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Database: UniProt
Entry: A0A364L270_9EURO
LinkDB: A0A364L270_9EURO
Original site: A0A364L270_9EURO 
ID   A0A364L270_9EURO        Unreviewed;       343 AA.
AC   A0A364L270;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   28-JUN-2023, entry version 18.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=BHQ10_005902 {ECO:0000313|EMBL:RAO69890.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO69890.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO69890.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO69890.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAO69890.1}.
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DR   EMBL; MIKG01000010; RAO69890.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364L270; -.
DR   STRING; 1196081.A0A364L270; -.
DR   OrthoDB; 1380829at2759; -.
DR   Proteomes; UP000249363; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF62; SEXUAL DIFFERENTIATION PROCESS PROTEIN ISP7; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249363}.
FT   DOMAIN          179..283
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   343 AA;  38814 MW;  FF34EC52FCE8C4BB CRC64;
     MAIASAPPIL DFSAYYGDDE IARAKLVEEV RKCCLYNGFF QIKGHSVPLE LQRRVMKCAK
     RFFDLPVEEK LQIDKNLNTF NRGYELLRSQ MLEAGTGPEL KEGLYIGEEI PEDHPYYVQK
     KLNSGPNQWP QTIADKEEFQ KTTMEYYHAV YELAKDVLSV IALTLGVDSS FFKPLTDEAV
     ATMRYLHYPA QPKDQDEKLN RGIGAHTDFG CVTLLLQDEV DGLQVLDAPS GQWLDVQPVE
     GAYVVNLGDL FMRMANDTYK SNIHRVINKS GRERYSIPFF FSGNPDYLCE CLPNCRAPGE
     AAKYAPITVQ DMVTGAYKAS YGRAEQYKKE MEKKNMASSS ITA
//
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