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Database: UniProt
Entry: F7VWQ2_SORMK
LinkDB: F7VWQ2_SORMK
Original site: F7VWQ2_SORMK 
ID   F7VWQ2_SORMK            Unreviewed;       843 AA.
AC   F7VWQ2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=WGS project CABT00000000 data, contig 2.11 {ECO:0000313|EMBL:CCC09943.1};
GN   ORFNames=SMAC_02523 {ECO:0000313|EMBL:CCC09943.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC09943.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC09943.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC09943.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
CC   -!- SIMILARITY: Belongs to the peroxidase family.
CC       {ECO:0000256|RuleBase:RU004241}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCC09943.1}.
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DR   EMBL; CABT02000011; CCC09943.1; -; Genomic_DNA.
DR   RefSeq; XP_003352088.1; XM_003352040.1.
DR   AlphaFoldDB; F7VWQ2; -.
DR   GeneID; 10809781; -.
DR   KEGG; smp:SMAC_02523; -.
DR   VEuPathDB; FungiDB:SMAC_02523; -.
DR   eggNOG; KOG4157; Eukaryota.
DR   HOGENOM; CLU_004824_1_0_1; -.
DR   InParanoid; F7VWQ2; -.
DR   OMA; HDMSTAN; -.
DR   OrthoDB; 1478506at2759; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   CDD; cd08201; plant_peroxidase_like_1; 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; IPR002889; WSC_carb-bd.
DR   PANTHER; PTHR31356:SF53; PEROXIDASE; 1.
DR   PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   Pfam; PF01822; WSC; 2.
DR   SMART; SM00321; WSC; 2.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
DR   PROSITE; PS51212; WSC; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..843
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003364566"
FT   DOMAIN          125..342
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   DOMAIN          612..703
FT                   /note="WSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51212"
FT   DOMAIN          730..822
FT                   /note="WSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51212"
FT   REGION          541..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  87725 MW;  01DA8AA23AB02203 CRC64;
     MKYNAYHALA GLLSLAARTG ADPTWPAATD EMEEIVYQLQ GFKGRVFNDI ITPCNNEAAG
     PGRVTASEWL RVGFHDMATH NRVFGTGGLD ASLQFELTNG ENTGPGHNTT LKFFANYYSS
     QSTMSDLIAA GVYASVRSCG GPIIPLRLGR KDATSGGSTG VPQPQNSAET FRQQFDRMGF
     STEEMIQVTA CGHTLGGVHT EEFPEIVPVG TGTNGQKSLD TTDATFDNKV VTEYISGTTQ
     NPLVVGPAVA LNRHSDFKVY NIDGNATMNG LTSAENFRNV CKTVLQKMID TVPSGVTLTD
     PIAPYAVKPV DMQLTLNSGG SSFLLTGYIR VRTTNRASGA IKNIKMTWKD RNGGCASGSC
     SYTATVQGAG TGFDDTFEFY PISTNIPASS GISSFTVTIN LNDGTSESYD NNGNSYPLSD
     AIILQKPQSC LLQTSGALTV SALVRNDITT TPSLGISYLT PRGVVRNGNP VPILSSATVA
     MTKGDCIGPY TFYSASYTIA GGLSYAAKLS VTAGSSSDSF NKASDLSGSC ATFSGTASCT
     TPGSGGGDGG GNDPDASSTV ASTAASSSAA EPSSTSSVVK EISSSDVPSS TTTTSSSTPT
     ATGPARKLTV AGYTRLRCAT EGSGVRALTG ASFAYDTMTL ESCAANCTGF AYFGTEYSRE
     CFCGNTLASS SSEAPDSECN MLCAGDSTEY CGAGNRLELY STTAGTGTGT ATSSAAQPTA
     TLGRKDAVGD YVFVGCQTEA TQGGRALEGK FWADDGMTLE GCAEACEGWE YFGAEYGREC
     FCGNTLRGGS APAPLADCSF TCAGNPYQYC GAGNRLELYR LASASSSSTK ARKRTRGERA
     RRL
//
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