ID A0A167VNV1_9AGAM Unreviewed; 386 AA.
AC A0A167VNV1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
DE Flags: Fragment;
GN ORFNames=FIBSPDRAFT_766202 {ECO:0000313|EMBL:KZP05214.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP05214.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP05214.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP05214.1,
RC ECO:0000313|Proteomes:UP000076532};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; KV417854; KZP05214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167VNV1; -.
DR STRING; 436010.A0A167VNV1; -.
DR OrthoDB; 38879at2759; -.
DR Proteomes; UP000076532; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076532}.
FT DOMAIN 262..384
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZP05214.1"
SQ SEQUENCE 386 AA; 41675 MW; 120111FAB3368E03 CRC64;
SLTSRVSSAL TGQRWTDAKV LLAEMRIRGQ RPKLGALQRW TRDCDAASTA DGSEGDREVL
GVLDAIMRTA DYAGADASPV RRHADWTPDA GQRTISTGLF RAAMEGTLFD QGKVDDIRAL
FRVCSNTPGN ERRPPNLHPA IVYASSPNAI SLSPASSSDS SSLPGPLQCS PPVEPVTRHD
VPHVPGAFFL TSVLSPSECS AIISATSALE FLPDQPISSS DAPASILAAN VYWLADPPFL
AALWARLAHL LPETIAGKHV RGLNARFRVY RYVPGAIYRP HLDGAWPASG VDPATGEYVY
DSAPKDDPLW SRLTFLIYLN DEFSNGQTTF FLPSPTIGVL DARPVKPRQG SVLVFPHGET
HALLHEGSPV TEGGKFVIRT DVLYTK
//
