NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1724161783|ref|WP_146972689|]
View 

DUF971 domain-containing protein [Lujinxingia vulgaris]

Protein Classification

DUF971 domain-containing protein( domain architecture ID 10007526)

DUF971 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724161783   1 MGYVPHPTEIEYKSAARALRIAFSDDHEAVYPTRYLRGFCPCARCQGHTSGPHKFiehQPPQAEV--VDVRQVGNYAINI 78
Cdd:COG3536     1 MMTTPWPTEIRLHQASRVLEITFDDGHRFRLPAEYLRVYSPSAEVQGHGPGQEVL---QPGKRDVniTGIEPVGNYAVRL 77

                          90       100
                  ....*....|....*....|....*...
gi 1724161783  79 VFADGHDTGIYSFQRLRELCPCPACMPQ 106
Cdd:COG3536    78 TFDDGHDSGIYSWDYLYELGRNQEALWQ 105
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724161783   1 MGYVPHPTEIEYKSAARALRIAFSDDHEAVYPTRYLRGFCPCARCQGHTSGPHKFiehQPPQAEV--VDVRQVGNYAINI 78
Cdd:COG3536     1 MMTTPWPTEIRLHQASRVLEITFDDGHRFRLPAEYLRVYSPSAEVQGHGPGQEVL---QPGKRDVniTGIEPVGNYAVRL 77

                          90       100
                  ....*....|....*....|....*...
gi 1724161783  79 VFADGHDTGIYSFQRLRELCPCPACMPQ 106
Cdd:COG3536    78 TFDDGHDSGIYSWDYLYELGRNQEALWQ 105
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724161783  10 IEYKSAARALRIAFSDDHEAVYPTRYLRGFCPCARCQGHTSGPHKFIEH-QPPQAEVVDVRQVGNYAINIVFADGHDTGI 88
Cdd:pfam06155   1 IRLHKDSRVLEIEWDDGKTSRLPAEWLRVNCPCAECRGHGPGQRLLQTGkIPRDVKIVSIEPVGNYAVRIVFSDGHDSGI 80


                  ....*..
gi 1724161783  89 YSFQRLR 95
Cdd:pfam06155  81 YSWDYLR 87
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724161783   1 MGYVPHPTEIEYKSAARALRIAFSDDHEAVYPTRYLRGFCPCARCQGHTSGPHKFiehQPPQAEV--VDVRQVGNYAINI 78
Cdd:COG3536     1 MMTTPWPTEIRLHQASRVLEITFDDGHRFRLPAEYLRVYSPSAEVQGHGPGQEVL---QPGKRDVniTGIEPVGNYAVRL 77

                          90       100
                  ....*....|....*....|....*...
gi 1724161783  79 VFADGHDTGIYSFQRLRELCPCPACMPQ 106
Cdd:COG3536    78 TFDDGHDSGIYSWDYLYELGRNQEALWQ 105
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724161783  10 IEYKSAARALRIAFSDDHEAVYPTRYLRGFCPCARCQGHTSGPHKFIEH-QPPQAEVVDVRQVGNYAINIVFADGHDTGI 88
Cdd:pfam06155   1 IRLHKDSRVLEIEWDDGKTSRLPAEWLRVNCPCAECRGHGPGQRLLQTGkIPRDVKIVSIEPVGNYAVRIVFSDGHDSGI 80


                  ....*..
gi 1724161783  89 YSFQRLR 95
Cdd:pfam06155  81 YSWDYLR 87
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
                          10        20        30
                  ....*....|....*....|....*....|
gi 1724161783  78 IVFADGHDTgIYSFQRLRELCPCPACMPQG 107
Cdd:pfam06155  12 IEWDDGKTS-RLPAEWLRVNCPCAECRGHG 40
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH