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DUF971 domain-containing protein [Lujinxingia vulgaris]
DUF971 domain-containing protein( domain architecture ID 10007526)
DUF971 domain-containing protein
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
COG3536 | COG3536 | Uncharacterized conserved protein, DUF971 family [Function unknown]; |
1-106 | 9.74e-43 | |||
Uncharacterized conserved protein, DUF971 family [Function unknown]; : Pssm-ID: 442757 Cd Length: 124 Bit Score: 136.12 E-value: 9.74e-43
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Name | Accession | Description | Interval | E-value | |||
COG3536 | COG3536 | Uncharacterized conserved protein, DUF971 family [Function unknown]; |
1-106 | 9.74e-43 | |||
Uncharacterized conserved protein, DUF971 family [Function unknown]; Pssm-ID: 442757 Cd Length: 124 Bit Score: 136.12 E-value: 9.74e-43
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GBBH-like_N | pfam06155 | Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ... |
10-95 | 4.69e-31 | |||
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: 105.38 E-value: 4.69e-31
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Name | Accession | Description | Interval | E-value | |||
COG3536 | COG3536 | Uncharacterized conserved protein, DUF971 family [Function unknown]; |
1-106 | 9.74e-43 | |||
Uncharacterized conserved protein, DUF971 family [Function unknown]; Pssm-ID: 442757 Cd Length: 124 Bit Score: 136.12 E-value: 9.74e-43
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GBBH-like_N | pfam06155 | Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ... |
10-95 | 4.69e-31 | |||
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: 105.38 E-value: 4.69e-31
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GBBH-like_N | pfam06155 | Gamma-butyrobetaine hydroxylase-like, N-terminal; This domain is found in several proteins ... |
78-107 | 6.84e-03 | |||
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: 33.35 E-value: 6.84e-03
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Blast search parameters | ||||
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