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Conserved domains on  [gi|1002293625|ref|XP_015651152|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

malonyl-CoA decarboxylase( domain architecture ID 13603468)

malonyl-CoA decarboxylase (MCD) is a key intermediate in the biosynthesis of long-chain and very long-chain fatty acids, and also has a crucial role in the regulation of fatty acid oxidation through its potent inhibition of carnitine palmitoyltransferase I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MCD super family cl09364
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 206-485 6.73e-118

Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


The actual alignment was detected with superfamily member pfam05292:

Pssm-ID: 461613  Cd Length: 245  Bit Score: 346.86  E-value: 6.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 206 LTLHQITWDDPASLLEKIVAYEAVHPIRNLIDLKRRLGVGRRCFGYFHPAIPGEPLIFIEVALLKDTAASIQEVL-WDDP 284
Cdd:pfam05292   3 LELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLdEDAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 285 PTPESEARCALFYSISSTQPGLSGINLGKFLLKRVIEMLRRDMPSVQIFATLSPIPGFMQWLLAKLASQiklaeaesqdg 364
Cdd:pfam05292  83 PIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAKE----------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 365 sllegtsstfRESILFPEEERMIHDavehaggksgikllqdiLKSSQWVKSDKLSSALKSPLMRLCARYLAREKKRGKAL 444
Cdd:pfam05292 152 ----------SDALLSAEDREALAA-----------------LDDPEWHEDPELAEALREPLLRLAARYLLRAKRDGRPL 204

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1002293625 445 DAVANFHLQNGAMIERINWMADQSEKGIQQSGGIMVNYMYR 485
Cdd:pfam05292 205 DPVARFHLGNGARLERLNWLGDTSAKGLKQSYGLMVNYLYD 245
MCD_N super family cl38688
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 137-200 3.63e-07

Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


The actual alignment was detected with superfamily member pfam17408:

Pssm-ID: 465421  Cd Length: 85  Bit Score: 47.96  E-value: 3.63e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002293625 137 RMERGLREALRPKYAGFLEAMNAQPGGLKLLAVIRADLLALLGEEnlPALRALDGYLKEKLVTW 200
Cdd:pfam17408  23 AAEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLKGN--PDLRALDRDLEHLLSSW 84
 
Name Accession Description Interval E-value
MCD pfam05292
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 206-485 6.73e-118

Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 461613  Cd Length: 245  Bit Score: 346.86  E-value: 6.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 206 LTLHQITWDDPASLLEKIVAYEAVHPIRNLIDLKRRLGVGRRCFGYFHPAIPGEPLIFIEVALLKDTAASIQEVL-WDDP 284
Cdd:pfam05292   3 LELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLdEDAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 285 PTPESEARCALFYSISSTQPGLSGINLGKFLLKRVIEMLRRDMPSVQIFATLSPIPGFMQWLLAKLASQiklaeaesqdg 364
Cdd:pfam05292  83 PIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAKE----------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 365 sllegtsstfRESILFPEEERMIHDavehaggksgikllqdiLKSSQWVKSDKLSSALKSPLMRLCARYLAREKKRGKAL 444
Cdd:pfam05292 152 ----------SDALLSAEDREALAA-----------------LDDPEWHEDPELAEALREPLLRLAARYLLRAKRDGRPL 204

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1002293625 445 DAVANFHLQNGAMIERINWMADQSEKGIQQSGGIMVNYMYR 485
Cdd:pfam05292 205 DPVARFHLGNGARLERLNWLGDTSAKGLKQSYGLMVNYLYD 245
MCD_N pfam17408
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 137-200 3.63e-07

Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 465421  Cd Length: 85  Bit Score: 47.96  E-value: 3.63e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002293625 137 RMERGLREALRPKYAGFLEAMNAQPGGLKLLAVIRADLLALLGEEnlPALRALDGYLKEKLVTW 200
Cdd:pfam17408  23 AAEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLKGN--PDLRALDRDLEHLLSSW 84
 
Name Accession Description Interval E-value
MCD pfam05292
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 206-485 6.73e-118

Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 461613  Cd Length: 245  Bit Score: 346.86  E-value: 6.73e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 206 LTLHQITWDDPASLLEKIVAYEAVHPIRNLIDLKRRLGVGRRCFGYFHPAIPGEPLIFIEVALLKDTAASIQEVL-WDDP 284
Cdd:pfam05292   3 LELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLdEDAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 285 PTPESEARCALFYSISSTQPGLSGINLGKFLLKRVIEMLRRDMPSVQIFATLSPIPGFMQWLLAKLASQiklaeaesqdg 364
Cdd:pfam05292  83 PIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAKE----------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002293625 365 sllegtsstfRESILFPEEERMIHDavehaggksgikllqdiLKSSQWVKSDKLSSALKSPLMRLCARYLAREKKRGKAL 444
Cdd:pfam05292 152 ----------SDALLSAEDREALAA-----------------LDDPEWHEDPELAEALREPLLRLAARYLLRAKRDGRPL 204

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1002293625 445 DAVANFHLQNGAMIERINWMADQSEKGIQQSGGIMVNYMYR 485
Cdd:pfam05292 205 DPVARFHLGNGARLERLNWLGDTSAKGLKQSYGLMVNYLYD 245
MCD_N pfam17408
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 137-200 3.63e-07

Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic malonyl-CoA decarboxylase (MLYCD) proteins. Malonyl-CoA, in addition to being an intermediate in the de novo synthesis of fatty acids, is an inhibitor of carnitine palmitoyltransferase I, the enzyme that regulates the transfer of long-chain fatty acyl-CoA into mitochondria, where they are oxidized. After exercise, malonyl-CoA decarboxylase participates with acetyl-CoA carboxylase in regulating the concentration of malonyl-CoA in liver and adipose tissue, as well as in muscle. Malonyl-CoA decarboxylase is regulated by AMP-activated protein kinase (AMPK).


Pssm-ID: 465421  Cd Length: 85  Bit Score: 47.96  E-value: 3.63e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002293625 137 RMERGLREALRPKYAGFLEAMNAQPGGLKLLAVIRADLLALLGEEnlPALRALDGYLKEKLVTW 200
Cdd:pfam17408  23 AAEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLKGN--PDLRALDRDLEHLLSSW 84
 
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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