GenomeNet

Database: UniProt
Entry: G2XN38_BOTF4
LinkDB: G2XN38_BOTF4
Original site: G2XN38_BOTF4 
ID   G2XN38_BOTF4            Unreviewed;       372 AA.
AC   G2XN38;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE            EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN   ORFNames=BofuT4P9000007001 {ECO:0000313|EMBL:CCD42294.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD42294.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00003917}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC         [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00035967};
CC   -!- SUBUNIT: Forms a one-to-one complex with cytochrome c.
CC       {ECO:0000256|ARBA:ARBA00038574}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC       subfamily. {ECO:0000256|ARBA:ARBA00005997}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQ790245; CCD42294.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2XN38; -.
DR   STRING; 999810.G2XN38; -.
DR   eggNOG; ENOG502QR1E; Eukaryota.
DR   HOGENOM; CLU_036959_1_1_1; -.
DR   InParanoid; G2XN38; -.
DR   Proteomes; UP000008177; Unplaced contigs.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   CDD; cd00691; ascorbate_peroxidase; 1.
DR   Gene3D; 1.10.520.10; -; 1.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR   InterPro; IPR044831; Ccp1-like.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR002207; Peroxidase_I.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR31356:SF58; CYTOCHROME C PEROXIDASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU363051};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          181..354
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   REGION          27..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   372 AA;  40750 MW;  444094459B823125 CRC64;
     MASATRTFAR AGAAFKSTPF RSATRTALSA PRQAFRQQSR RGYASEGPAK SSFPLSIGVA
     ALAIAGGAGY YFVSQGNGSL LSGSAKETSG LFTPKFDDYQ KVYNEIAERL EEKDDYDDGS
     YGPVLVRLAW HCSGTFDKET GTGGSNGATM RFAPEGDHGA NAGLVAARDF LAPIKAKHPW
     ISYSDLWILA GICAIQEMQG PVIPFRPGRQ DKDAAACTPD GRLPDASQGN KHLRDIFGRM
     GFNDQEIVAL SGAHALGRCH TDRSGFEGPW TFSPTVVTND YYKLLLNEKW SWKKWNGPKQ
     YEDKTSKSLM MLPTDMALVS DKSFRSYVEK YANDESLFMK DFANVITRLF ELGVPFAETT
     EQAPMKFKPT TA
//
DBGET integrated database retrieval system