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Conserved domains on  [gi|957951445|gb|ALQ34200|]
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methylcrotonoyl-CoA carboxylase 2 isoform 2, partial [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 ...
36-358 0e+00

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: 514.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  36 DLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDnEEVP 115
Cdd:PLN02820  37 DRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELYG-EDLP 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 116 GGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTF 195
Cdd:PLN02820 116 SGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 196 YNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDH 275
Cdd:PLN02820 196 YNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDH 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 276 WALDDHHALHLTRKVVRNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKA 349
Cdd:PLN02820 276 FAQDELHALAIGRNIVKNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKK 355

                 ....*....
gi 957951445 350 FYGDTLVTG 358
Cdd:PLN02820 356 NYGTTLVTG 364
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
36-358 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 514.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  36 DLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDnEEVP 115
Cdd:PLN02820  37 DRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELYG-EDLP 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 116 GGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTF 195
Cdd:PLN02820 116 SGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 196 YNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDH 275
Cdd:PLN02820 196 YNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDH 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 276 WALDDHHALHLTRKVVRNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKA 349
Cdd:PLN02820 276 FAQDELHALAIGRNIVKNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKK 355

                 ....*....
gi 957951445 350 FYGDTLVTG 358
Cdd:PLN02820 356 NYGTTLVTG 364
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
48-358 1.66e-153

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 441.77  E-value: 1.66e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  48 QMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYD-NEEVPGGGIITGIGRV 126
Cdd:COG4799    1 AMRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDdDDRVPGDGVVTGIGTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 127 SGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFpdrDHFGRTFYNQAiMSSKNI 206
Cdd:COG4799   80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 207 AQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHL 286
Cdd:COG4799  156 PQISVIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALAL 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 957951445 287 TRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTG 358
Cdd:COG4799  236 ARRLLSYLPSNNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTG 307
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
77-358 7.10e-94

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: 288.77  E-value: 7.10e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445   77 SRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYDN--EEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQL 154
Cdd:pfam01039   4 PRGKLTARERIDLLLDPGS-FGELEDLFFHRATEFgrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  155 RAQEIAMQNRLPCIYLVDSGGAylpRQADVFPDRDHFGRTFYNQAIMSSKnIAQIAVVMGSCTAGGAYVPAMADENIIVR 234
Cdd:pfam01039  83 RAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLASGV-IPQISLIMGPCAGGGAYLPALGDFVIMVE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  235 KQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKK---LDVTIEPSEEPL 311
Cdd:pfam01039 159 GTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPnnrEPVPIVPTKDPP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 957951445  312 FPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTG 358
Cdd:pfam01039 239 DRDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTG 285
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
36-358 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 514.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  36 DLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDnEEVP 115
Cdd:PLN02820  37 DRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELYG-EDLP 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 116 GGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTF 195
Cdd:PLN02820 116 SGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIF 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 196 YNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDH 275
Cdd:PLN02820 196 YNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDH 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 276 WALDDHHALHLTRKVVRNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKA 349
Cdd:PLN02820 276 FAQDELHALAIGRNIVKNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKK 355

                 ....*....
gi 957951445 350 FYGDTLVTG 358
Cdd:PLN02820 356 NYGTTLVTG 364
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
48-358 1.66e-153

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 441.77  E-value: 1.66e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  48 QMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYD-NEEVPGGGIITGIGRV 126
Cdd:COG4799    1 AMRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDdDDRVPGDGVVTGIGTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 127 SGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFpdrDHFGRTFYNQAiMSSKNI 206
Cdd:COG4799   80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445 207 AQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHL 286
Cdd:COG4799  156 PQISVIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALAL 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 957951445 287 TRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTG 358
Cdd:COG4799  236 ARRLLSYLPSNNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTG 307
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
77-358 7.10e-94

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: 288.77  E-value: 7.10e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445   77 SRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYDN--EEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQL 154
Cdd:pfam01039   4 PRGKLTARERIDLLLDPGS-FGELEDLFFHRATEFgrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  155 RAQEIAMQNRLPCIYLVDSGGAylpRQADVFPDRDHFGRTFYNQAIMSSKnIAQIAVVMGSCTAGGAYVPAMADENIIVR 234
Cdd:pfam01039  83 RAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLASGV-IPQISLIMGPCAGGGAYLPALGDFVIMVE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957951445  235 KQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKK---LDVTIEPSEEPL 311
Cdd:pfam01039 159 GTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPnnrEPVPIVPTKDPP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 957951445  312 FPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTG 358
Cdd:pfam01039 239 DRDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTG 285
 
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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