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Conserved domains on  [gi|145322919|ref|NP_001030782|]
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Myb domain protein [Arabidopsis thaliana]

Protein Classification

COG3536 superfamily protein( domain architecture ID 1905239)

COG3536 superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3536 super family cl43893
Uncharacterized conserved protein, DUF971 family [Function unknown];
32-92 5.25e-19

Uncharacterized conserved protein, DUF971 family [Function unknown];


The actual alignment was detected with superfamily member COG3536:

Pssm-ID: 442757  Cd Length: 124  Bit Score: 75.26  E-value: 5.25e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145322919  32 KQVEVEYADGTKFNFSSEFLRIHSPAAdgKVR--SIGGEKVISGRRYVGIMSAEPVGNYGVRI 92
Cdd:COG3536   17 RVLEITFDDGHRFRLPAEYLRVYSPSA--EVQghGPGQEVLQPGKRDVNITGIEPVGNYAVRL 77
 
Name Accession Description Interval E-value
COG3536 COG3536
Uncharacterized conserved protein, DUF971 family [Function unknown];
32-92 5.25e-19

Uncharacterized conserved protein, DUF971 family [Function unknown];


Pssm-ID: 442757  Cd Length: 124  Bit Score: 75.26  E-value: 5.25e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145322919  32 KQVEVEYADGTKFNFSSEFLRIHSPAAdgKVR--SIGGEKVISGRRYVGIMSAEPVGNYGVRI 92
Cdd:COG3536   17 RVLEITFDDGHRFRLPAEYLRVYSPSA--EVQghGPGQEVLQPGKRDVNITGIEPVGNYAVRL 77
GBBH-like_N pfam06155
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ...
 32-92 2.28e-14

Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins including gamma-butyrobetaine dioxygenase, Fe-S cluster assembly factor HCF101 and trimethyllysine dioxygenase proteins. Gamma-butyrobetaine hydroxylase (GBBH) is a alpha-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic double-stranded beta-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. The N-terminal domain could facilitate dimer formation, but its precise function is not known. Other family members have been suggested to be involved in FeS cluster maintenance (see Supplementary note 5 in.)


Pssm-ID: 461840 [Multi-domain]  Cd Length: 87  Bit Score: 62.24  E-value: 2.28e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145322919  32 KQVEVEYADGTKFNFSSEFLRIHSPAAdGKVRSIGGEKVISG---RRYVGIMSAEPVGNYGVRI 92
Cdd:pfam06155  8 RVLEIEWDDGKTSRLPAEWLRVNCPCA-ECRGHGPGQRLLQTgkiPRDVKIVSIEPVGNYAVRI 70
 
Name Accession Description Interval E-value
COG3536 COG3536
Uncharacterized conserved protein, DUF971 family [Function unknown];
32-92 5.25e-19

Uncharacterized conserved protein, DUF971 family [Function unknown];


Pssm-ID: 442757  Cd Length: 124  Bit Score: 75.26  E-value: 5.25e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145322919  32 KQVEVEYADGTKFNFSSEFLRIHSPAAdgKVR--SIGGEKVISGRRYVGIMSAEPVGNYGVRI 92
Cdd:COG3536   17 RVLEITFDDGHRFRLPAEYLRVYSPSA--EVQghGPGQEVLQPGKRDVNITGIEPVGNYAVRL 77
GBBH-like_N pfam06155
Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ...
 32-92 2.28e-14

Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins including gamma-butyrobetaine dioxygenase, Fe-S cluster assembly factor HCF101 and trimethyllysine dioxygenase proteins. Gamma-butyrobetaine hydroxylase (GBBH) is a alpha-ketoglutarate-dependent dioxygenase that catalyzes the biosynthesis of L-carnitine by hydroxylation of gamma-butyrobetaine (GBB). GBBH is a dimeric enzyme. The monomer consists of a catalytic double-stranded beta-helix domain and a smaller N-terminal domain. The N-terminal domain has a bound Zn ion, which is coordinated by three cysteines and one histidine. The N-terminal domain could facilitate dimer formation, but its precise function is not known. Other family members have been suggested to be involved in FeS cluster maintenance (see Supplementary note 5 in.)


Pssm-ID: 461840 [Multi-domain]  Cd Length: 87  Bit Score: 62.24  E-value: 2.28e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145322919  32 KQVEVEYADGTKFNFSSEFLRIHSPAAdGKVRSIGGEKVISG---RRYVGIMSAEPVGNYGVRI 92
Cdd:pfam06155  8 RVLEIEWDDGKTSRLPAEWLRVNCPCA-ECRGHGPGQRLLQTgkiPRDVKIVSIEPVGNYAVRI 70
 
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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