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
//