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Conserved domains on  [gi|193786913|dbj|BAG52236|]
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unnamed protein product [Homo sapiens]

Protein Classification

carboxyltransferase domain-containing protein( domain architecture ID 1001328)

carboxyltransferase domain-containing protein catalyzes the transcarboxylation from biotin to an acyl-CoA acceptor molecule; similar to methylcrotonyl-CoA carboxylase subunit beta

CATH:  3.90.226.10
Gene Ontology:  GO:0016740|GO:0009374
PubMed:  8102604

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Carboxyl_trans super family cl47203
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
1-203 1.75e-126

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.


The actual alignment was detected with superfamily member PLN02820:

Pssm-ID: 481543 [Multi-domain]  Cd Length: 569  Bit Score: 369.14  E-value: 1.75e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913   1 MIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTFYNQAIMSSKNIAQIAV 80
Cdd:PLN02820 132 MFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIFYNQARMSSAGIPQIAL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913  81 VMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVV 160
Cdd:PLN02820 212 VLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIGRNIV 291
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 193786913 161 RNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREV 203
Cdd:PLN02820 292 KNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSV 340
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
1-203 1.75e-126

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 369.14  E-value: 1.75e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913   1 MIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTFYNQAIMSSKNIAQIAV 80
Cdd:PLN02820 132 MFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIFYNQARMSSAGIPQIAL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913  81 VMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVV 160
Cdd:PLN02820 212 VLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIGRNIV 291
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 193786913 161 RNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREV 203
Cdd:PLN02820 292 KNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSV 340
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
1-203 6.86e-107

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 316.97  E-value: 6.86e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913   1 MIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFpdrDHFGRTFYNQAiMSSKNIAQIAV 80
Cdd:COG4799   85 VVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGIPQISV 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913  81 VMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVV 160
Cdd:COG4799  161 IMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLL 240
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 193786913 161 RNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREV 203
Cdd:COG4799  241 SYLPSNNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREV 283
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
1-203 2.54e-67

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: 214.81  E-value: 2.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913    1 MIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAylpRQADVFPDRDHFGRTFYNQAIMSSKnIAQIAV 80
Cdd:pfam01039  60 EVVAQDFTVFGGSLGPAKGEKILRAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLASGV-IPQISL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913   81 VMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVV 160
Cdd:pfam01039 136 IMGPCAGGGAYLPALGDFVIMVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWL 215
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 193786913  161 RNLNYQKK---LDVTIEPSEEPLFPADELYGIVGANLKRSFDVREV 203
Cdd:pfam01039 216 SYLPKPAPnnrEPVPIVPTKDPPDRDAPLVSIVPDDPKKPYDVREV 261
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
1-203 1.75e-126

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 369.14  E-value: 1.75e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913   1 MIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTFYNQAIMSSKNIAQIAV 80
Cdd:PLN02820 132 MFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIFYNQARMSSAGIPQIAL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913  81 VMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVV 160
Cdd:PLN02820 212 VLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIGRNIV 291
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 193786913 161 RNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREV 203
Cdd:PLN02820 292 KNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSV 340
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
1-203 6.86e-107

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 316.97  E-value: 6.86e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913   1 MIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFpdrDHFGRTFYNQAiMSSKNIAQIAV 80
Cdd:COG4799   85 VVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGIPQISV 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913  81 VMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVV 160
Cdd:COG4799  161 IMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLL 240
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 193786913 161 RNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREV 203
Cdd:COG4799  241 SYLPSNNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREV 283
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
1-203 2.54e-67

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: 214.81  E-value: 2.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913    1 MIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAylpRQADVFPDRDHFGRTFYNQAIMSSKnIAQIAV 80
Cdd:pfam01039  60 EVVAQDFTVFGGSLGPAKGEKILRAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLASGV-IPQISL 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193786913   81 VMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVV 160
Cdd:pfam01039 136 IMGPCAGGGAYLPALGDFVIMVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWL 215
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 193786913  161 RNLNYQKK---LDVTIEPSEEPLFPADELYGIVGANLKRSFDVREV 203
Cdd:pfam01039 216 SYLPKPAPnnrEPVPIVPTKDPPDRDAPLVSIVPDDPKKPYDVREV 261
 
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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