ID M7X700_RHOT1 Unreviewed; 391 AA.
AC M7X700;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Chloroperoxidase-like protein {ECO:0000313|EMBL:EMS25840.1};
GN ORFNames=RHTO_00268 {ECO:0000313|EMBL:EMS25840.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS25840.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS25840.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS25840.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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; KB722642; EMS25840.1; -; Genomic_DNA.
DR RefSeq; XP_016276959.1; XM_016413952.1.
DR AlphaFoldDB; M7X700; -.
DR GeneID; 27364281; -.
DR eggNOG; ENOG502S5K7; Eukaryota.
DR HOGENOM; CLU_059431_0_0_1; -.
DR OrthoDB; 1693254at2759; -.
DR Proteomes; UP000016926; 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:SF18; 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:EMS25840.1}.
FT DOMAIN 107..331
FT /note="Heme haloperoxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS51405"
FT REGION 368..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 43989 MW; BFA029793CE394A4 CRC64;
MVAAPETQRQ REEESPTFAQ PIFPSLRFFH TILYAFKVVA FLVTLHTSDL VLLLLNLVSP
SRKGRDVSPP AFSPSNPPPF ADYPFLWGLC KTANWLGKEW SPEWLWSWTH WSGLLRKGKI
SQPMNEEGWS RSPCPALNAL ANHGIIPRDG RHLTPSQLSS AIQYAYNLSP TLAIQLLSPF
EPLWRDRGWF DLSDLGVHNL VEHDGSLTRE DNNSPFAQAT DVATQATPSK RLIDRYFPPE
VERPLTWQNF AAMLRHRRLE AREHNPQFVY NTLHRIFASG NAALEFRTID DKIQDHRDWL
GVGDDGCERF PRNFHSGAKD AYGYTILQAQ LFTAMIELAA GPIDGTPRMK TIADGVAAQD
GWNAMLGETG TKSRRHRASS PMSSAGGSSR D
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