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Conserved domains on  [gi|489736323|ref|WP_003640418|]
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MULTISPECIES: carboxyltransferase subunit alpha [Lactiplantibacillus]

Protein Classification

acetyl-CoA carboxylase carboxyltransferase subunit alpha( domain architecture ID 10002787)

acetyl-CoA carboxylase carboxyltransferase subunit alpha (AccA) is a component of the acetyl coenzyme A carboxylase (ACC) complex that catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA

CATH:  3.90.226.10
EC:  2.1.3.15
Gene Ontology:  GO:0003989|GO:0005524|GO:0016743|GO:0006633|GO:0005524|GO:0009317
PubMed:  1355089
SCOP:  4000456

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
AccA_sub NF041504
carboxyltransferase subunit alpha;
7-256 1.16e-131

carboxyltransferase subunit alpha;


:

Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 372.17  E-value: 1.16e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   7 YEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCATPSGY 86
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  87 RKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGDQVWML 166
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 167 ANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE------VATAADCQPLKTAIDETLTALTAK 240
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEplggahRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|....*.
gi 489736323 241 SVTELVTQRQARYRQF 256
Cdd:NF041504 241 SADELIAQRREKFLAM 256
 
Name Accession Description Interval E-value
AccA_sub NF041504
carboxyltransferase subunit alpha;
7-256 1.16e-131

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 372.17  E-value: 1.16e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   7 YEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCATPSGY 86
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  87 RKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGDQVWML 166
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 167 ANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE------VATAADCQPLKTAIDETLTALTAK 240
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEplggahRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|....*.
gi 489736323 241 SVTELVTQRQARYRQF 256
Cdd:NF041504 241 SADELIAQRREKFLAM 256
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 2-256 2.66e-117

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: 338.17  E-value: 2.66e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:COG0825   50 SNLTPWQKVQLARHPQRPYTLDYIEAIFTDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:COG0825  130 HPEGYRKALRLMKLAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGD 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE--------VATAADCqpLKTAIDET 233
Cdd:COG0825  210 RVLMLEHSIYSVISPEGCASILWKDASKAPEAAEALKITAQDLKELGIIDEIIPEplggahrdPEAAAEN--LKEALLKA 287

                        250       260
                 ....*....|....*....|...
gi 489736323 234 LTALTAKSVTELVTQRQARYRQF 256
Cdd:COG0825  288 LKELKGLSPEELLEQRYEKFRAI 310
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 2-256 1.04e-107

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 314.00  E-value: 1.04e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:PRK05724  53 SNLTPWQKVQLARHPQRPYTLDYIELLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:PRK05724 133 RPEGYRKALRLMKMAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGD 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE--------VATAAdcQPLKTAIDET 233
Cdd:PRK05724 213 RVLMLEYSTYSVISPEGCASILWKDASKAPEAAEAMKITAQDLKELGIIDEIIPEplggahrdPEAAA--AALKEALLEA 290

                        250       260
                 ....*....|....*....|...
gi 489736323 234 LTALTAKSVTELVTQRQARYRQF 256
Cdd:PRK05724 291 LAELKGLSPEELLERRYEKFMSI 313
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 2-256 5.26e-89

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: 266.29  E-value: 5.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323    2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:TIGR00513  53 SNLGAWQRLQLARHPDRPYTLDYIELIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:TIGR00513 133 APEGYRKALRLMKMAERFKMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGD 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPEVATAADCQP------LKTAIDETLT 235
Cdd:TIGR00513 213 KVNMLEYSTYSVISPEGCAAILWKDASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPlaaaasLKEQLLADLA 292

                         250       260
                  ....*....|....*....|.
gi 489736323  236 ALTAKSVTELVTQRQARYRQF 256
Cdd:TIGR00513 293 TLDQLSTEELKNRRYQKLMSL 313
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 2-97 1.26e-39

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: 134.07  E-value: 1.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323    2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:pfam03255  49 SNLTPWQKVQLARHPERPYTLDYIEALFDDFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMP 128

                          90
                  ....*....|....*.
gi 489736323   82 TPSGYRKALRLMRQAE 97
Cdd:pfam03255 129 HPEGYRKALRLMKLAE 144
 
Name Accession Description Interval E-value
AccA_sub NF041504
carboxyltransferase subunit alpha;
7-256 1.16e-131

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 372.17  E-value: 1.16e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   7 YEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCATPSGY 86
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  87 RKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGDQVWML 166
Cdd:NF041504  81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 167 ANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE------VATAADCQPLKTAIDETLTALTAK 240
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEplggahRDPAALIAALGDAIEEALAELAGL 240

                        250
                 ....*....|....*.
gi 489736323 241 SVTELVTQRQARYRQF 256
Cdd:NF041504 241 SADELIAQRREKFLAM 256
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 2-256 2.66e-117

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: 338.17  E-value: 2.66e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:COG0825   50 SNLTPWQKVQLARHPQRPYTLDYIEAIFTDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:COG0825  130 HPEGYRKALRLMKLAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGD 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE--------VATAADCqpLKTAIDET 233
Cdd:COG0825  210 RVLMLEHSIYSVISPEGCASILWKDASKAPEAAEALKITAQDLKELGIIDEIIPEplggahrdPEAAAEN--LKEALLKA 287

                        250       260
                 ....*....|....*....|...
gi 489736323 234 LTALTAKSVTELVTQRQARYRQF 256
Cdd:COG0825  288 LKELKGLSPEELLEQRYEKFRAI 310
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 2-256 1.04e-107

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 314.00  E-value: 1.04e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:PRK05724  53 SNLTPWQKVQLARHPQRPYTLDYIELLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:PRK05724 133 RPEGYRKALRLMKMAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGD 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE--------VATAAdcQPLKTAIDET 233
Cdd:PRK05724 213 RVLMLEYSTYSVISPEGCASILWKDASKAPEAAEAMKITAQDLKELGIIDEIIPEplggahrdPEAAA--AALKEALLEA 290

                        250       260
                 ....*....|....*....|...
gi 489736323 234 LTALTAKSVTELVTQRQARYRQF 256
Cdd:PRK05724 291 LAELKGLSPEELLERRYEKFMSI 313
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 1-256 1.32e-102

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 298.61  E-value: 1.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   1 MSKVTayEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGC 80
Cdd:PRK12319   1 MTDVA--RILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  81 ATPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACG 160
Cdd:PRK12319  79 PHPEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 161 DQVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPE--VATAADCQPLKTAIDETLTALT 238
Cdd:PRK12319 159 DQVWMLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPEhgYFSSEIIDMIKKNLIEELAQLS 238

                        250
                 ....*....|....*...
gi 489736323 239 AKSVTELVTQRQARYRQF 256
Cdd:PRK12319 239 QKPLEQLLEERYQRFRKY 256
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 2-256 5.26e-89

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: 266.29  E-value: 5.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323    2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:TIGR00513  53 SNLGAWQRLQLARHPDRPYTLDYIELIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:TIGR00513 133 APEGYRKALRLMKMAERFKMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGD 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPEVATAADCQP------LKTAIDETLT 235
Cdd:TIGR00513 213 KVNMLEYSTYSVISPEGCAAILWKDASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPlaaaasLKEQLLADLA 292

                         250       260
                  ....*....|....*....|.
gi 489736323  236 ALTAKSVTELVTQRQARYRQF 256
Cdd:TIGR00513 293 TLDQLSTEELKNRRYQKLMSL 313
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 2-255 3.59e-80

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 243.95  E-value: 3.59e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:CHL00198  56 YSLTPLQRLHLVRQSERPTTLDYIPYILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:CHL00198 136 SPGGYRKALRLMKHANKFGLPILTFIDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPEVATAADCQP------LKTAIDETLT 235
Cdd:CHL00198 216 SIMMLEYAVYTVATPEACAAILWKDSKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPasaskiLKKKLIRQLD 295

                        250       260
                 ....*....|....*....|
gi 489736323 236 ALTAKSVTELVTQRQARYRQ 255
Cdd:CHL00198 296 FLKILSPSELKAHRYEKFRK 315
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 2-255 2.19e-72

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 227.52  E-value: 2.19e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:PLN03230 123 SRLTPVQRLSVARHPNRPTFLDHVLNMTDKWVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMP 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  82 TPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGD 161
Cdd:PLN03230 203 QPNGYRKALRFMRHAEKFGFPILTFVDTPGAYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGN 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 162 QVWMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPEVATAADCQP------LKTAIDETLT 235
Cdd:PLN03230 283 RMLMMENAVYYVASPEACAAILWKSAAAAPKAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPlqasknIKEVILRHMK 362

                        250       260
                 ....*....|....*....|
gi 489736323 236 ALTAKSVTELVTQRQARYRQ 255
Cdd:PLN03230 363 ELMKMDPEELLQDRAAKFRK 382
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 4-255 3.92e-72

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 234.75  E-value: 3.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   4 VTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCATP 83
Cdd:PLN03229 146 LTPIQRVNIARHPNRPTFLDHIFNITDKFVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTP 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  84 SGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALACGDQV 163
Cdd:PLN03229 226 HGYRKALRMMYYADHHGFPIVTFIDTPGAYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKL 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 164 WMLANSTYSVLSPEGYATILWKESQRAAEAAEKMRLTPTELLADGIIDRIIPEVATAADCQP------LKTAIDETLTAL 237
Cdd:PLN03229 306 LMLENAVFYVASPEACAAILWKSAKAAPKAAEKLRITAQELCRLQIADGIIPEPLGGAHADPswtsqqIKIAINENMDEL 385

                        250
                 ....*....|....*...
gi 489736323 238 TAKSVTELVTQRQARYRQ 255
Cdd:PLN03229 386 GKMDTEELLKHRMLKFRK 403
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 2-97 1.26e-39

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: 134.07  E-value: 1.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323    2 SKVTAYEQVQAARDASKISIQTLIDGLTEDFFDCHGDRQRADDPAVIAGLATIAQRPVTIIGIQKGQNLAENQARHFGCA 81
Cdd:pfam03255  49 SNLTPWQKVQLARHPERPYTLDYIEALFDDFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMP 128

                          90
                  ....*....|....*.
gi 489736323   82 TPSGYRKALRLMRQAE 97
Cdd:pfam03255 129 HPEGYRKALRLMKLAE 144
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
21-215 3.62e-18

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 83.15  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  21 IQTLIDGltEDFFDCHGDRqradDPAVIAGLATIAQRPVTIIGiqkgqnlaeNQARHF-GCATPSGYRKALRLMRQAEQL 99
Cdd:COG4799  284 IARLVDG--GSFFEFKPLY----GPNIVTGFARIDGRPVGIVA---------NQPMVLaGVLDIDAADKAARFIRLCDAF 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323 100 RQPVVTLINTPGAYPGVDAEYEGQGRAIADCLLAGLQLRVPFLSLIVGeGGSGGALALACG-----DQVWMLANSTYSVL 174
Cdd:COG4799  349 NIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILR-KAYGAGYYAMCGkalgpDFLFAWPTAEIAVM 427

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489736323 175 SPEGYATILW-KESQRAAEAAEKMR---------LTPTELLADGIIDRIIP 215
Cdd:COG4799  428 GGEGAANVLYrRELAAAEDPEALRAeliaeyeeqANPYYAAARGWIDDVID 478
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 45-212 4.60e-18

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: 83.08  E-value: 4.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323   45 PAVIAGLATIAQRPVTIIGiqkgqnlaeNQARHF-GCATPSGYRKALRLMRQAEQLRQPVVTLINTPGAYPGVDAEYEGQ 123
Cdd:pfam01039 280 KTVVTGFARLGGIPVGVVA---------NQPRVGaGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGI 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  124 GRAIADCLLAGLQLRVPFLSLIVGEGGSGGALALA----CGDQVWMLANSTYSVLSPEGYATILwkeSQRAAEAAEKMRL 199
Cdd:pfam01039 351 LKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskinGADINFAWPTARIAVMGPEGAVEIK---FRKEKAAAEMRGK 427

                         170
                  ....*....|...
gi 489736323  200 TPTELLADGIIDR 212
Cdd:pfam01039 428 DLAATRKQKIAEY 440
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
33-165 8.11e-05

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 43.48  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736323  33 FDCHGDRQRAddPA--VIAGLATIAQRPV-------TIIGiqkgqnlaenqarhfGCATPSGYRKALRLMRQAEQLRQPV 103
Cdd:COG4799   58 HRMYDDDDRV--PGdgVVTGIGTVDGRPVvvvandfTVKG---------------GSLGPMTAKKILRAQDIALENGLPV 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489736323 104 VTLINTPGAYP--GVDAeYEGQGRAIADclLAGLQLRVPFLSLIVGEGGSGGALALACGDQVWM 165
Cdd:COG4799  121 IYLVDSGGARLqeGVES-FAGYGRIFYR--NARSSGGIPQISVIMGPCAAGGAYSPALSDFVIM 181
 
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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