ID A0A165IY63_EXIGL Unreviewed; 377 AA.
AC A0A165IY63;
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:KZV94047.1};
GN ORFNames=EXIGLDRAFT_612134 {ECO:0000313|EMBL:KZV94047.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV94047.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV94047.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV94047.1,
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; KV425979; KZV94047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165IY63; -.
DR InParanoid; A0A165IY63; -.
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:KZV94047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..377
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007859625"
FT DOMAIN 67..291
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 377 AA; 40620 MW; 8537678B55DF1DB2 CRC64;
MFISLQLAVV LALQLGNVFS YAIREFDSLA GLSNDEIEKF ARSVKVVGAQ PPPAPISDTS
AKLVHDIFHP FIPLFPGQQR GPCPGLNTLA SHGYLPRSGV ATPAQIITAV QEAPNAHRGT
QVTYAAFLVD GNPLTNLMSI GIKSPLTGPA PPSPALVSGL STHATFEGDS SMTRGDAFFG
DNHSFNETLF QQIVDAANLV GGGKYTVNVA AEVRFRRVQD SIATNPQFDF GNPRFATAFA
ETVFPLAFFI DGRSTAQELD LDVMRSFFQD SRMPVGFHRR DGPLDLSTLG QQIQVVMSAH
QFFPGFNNGT VNNFVPDVGF LGTQTNQLCA LVEHFTNNTL AQYPNPKGAL RTALNQNLDN
FFSAGVGATC VRPNIFP
//
