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Conserved domains on  [gi|491967586|ref|WP_005697172|]
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MULTISPECIES: acetyl-CoA carboxylase carboxyl transferase subunit alpha [Haemophilus]

Protein Classification

AccA family protein( domain architecture ID 10002787)

AccA family protein

Graphical summary

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List of domain hits

 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
 
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
 
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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