ID A0A177CJ13_9PLEO Unreviewed; 256 AA.
AC A0A177CJ13;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cloroperoxidase {ECO:0000313|EMBL:OAG06777.1};
GN ORFNames=CC84DRAFT_1241503 {ECO:0000313|EMBL:OAG06777.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG06777.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG06777.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG06777.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441551; OAG06777.1; -; Genomic_DNA.
DR RefSeq; XP_018037142.1; XM_018184057.1.
DR AlphaFoldDB; A0A177CJ13; -.
DR STRING; 1460663.A0A177CJ13; -.
DR GeneID; 28767543; -.
DR InParanoid; A0A177CJ13; -.
DR OrthoDB; 2292322at2759; -.
DR Proteomes; UP000077069; 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:SF19; HEME HALOPEROXIDASE FAMILY PROFILE DOMAIN-CONTAINING PROTEIN-RELATED; 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:OAG06777.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..256
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008058363"
FT DOMAIN 37..246
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
SQ SEQUENCE 256 AA; 27601 MW; 3E48AD1CA94091D2 CRC64;
MRDHIVVLGL ISSSFVAASP ISPFGRHLSA ASTSAPAGHE WRIAGPSDSR SPCPMLNSMS
NHGWLPHNGK NIDLATIQSA FQSAMGFSTE SFISITEQAL TLSTTGNSST FHLSDLAHHN
AIEHDGSLSR NDQFFGDDLH FNPKIWATTA QRYGIRVPFS TPVITVETAS KARAARVRDA
KLVNPAFNLT DQSGSIGETS IFLTAFWDQS AGGVPKDYAR VLFEQERIPY AEGFVKGNHT
LADIVTMISA VSAVKV
//
