  E-value: 2.12e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   12 DFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILDEWIEL 91
Cdd:PRK05724   7 DFEKPIAELEAKIEELRAVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELLFTDFTEL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   92 HGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTFIDTPGAWAG 171
Cdd:PRK05724  87 HGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIITFIDTPGAYPG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  172 LKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKNSKESLAAAE 251
Cdd:PRK05724 167 IGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWKDASKAPEAAE 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90994562  252 ALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFYE 323
Cdd:PRK05724 247 AMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRFLE 318
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 12-321 1.37e-145

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: 412.66  E-value: 1.37e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    12 DFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILDEWIEL 91
Cdd:TIGR00513   7 DFEKPIAELEAKIESLRARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIFDDFFEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    92 HGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTFIDTPGAWAG 171
Cdd:TIGR00513  87 AGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITFIDTPGAYPG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   172 LKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKNSKESLAAAE 251
Cdd:TIGR00513 167 IGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKDASKAPKAAE 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   252 ALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAF 321
Cdd:TIGR00513 247 AMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLGYF 316
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 7-323 5.37e-138

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 397.78  E-value: 5.37e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    7 KPIVPDFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILD 86
Cdd:PLN03230  72 KPVTLPFEKPIVDLENRIDEVRELANKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   87 EWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTFIDTP 166
Cdd:PLN03230 152 KWVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFVDTP 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  167 GAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKNSKES 246
Cdd:PLN03230 232 GAYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSAAAA 311

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90994562  247 LAAAEALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFYE 323
Cdd:PLN03230 312 PKAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIGEFDE 388
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 7-323 5.59e-122

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 367.64  E-value: 5.59e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    7 KPIVPDFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILD 86
Cdd:PLN03229  93 KPVTLDFEKPLVDLEKKIVDVRKMANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRPTFLDHIFNITD 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   87 EWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHANRFGMPILTFIDTP 166
Cdd:PLN03229 173 KFVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTP 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  167 GAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYAIYTVATPEACAAILWKNSKES 246
Cdd:PLN03229 253 GAYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSAKAA 332

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90994562  247 LAAAEALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLDSQTLKKRRYEKFRRMGAFYE 323
Cdd:PLN03229 333 PKAAEKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHRMLKFRKIGGFQE 409
AccA_sub NF041504
carboxyltransferase subunit alpha;
64-319 6.60e-122

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 350.22  E-value: 6.60e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   64 QRLHLVRQSERPTTLDYIPGILDEWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYR 143
Cdd:NF041504   2 QKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  144 KALRLMKHANRFGMPILTFIDTPGAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLE 223
Cdd:NF041504  82 KALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLMLE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  224 YAIYTVATPEACAAILWKNSKESLAAAEALKITSHDLKVLGIVDEILQEPLGGAQADPYTASQYLKKELTEQLDSLSKLD 303
Cdd:NF041504 162 HAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEALAELAGLS 241

                        250
                 ....*....|....*.
gi 90994562  304 SQTLKKRRYEKFRRMG 319
Cdd:NF041504 242 ADELIAQRREKFLAMG 257
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 66-317 3.67e-83

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 252.00  E-value: 3.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562   66 LHLVRQSERPTTLDYIPGILDEWIELHGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKA 145
Cdd:PRK12319   8 LKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPEGYRKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  146 LRLMKHANRFGMPILTFIDTPGAWAGLKAEELGQGEAIAVNLREMFSFEVPIVCTIIGEGGSGGALGIGIGDSILMLEYA 225
Cdd:PRK12319  88 LRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVWMLENT 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  226 IYTVATPEACAAILWKNSKESLAAAEALKITSHDLKVLGIVDEILQEplggaqaDPYTAS---QYLKKELTEQLDSLSKL 302
Cdd:PRK12319 168 MYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPE-------HGYFSSeiiDMIKKNLIEELAQLSQK 240

                        250
                 ....*....|....*
gi 90994562  303 DSQTLKKRRYEKFRR 317
Cdd:PRK12319 241 PLEQLLEERYQRFRK 255
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 12-152 7.59e-75

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: 226.52  E-value: 7.59e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    12 DFMRPVAELEGQVEELKKLAPKNDIIINNKIARFQNQLVKLQKEIFSSLTPLQRLHLVRQSERPTTLDYIPGILDEWIEL 91
Cdd:pfam03255   3 DFEKPIAELEAKIEELRKLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFIEL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90994562    92 HGDRGGADDPALVGGIGKINGRNIVFIGHQRGRGTKENVARNFGMPAPGGYRKALRLMKHA 152
Cdd:pfam03255  83 HGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLA 143
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 81-202 3.50e-04

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: 42.25  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562    81 IPGILD--EWIELHGDRGgaddPALVGGIGKINGRNIVFIGHQRGRGTkenvarnfGMPAPGGYRKALRLMKHANRFGMP 158
Cdd:pfam01039 262 IAGIVDegEFFEIKPGYA----KTVVTGFARLGGIPVGVVANQPRVGA--------GVLFPDSADKAARFIRDCDAFNLP 329

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 90994562   159 ILTFIDTPGAWAGLKAEE---LGQGEAIAVNLREmfsFEVPIVcTII 202
Cdd:pfam01039 330 LVILADVPGFLPGQRQEYggiLKHGAKLLYALAE---ATVPKI-TVI 372
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
85-168 1.43e-03

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 40.01  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90994562  85 LDE--WIEL-----HGDRGGADDPA---LVGGIGKINGRnIVFIghqrgrgtkenVARNF----GMPAPGGYRKALRLMK 150
Cdd:COG4799  44 LDPgsFLELgalagHRMYDDDDRVPgdgVVTGIGTVDGR-PVVV-----------VANDFtvkgGSLGPMTAKKILRAQD 111

                        90
                ....*....|....*...
gi 90994562 151 HANRFGMPILTFIDTPGA 168
Cdd:COG4799 112 IALENGLPVIYLVDSGGA 129
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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