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Conserved domains on  [gi|2786578307|ref|WP_369827009|]
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cupin domain-containing protein [Geobacillus sp. 46C-IIa]

Protein Classification

cupin domain-containing protein( domain architecture ID 10004899)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

CATH:  2.60.120.10
Gene Ontology:  GO:0046872
SCOP:  3001825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
6-44 2.03e-06

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


:

Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 40.99  E-value: 2.03e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 2786578307  6 VEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALFP 44
Cdd:COG1917   58 VGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFS 96
 
Name Accession Description Interval E-value
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
6-44 2.03e-06

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 40.99  E-value: 2.03e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 2786578307  6 VEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALFP 44
Cdd:COG1917   58 VGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFS 96
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
6-40 5.26e-06

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel).


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 39.85  E-value: 5.26e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2786578307   6 VEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFL 40
Cdd:cd06122    63 VGDEERELGAGEAVLAPAGVPHGVRNTGAERLVLL 97
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
5-43 2.10e-04

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 35.31  E-value: 2.10e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 2786578307  5 VVEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALF 43
Cdd:pfam07883 33 TVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
 
Name Accession Description Interval E-value
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
6-44 2.03e-06

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 40.99  E-value: 2.03e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 2786578307  6 VEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALFP 44
Cdd:COG1917   58 VGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFS 96
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
6-40 5.26e-06

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel).


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 39.85  E-value: 5.26e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2786578307   6 VEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFL 40
Cdd:cd06122    63 VGDEERELGAGEAVLAPAGVPHGVRNTGAERLVLL 97
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
6-41 7.53e-06

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 39.42  E-value: 7.53e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2786578307   6 VEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLA 41
Cdd:cd02214    55 IDGEPREVGPGDAVLIPPGAVQRIENTGEEDLVFLC 90
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
5-43 1.66e-04

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 36.27  E-value: 1.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2786578307   5 VVEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALF 43
Cdd:COG0662    62 TIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQ 100
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
5-43 2.10e-04

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 35.31  E-value: 2.10e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 2786578307  5 VVEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALF 43
Cdd:pfam07883 33 TVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
5-41 2.83e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 35.76  E-value: 2.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2786578307   5 VVEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLA 41
Cdd:COG3837    64 RIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLV 100
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
5-41 2.32e-03

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 32.86  E-value: 2.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 2786578307  5 VVEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLA 41
Cdd:cd02209   51 TVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVLW 87
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
5-43 2.56e-03

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 32.45  E-value: 2.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 2786578307  5 VVEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALF 43
Cdd:cd02208   35 LDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
1-40 4.55e-03

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 32.49  E-value: 4.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2786578307   1 MAGAV---VEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFL 40
Cdd:cd02211    54 LEGEVeltVGGETHTLTAGGYAYLPPGTKHSLRNAGDEPARLL 96
cupin_Moth_1897 cd06984
uncharacterized Methanocaldococcus jannaschii Moth_1897 and related proteins, cupin domain; ...
8-40 5.22e-03

uncharacterized Methanocaldococcus jannaschii Moth_1897 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to Moth_1897, a Methanocaldococcus jannaschii protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380389 [Multi-domain]  Cd Length: 83  Bit Score: 31.83  E-value: 5.22e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 2786578307  8 DQRQQLVAGRLVVILADVPHSIKNNGEQRARFL 40
Cdd:cd06984   48 EEKQEVEADTLIESPANIPHCLYNESDADLRVL 80
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
15-46 6.69e-03

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 32.25  E-value: 6.69e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2786578307  15 AGRLVVILADVPHSIKNNGEQRARFLALFPSA 46
Cdd:COG2140    53 PGDVVYVPPGYGHYIINTGDEPLVFLAVFDDD 84
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
4-45 8.64e-03

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 31.27  E-value: 8.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 2786578307  4 AVVEDQRQQLVAGRLVVILADVPHSIKNNGEQRARFLALFPS 45
Cdd:cd02222   50 VVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLGFLCIVPK 91
 
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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