ID A0A165FJU1_EXIGL Unreviewed; 376 AA.
AC A0A165FJU1;
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:KZV89111.1};
GN ORFNames=EXIGLDRAFT_721985 {ECO:0000313|EMBL:KZV89111.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV89111.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV89111.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV89111.1,
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; KV426081; KZV89111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165FJU1; -.
DR InParanoid; A0A165FJU1; -.
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:KZV89111.1};
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..376
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007857784"
FT DOMAIN 67..297
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 376 AA; 40920 MW; 9650AE3FD05AFBAA CRC64;
MFLLSHIYIV LALQLGGVFG VALRPYESLA GLTREEVDAF ARSVKVVGGQ PVPPAIKDTS
SKLVNDKAHP WFPLAPGQQR GPCPGLNTLA SHGYLPRSGV ASPGQIVTAV QEGFNMAWDL
ATLVTYGAFL VDGNPLTNLM SIGSTSRLTG PAPPKPALVS GLSTHGTFEG DASMTRSDAF
LGDNHSFNET LFDQLVQISK EVGGGKYNVS AAAEVRFQRF QDSVARNPTF NFANPRFATA
FVETIFPLAF FIDGRDKSLA LDLDVMRGFF KDSRMPHDFH RREGAFEGGG DEFDIIQSSH
NYFPGFNNGT VNNFVPDPNF LGTQTEEICA LYEKFVNTTM ELYPNPQGAL RKALNVNLDN
FFIPVSSGCT QLHPFP
//
