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Database: UniProt
Entry: A0A0M8MW61_9BASI
LinkDB: A0A0M8MW61_9BASI
Original site: A0A0M8MW61_9BASI 
ID   A0A0M8MW61_9BASI        Unreviewed;       419 AA.
AC   A0A0M8MW61;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Clavaminate synthase-like protein {ECO:0000313|EMBL:KOS15000.1};
GN   ORFNames=Malapachy_1271 {ECO:0000313|EMBL:KOS15000.1};
OS   Malassezia pachydermatis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS15000.1, ECO:0000313|Proteomes:UP000037751};
RN   [1] {ECO:0000313|EMBL:KOS15000.1, ECO:0000313|Proteomes:UP000037751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS15000.1,
RC   ECO:0000313|Proteomes:UP000037751};
RA   Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT   "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT   pachydermatis CBS1879.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {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:KOS15000.1}.
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DR   EMBL; LGAV01000003; KOS15000.1; -; Genomic_DNA.
DR   RefSeq; XP_017992632.1; XM_018135776.1.
DR   AlphaFoldDB; A0A0M8MW61; -.
DR   STRING; 77020.A0A0M8MW61; -.
DR   GeneID; 28727651; -.
DR   VEuPathDB; FungiDB:Malapachy_1271; -.
DR   OrthoDB; 101125at2759; -.
DR   Proteomes; UP000037751; 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: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:SF39; 2OG-FE(II) OXYGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00800)-RELATED; 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:UP000037751}.
FT   DOMAIN          191..299
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          379..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  47351 MW;  7F025C523D752922 CRC64;
     MSTRSIPPWI PPPPSKVTDF DWAPLETLDL SLITGENMDQ VPVSVVEQVG TAFSSTGFMY
     AINHGLTYDQ VLRQFSIAQY GFDHITDDEK DRCVADMREA GSFVGYKPMG HWHIDGVKDR
     IEQLNFGSQH FTEGQHARYP SQVQPFLEEI HAFSRFNHDV ILRKVLAVLS LVLKLPVHTL
     WDLSKDHETK GLDLLRFALY RPPPPEDDEA LGGVRLQGHT DFNSVSILWS QPITSLEVLM
     PDNVWRKVRH RPNAVVLNLG DAMHFISGGL LKQTIHRVVG PPEDQQALQR LGVFYFALFN
     EDVPLEPLLQ SEVVKKAYHG RDFWAERRAQ GLPAVTAGEW ERLRVRAYGQ GGQKKGSDGH
     DHERIAGVDV KLYNSIPSTQ ATSHESRPAT HNVRASSPIR ARHKHLTETP RRVMSPLRA
//
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