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Database: UniProt
Entry: F0XF36_GROCL
LinkDB: F0XF36_GROCL
Original site: F0XF36_GROCL 
ID   F0XF36_GROCL            Unreviewed;       384 AA.
AC   F0XF36;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Pepsinogen c {ECO:0000313|EMBL:EFX04034.1};
GN   ORFNames=CMQ_962 {ECO:0000313|EMBL:EFX04034.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX04034.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; GL629765; EFX04034.1; -; Genomic_DNA.
DR   RefSeq; XP_014173516.1; XM_014318041.1.
DR   AlphaFoldDB; F0XF36; -.
DR   STRING; 655863.F0XF36; -.
DR   MEROPS; A01.081; -.
DR   GeneID; 25982099; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_062498_0_0_1; -.
DR   InParanoid; F0XF36; -.
DR   OrthoDB; 398606at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF68; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..384
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012203847"
FT   DOMAIN          29..374
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        60..67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   384 AA;  41027 MW;  302DC4E39B73B912 CRC64;
     MKSVLPLACL PGTLAAVFEL PVWIRNTYAV VEIEAGTPPV SHYLEFDTGS SSTWMASSDC
     VADPSACPNS SGYKRPGYDA SASSTSSSLN TTASIGYLGG TTGGSGAKDM FAMPSAPKDT
     WAQTFLAVNE SSFAALPGDG FLGLAFSTIA EGETTTLVET MMQDGLLDEP RFALYRGSET
     NDTGSSPGNG MLTVGGSHED KYVNGSLAWT QLQYPGSEAQ LWRTAMQSVV SRRPNTANTT
     FLDVNDCWAV FDTGAGGITV PDRLIDQIYE SIGMNYTAIL NGDVIPLCED FTDDWGITVY
     IGDFVPATEL TITGSMLKNP GFADGEAKYC WPPFDSNEAD GLFLFGNSFL QHFYTVFDFG
     GNLPTNYSAR IGLGPLKDEY KPVL
//
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