ID A0A165Z3S2_EXIGL Unreviewed; 238 AA.
AC A0A165Z3S2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cloroperoxidase {ECO:0000313|EMBL:KZV79089.1};
GN ORFNames=EXIGLDRAFT_757215 {ECO:0000313|EMBL:KZV79089.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV79089.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV79089.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV79089.1,
RC ECO:0000313|Proteomes:UP000077266};
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=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the chloroperoxidase family.
CC {ECO:0000256|ARBA:ARBA00025795}.
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DR EMBL; KV426683; KZV79089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165Z3S2; -.
DR STRING; 1314781.A0A165Z3S2; -.
DR InParanoid; A0A165Z3S2; -.
DR OrthoDB; 2292322at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.489.10; Chloroperoxidase-like; 1.
DR InterPro; IPR000028; Chloroperoxidase.
DR InterPro; IPR036851; Chloroperoxidase-like_sf.
DR PANTHER; PTHR33577:SF9; PEROXIDASE STCC; 1.
DR PANTHER; PTHR33577; STERIGMATOCYSTIN BIOSYNTHESIS PEROXIDASE STCC-RELATED; 1.
DR Pfam; PF01328; Peroxidase_2; 1.
DR SUPFAM; SSF47571; Cloroperoxidase; 1.
DR PROSITE; PS51405; HEME_HALOPEROXIDASE; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KZV79089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..238
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007869740"
FT DOMAIN 24..223
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 238 AA; 24663 MW; 62A89D2A7E148298 CRC64;
MFVFSLAVLS LGSLVVSRSV ASDIRRSFVP PGPGDSRSPC PLLNALANEN IMPHTGQNIP
IALLNQTMRE VLNLGADLTD ALVGGAQQFA DDNGTINLHD LATHNVLEHD ASLVHDDAAP
GAVYAPTDTN KAKVAAVSGL STDGVGLTAR DLAHARVIAE ETSLPLPDNL AFAANVEAAL
ALTVIGDGTT VDLAAFGDLF GENKLPEGWV KPTEPITLDV VVGIASQVAA AKEEFESI
//
