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Database: UniProt
Entry: T5ABQ4_OPHSC
LinkDB: T5ABQ4_OPHSC
Original site: T5ABQ4_OPHSC 
ID   T5ABQ4_OPHSC            Unreviewed;       484 AA.
AC   T5ABQ4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Chloroperoxidase {ECO:0000313|EMBL:EQL00024.1};
GN   ORFNames=OCS_04265 {ECO:0000313|EMBL:EQL00024.1};
OS   Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS   caterpillar fungus) (Hirsutella sinensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL00024.1, ECO:0000313|Proteomes:UP000019374};
RN   [1] {ECO:0000313|EMBL:EQL00024.1, ECO:0000313|Proteomes:UP000019374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC   TISSUE=Fruit-body {ECO:0000313|EMBL:EQL00024.1};
RX   DOI=10.1007/s11434-013-5929-5;
RA   Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA   Liu X., Wang C.;
RT   "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT   fungus.";
RL   Chin. Sci. Bull. 58:2846-2854(2013).
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; KE653000; EQL00024.1; -; Genomic_DNA.
DR   AlphaFoldDB; T5ABQ4; -.
DR   eggNOG; ENOG502S170; Eukaryota.
DR   HOGENOM; CLU_563920_0_0_1; -.
DR   Proteomes; UP000019374; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:EQL00024.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..484
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004596802"
FT   TRANSMEM        444..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..254
FT                   /note="Heme haloperoxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51405"
FT   REGION          326..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  54387 MW;  9C9BAC793A56132C CRC64;
     MRKTWIFGLF LPCLVQSLHC IKSAKTCKIL NPDDSRFLHY RKPGPDDSRS PCPALNALAN
     HGFLPRDGKN IGMAQIVCAL FEGIGVDPVI SVAILAFGIA SSKKPLCFTF DLEDLASHKM
     AIEHDCSFSR DDWKNGTGNN RDFNPELWKV TYDELRRSYG SSTPRTYINF ITMGRAKAVR
     VKDALRRNPD SQWAPRAWFN GYSEHGLVLS AFSDNIPGFA RLCVIKALFE EERLPWKEGW
     RPGKFRLNLV SLVVVGTLSI LGDRNAFLSM WRFLKGEPME LLEVFIPPKI DHFPDMVEMV
     GALGFDKSGM EKAVKTMTKI FHKRKRIVPP IEQHPEHRRP REYKKRGLEN LESIEGLESL
     ESLENLESIE GLEGIEGQES LEGQESLEGQ EGLESLERLK KHRPSHASGH SDGRCIDVKH
     GGMGVLFGNM KGAIYDCLHI NPAAVVEMIV FLLQNLGVLG LAGLVPMRKF LLSTMAEIGF
     KFGH
//
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