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Conserved domains on  [gi|511911022|ref|XP_004774899|]
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acyl-CoA-binding domain-containing protein 7 [Mustela putorius furo]

Protein Classification

acyl-CoA-binding protein( domain architecture ID 1012)

acyl-CoA-binding protein binds acyl-CoA esters and may play a role in housekeeping and/or trafficking

CATH:  1.20.80.10
Gene Ontology:  GO:0000062
PubMed:  16018771
SCOP:  4000745

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACBP super family cl00221
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 3-87 9.35e-38

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


The actual alignment was detected with superfamily member cd00435:

Pssm-ID: 469667  Cd Length: 85  Bit Score: 121.28  E-value: 9.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511911022  3 LQADFDRITKDVRKLKTRPDDEELKELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKAKEL 82
Cdd:cd00435   1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80


                ....*
gi 511911022 83 IEKYG 87
Cdd:cd00435  81 IAKYA 85
 
Name Accession Description Interval E-value
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 3-87 9.35e-38

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 121.28  E-value: 9.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511911022  3 LQADFDRITKDVRKLKTRPDDEELKELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKAKEL 82
Cdd:cd00435   1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80


                ....*
gi 511911022 83 IEKYG 87
Cdd:cd00435  81 IAKYA 85
ACBP pfam00887
Acyl CoA binding protein;
4-79 4.86e-30

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 101.52  E-value: 4.86e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511911022   4 QADFDRITKDVRKLKTRPDDEELKELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKA 79
Cdd:pfam00887  1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
1-86 5.41e-26

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 91.45  E-value: 5.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511911022  1 MSLQADFDRITKDVRKLKTRPDDEELKELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKAK 80
Cdd:COG4281   2 SDLQAAFEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVN 81


                ....*.
gi 511911022 81 ELIEKY 86
Cdd:COG4281  82 SLLGKQ 87
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 18-86 3.39e-08

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 46.35  E-value: 3.39e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511911022 18 KTRPDDEELK-ELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKAKELIEKY 86
Cdd:PTZ00458 17 KTVNLSVEIKlDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
 
Name Accession Description Interval E-value
ACBP cd00435
Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a ...
 3-87 9.35e-38

Acyl CoA binding protein (ACBP) binds thiol esters of long fatty acids and coenzyme A in a one-to-one binding mode with high specificity and affinity. Acyl-CoAs are important intermediates in fatty lipid synthesis and fatty acid degradation and play a role in regulation of intermediary metabolism and gene regulation. The suggested role of ACBP is to act as a intracellular acyl-CoA transporter and pool former. ACBPs are present in a large group of eukaryotic species and several tissue-specific isoforms have been detected.


Pssm-ID: 238248  Cd Length: 85  Bit Score: 121.28  E-value: 9.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511911022  3 LQADFDRITKDVRKLKTRPDDEELKELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKAKEL 82
Cdd:cd00435   1 LQEEFEAAAEKVKKLKTKPSNEEKLQLYSLYKQATVGDCNTERPGMFDLKGRAKWDAWNSLKGMSKEDAMKAYIAKVEEL 80


                ....*
gi 511911022 83 IEKYG 87
Cdd:cd00435  81 IAKYA 85
ACBP pfam00887
Acyl CoA binding protein;
4-79 4.86e-30

Acyl CoA binding protein;


Pssm-ID: 459982  Cd Length: 76  Bit Score: 101.52  E-value: 4.86e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511911022   4 QADFDRITKDVRKLKTRPDDEELKELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKA 79
Cdd:pfam00887  1 EEKFEAAAEFVKKLKSKPSNEEKLELYGLYKQATVGDCNTPRPGMFDFKGKAKWDAWKKLGGMSKEEAMAKYVELV 76
ACB COG4281
Acyl-CoA-binding protein [Lipid transport and metabolism];
1-86 5.41e-26

Acyl-CoA-binding protein [Lipid transport and metabolism];


Pssm-ID: 443422  Cd Length: 87  Bit Score: 91.45  E-value: 5.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511911022  1 MSLQADFDRITKDVRKLKTRPDDEELKELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKAK 80
Cdd:COG4281   2 SDLQAAFEAAVARVKTLTERPDNDTLLKLYALYKQATEGDVTGKRPGMTDFVGRAKYDAWAQLKGMSKDEAMQQYIDLVN 81


                ....*.
gi 511911022 81 ELIEKY 86
Cdd:COG4281  82 SLLGKQ 87
PTZ00458 PTZ00458
acyl CoA binding protein; Provisional
 18-86 3.39e-08

acyl CoA binding protein; Provisional


Pssm-ID: 185637  Cd Length: 90  Bit Score: 46.35  E-value: 3.39e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511911022 18 KTRPDDEELK-ELYGLYKQSVVGDINIECPGMLDLKGKAKWEAWNLQKGQSKEDAMSAYISKAKELIEKY 86
Cdd:PTZ00458 17 KTVNLSVEIKlDLYKYYKQSTVGNCNIKEPSMFKYQDRKKYEAWKSIENLNREDAKKRYVEIVTELFPNW 86
 
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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