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Database: UniProt
Entry: A0A176VCU7_MARPO
LinkDB: A0A176VCU7_MARPO
Original site: A0A176VCU7_MARPO 
ID   A0A176VCU7_MARPO        Unreviewed;       316 AA.
AC   A0A176VCU7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=AXG93_4448s1290 {ECO:0000313|EMBL:OAE18694.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE18694.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE18694.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE18694.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAE18694.1}.
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DR   EMBL; LVLJ01004024; OAE18694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VCU7; -.
DR   OrthoDB; 2908779at2759; -.
DR   Proteomes; UP000077202; 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   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; PTHR47991:SF153; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 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|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          164..265
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   316 AA;  35019 MW;  2BA01F2F130D3988 CRC64;
     MSSEDGVPVI DLADIQGPGL ERICEQIAKA SEEWGFFHIV NHGVDLDLIR RTQKAYIDFF
     HLPTQEKRKY MMTADFEGWS SPEVYNDPDL MKFGLTTAKT CEFMYHVALS RDPNQQPALS
     TIPPALRPMV LEFAKEVTAA QERVLAAMSV ALGLDASALQ NRFGPADVGI RANYYPLKRE
     GKTVGELPAH SDLPAIVFLF ADKVPGLEIR KDERWVRVKP VADAFVVNVA DCLEVLSNGR
     FRSAEHRGAG SEAEERISMV SFYMPSKAAT IGPMDELLDE THPARFRSAN FGQMGLELLS
     TGLKGKGFVE ALRIEG
//
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