ID   A0A0G4F0B4_9ALVE        Unreviewed;       804 AA.
AC   A0A0G4F0B4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-NOV-2024, entry version 23.
DE   RecName: Full=Plant heme peroxidase family profile domain-containing protein {ECO:0000259|PROSITE:PS50873};
GN   ORFNames=Cvel_14436 {ECO:0000313|EMBL:CEM04887.1};
OS   Chromera velia CCMP2878.
OC   Eukaryota; Sar; Alveolata; Colpodellida; Chromeraceae; Chromera.
OX   NCBI_TaxID=1169474 {ECO:0000313|EMBL:CEM04887.1};
RN   [1] {ECO:0000313|EMBL:CEM04887.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Otto D Thomas, Naeem Raeece;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = O2 + 2 H2O; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001378};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR   EMBL; CDMZ01000030; CEM04887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4F0B4; -.
DR   VEuPathDB; CryptoDB:Cvel_14436; -.
DR   OrthoDB; 317402at2759; -.
DR   PhylomeDB; A0A0G4F0B4; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:TreeGrafter.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro.
DR   GO; GO:0033014; P:tetrapyrrole biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.520.10; -; 2.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR   PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR   PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..804
FT                   /note="Plant heme peroxidase family profile domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005187894"
FT   DOMAIN          170..366
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   REGION          52..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   804 AA;  86572 MW;  58B91540463A976D CRC64;
     MIQGKFHSLL VVAVLFLLLP TASSRCPFGF GGGDSHRAEG SASFERRALR MAPPAPAPSA
     DAVDSRQTGD GTSNSGVSRN PEFEKDAQPS PTYTEDFLSL NLSAVKEDLR RRFTTSNPVW
     PADYGNYGPM MVRLAWHSAG TYRVFDGRGG VNGARQRFPP ENSWDDNVNL DKARWLLEPV
     KRKYGQKISW GDLIVLAGDT ALETAGLKPL GFCGGRVDDI DGTKSLPLGP SAEQERDFPC
     PVNGDCHAPL GTTQMGLIYV NPEGYLGNPD PAMSVPHIRD TFARMGMNDS ETVALIGGGH
     TLGKTHGACE AGVGPPPDEA GPTSQGFGWK GKCGSGKGRD AWTSGFEGPW TSTPLTFDSD
     FLDNLLIYSW EKERGPGGKW QWRIGNETTE DAPQVDNSTE RVPLMMLTTD VALLHDPIYK
     GLLETFNNNH TKFEDAFRHA WYKLTTRDMG PHSRCIGSEV PPPQLFQDPV PSPPSNPPDW
     NQVRAAVKEL LRGSSSSSNG TAVQASHGEL VRLAWQCASS FRQTDFRGGC NGARIRLSPQ
     KDWEGNKGTD ATMQKLAVVK ARFPSLTWSD LIVLAGTEAL NDALVVSSDR EGGSPPVTFR
     FCPGRGDATA QETDAESFSV LEPSVSVVTD FPRTASVDTV KARMDLMGLG LSEWVAIVGA
     ARAVGAFHPY ASAVNVTGPA VASAEVPKSR TATSASSSDR LLNNRFFVLM RENLWVPAET
     ETENGKGGMF KVAGDGERQS EGGLRVTELD VALVTDPEVA NVMGTFAGDG NVFLQEAVRA
     WEKAMNLDRF EGPEGSPCAH SAAS
//