ID A0A165EU88_EXIGL Unreviewed; 380 AA.
AC A0A165EU88;
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:KZV87697.1};
GN ORFNames=EXIGLDRAFT_679730 {ECO:0000313|EMBL:KZV87697.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV87697.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV87697.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV87697.1,
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; KV426118; KZV87697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165EU88; -.
DR InParanoid; A0A165EU88; -.
DR OrthoDB; 1693254at2759; -.
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:SF16; HEME_HALOPEROXIDASE DOMAIN-CONTAINING PROTEIN; 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:KZV87697.1};
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..380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007857425"
FT DOMAIN 69..302
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 380 AA; 41401 MW; 0817D3E598F1B2DE CRC64;
MLLSLKFSVL AIALQLASVL AVPALQPYDS LAGLTRDEVD AFARSVKVVG GQPIPKPIKD
TSLKLVNDKK HPWKPLRAGD QRGPCPGLNA LASHGWLPRS GVATPGEIVT AVQNGYNMEW
TRAVLVTYAA FLVNGNPLTN LLSIGGMSWL TGHAPPPPAL ASGLNTHGTF EGDASLTRSD
AFLGDNHSFN ETLFQQLIDI SNKVGGGKYN VSAAAEMRFQ RVQDSIARNP NFNFANPRFN
TAFIEAVFPI VFFIDGRLQE AGETGLDLDV MRGFFQDHRM PKDFHRRGTP TGASDSELDF
VMAAHDYVPG FNNGSGTFVA DPNFMGTQTE TVCALYEKFV NSTVSLYPSP HGDLRKALNK
NLDNFYVAVE SRCDQIKPYH
//
