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Conserved domains on  [gi|1709604481|ref|XP_029881361|]
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malonyl-CoA decarboxylase, mitochondrial isoform X2 [Aquila chrysaetos chrysaetos]

Protein Classification

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 ...
 201-464 1.26e-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: 348.40  E-value: 1.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 201 GFLNLERVTWQSPCEVLQKISDSEAVHPVRNWVDMKRRVGSYRRCYFFSHCAIPGEPLIVLHVALTSDISSSIQAIVKEV 280
Cdd:pfam05292   1 GFLELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 281 PPleTEDTDKITTAIFYSISLTQQGLQGVELGTYLIKRVVKELQKELPQIKAFSTLSPIPGFTKWLVGLLSPqtkelEKN 360
Cdd:pfam05292  81 AP--PIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAK-----ESD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 361 ELFTESEWQEISEitgdsttetlkklLNNNEWVRSEKLVKVFHLPFMRLCAWYLYGEKHRGYALNPVANFHLQNGSVMWR 440
Cdd:pfam05292 154 ALLSAEDREALAA-------------LDDPEWHEDPELAEALREPLLRLAARYLLRAKRDGRPLDPVARFHLGNGARLER 220

                         250       260
                  ....*....|....*....|....
gi 1709604481 441 INWMADTSPRGIAASCGMMVNYRY 464
Cdd:pfam05292 221 LNWLGDTSAKGLKQSYGLMVNYLY 244
MCD_N super family cl38688
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 103-198 1.45e-11

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: 60.28  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 103 FGVDHGRVAefsakvlQAREQQREPGALLQAEDRLRYYLNPQYRGLFQHLGRLEGGLRFLVELRGDLVEGLAtkavDGPH 182
Cdd:pfam17408   1 FGPDPERLD-------KAIEAYRAAPGSDAAEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLK----GNPD 69

                          90
                  ....*....|....*.
gi 1709604481 183 VKEMNGVLKNMLSEWF 198
Cdd:pfam17408  70 LRALDRDLEHLLSSWF 85
 
Name Accession Description Interval E-value
MCD pfam05292
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 201-464 1.26e-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: 348.40  E-value: 1.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 201 GFLNLERVTWQSPCEVLQKISDSEAVHPVRNWVDMKRRVGSYRRCYFFSHCAIPGEPLIVLHVALTSDISSSIQAIVKEV 280
Cdd:pfam05292   1 GFLELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 281 PPleTEDTDKITTAIFYSISLTQQGLQGVELGTYLIKRVVKELQKELPQIKAFSTLSPIPGFTKWLVGLLSPqtkelEKN 360
Cdd:pfam05292  81 AP--PIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAK-----ESD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 361 ELFTESEWQEISEitgdsttetlkklLNNNEWVRSEKLVKVFHLPFMRLCAWYLYGEKHRGYALNPVANFHLQNGSVMWR 440
Cdd:pfam05292 154 ALLSAEDREALAA-------------LDDPEWHEDPELAEALREPLLRLAARYLLRAKRDGRPLDPVARFHLGNGARLER 220

                         250       260
                  ....*....|....*....|....
gi 1709604481 441 INWMADTSPRGIAASCGMMVNYRY 464
Cdd:pfam05292 221 LNWLGDTSAKGLKQSYGLMVNYLY 244
MCD_N pfam17408
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 103-198 1.45e-11

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: 60.28  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 103 FGVDHGRVAefsakvlQAREQQREPGALLQAEDRLRYYLNPQYRGLFQHLGRLEGGLRFLVELRGDLVEGLAtkavDGPH 182
Cdd:pfam17408   1 FGPDPERLD-------KAIEAYRAAPGSDAAEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLK----GNPD 69

                          90
                  ....*....|....*.
gi 1709604481 183 VKEMNGVLKNMLSEWF 198
Cdd:pfam17408  70 LRALDRDLEHLLSSWF 85
PRK12702 PRK12702
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 323-426 1.52e-03

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 105866  Cd Length: 302  Bit Score: 40.44  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 323 LQKELPQIKAFSTLSPIpGFTKWLVGLLSPQTK-ELEKNELFTESEWQEISEITGDSttETLKKLLNNNEWVRSEKLVKV 401
Cdd:PRK12702  103 LRHILQQVRQDSHLDLI-GFGDWTASELAAATGiPLEEAERAQKREYSEIFSYSGDP--ARLREAFAQQEANLTQHLLRL 179

                          90       100
                  ....*....|....*....|....*
gi 1709604481 402 FHLPFMRLCAWYLYGEKHRGYALNP 426
Cdd:PRK12702  180 HQLHFSDLPQWYLTGWMQPTLAAEP 204
 
Name Accession Description Interval E-value
MCD pfam05292
Malonyl-CoA decarboxylase C-terminal domain; This family consists of several eukaryotic ...
 201-464 1.26e-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: 348.40  E-value: 1.26e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 201 GFLNLERVTWQSPCEVLQKISDSEAVHPVRNWVDMKRRVGSYRRCYFFSHCAIPGEPLIVLHVALTSDISSSIQAIVKEV 280
Cdd:pfam05292   1 GFLELRRITWDSPASLLEKIIRYEAVHEIRGWDDLRRRLDSDRRCFAFFHPALPDEPLIFVEVALVDEIADSIQPLLDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 281 PPleTEDTDKITTAIFYSISLTQQGLQGVELGTYLIKRVVKELQKELPQIKAFSTLSPIPGFTKWLVGLLSPqtkelEKN 360
Cdd:pfam05292  81 AP--PIDPEKATTAIFYSISNTQVGLRGISFGNFLIKRVVEELQREFPNLKTFATLSPIPGFRRWLDRELAK-----ESD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 361 ELFTESEWQEISEitgdsttetlkklLNNNEWVRSEKLVKVFHLPFMRLCAWYLYGEKHRGYALNPVANFHLQNGSVMWR 440
Cdd:pfam05292 154 ALLSAEDREALAA-------------LDDPEWHEDPELAEALREPLLRLAARYLLRAKRDGRPLDPVARFHLGNGARLER 220

                         250       260
                  ....*....|....*....|....
gi 1709604481 441 INWMADTSPRGIAASCGMMVNYRY 464
Cdd:pfam05292 221 LNWLGDTSAKGLKQSYGLMVNYLY 244
MCD_N pfam17408
Malonyl-CoA decarboxylase N-terminal domain; This family consists of several eukaryotic ...
 103-198 1.45e-11

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: 60.28  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 103 FGVDHGRVAefsakvlQAREQQREPGALLQAEDRLRYYLNPQYRGLFQHLGRLEGGLRFLVELRGDLVEGLAtkavDGPH 182
Cdd:pfam17408   1 FGPDPERLD-------KAIEAYRAAPGSDAAEAELRRALEPRRQELLRRFNLAPGGTKFLVDMRADLLALLK----GNPD 69

                          90
                  ....*....|....*.
gi 1709604481 183 VKEMNGVLKNMLSEWF 198
Cdd:pfam17408  70 LRALDRDLEHLLSSWF 85
PRK12702 PRK12702
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 323-426 1.52e-03

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 105866  Cd Length: 302  Bit Score: 40.44  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709604481 323 LQKELPQIKAFSTLSPIpGFTKWLVGLLSPQTK-ELEKNELFTESEWQEISEITGDSttETLKKLLNNNEWVRSEKLVKV 401
Cdd:PRK12702  103 LRHILQQVRQDSHLDLI-GFGDWTASELAAATGiPLEEAERAQKREYSEIFSYSGDP--ARLREAFAQQEANLTQHLLRL 179

                          90       100
                  ....*....|....*....|....*
gi 1709604481 402 FHLPFMRLCAWYLYGEKHRGYALNP 426
Cdd:PRK12702  180 HQLHFSDLPQWYLTGWMQPTLAAEP 204
 
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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