uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen ...
22-299
4.39e-118
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.
:
Pssm-ID: 319960 Cd Length: 254 Bit Score: 340.29 E-value: 4.39e-118
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen ...
22-299
4.39e-118
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.
Pssm-ID: 319960 Cd Length: 254 Bit Score: 340.29 E-value: 4.39e-118
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and ...
21-307
7.26e-101
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and fungal proteins. This entry represents proteins involved in D-lysine metabolism, which catalyze a successive decarboxylation and intramolecular hydroxylation of 2-oxoadipate forming 2-hydroxyglutarate in a Fe(II) and oxygen-dependent manner. The structure of this domain has been solved by structural genomics. The structure implies a zinc-binding function (information derived from TOPSAN for PDB:3iuz).
Pssm-ID: 429271 Cd Length: 320 Bit Score: 299.13 E-value: 7.26e-101
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen ...
22-299
4.39e-118
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.
Pssm-ID: 319960 Cd Length: 254 Bit Score: 340.29 E-value: 4.39e-118
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and ...
21-307
7.26e-101
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and fungal proteins. This entry represents proteins involved in D-lysine metabolism, which catalyze a successive decarboxylation and intramolecular hydroxylation of 2-oxoadipate forming 2-hydroxyglutarate in a Fe(II) and oxygen-dependent manner. The structure of this domain has been solved by structural genomics. The structure implies a zinc-binding function (information derived from TOPSAN for PDB:3iuz).
Pssm-ID: 429271 Cd Length: 320 Bit Score: 299.13 E-value: 7.26e-101
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen ...
33-271
3.22e-24
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.
Pssm-ID: 319957 Cd Length: 221 Bit Score: 98.15 E-value: 3.22e-24
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen ...
34-308
6.85e-11
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.
Pssm-ID: 319959 Cd Length: 301 Bit Score: 61.93 E-value: 6.85e-11
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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