ID G0R9K1_HYPJQ Unreviewed; 399 AA.
AC G0R9K1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 22-FEB-2023, entry version 50.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EGR52488.1};
GN ORFNames=TRIREDRAFT_53961 {ECO:0000313|EMBL:EGR52488.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR52488.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR52488.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GL985056; EGR52488.1; -; Genomic_DNA.
DR RefSeq; XP_006961397.1; XM_006961335.1.
DR AlphaFoldDB; G0R9K1; -.
DR EnsemblFungi; EGR52488; EGR52488; TRIREDRAFT_53961.
DR GeneID; 18485629; -.
DR KEGG; tre:TRIREDRAFT_53961; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_53961; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_1_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..399
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003408223"
FT DOMAIN 98..396
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 290
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 399 AA; 42350 MW; 176292829D23DF36 CRC64;
MQPSFGSFLV TVLSASMAAG SVIPSTNANP GSFEIKRSAN KAFTGRNGPL ALARTYAKYG
VEVPKTLVDA IQLVKSIQLA KRDSATVTAT PDHDDIEYLV PVKIGTPPQT LNLDFDTGSS
DLWVFSSDVD PTSSQGHDIY TPSKSTSSKK LEGASWNITY GDRSSSSGDV YHDIVSVGNL
TVKSQAVESA RNVSAQFTQG NNDGLVGLAF SSINTVKPTP QKTWYDNIVG SLDSPVFVAD
LRHDTPGSYH FGSIPSEASK AFYAPIDNSK GFWQFSTSSN ISGQFNAVAD TGTTLLLASD
DLVKAYYAKV QGARVNVFLG GYVFNCTTQL PDFTFTVGEG NITVPGTLIN YSEAGNGQCF
GGIQPSGGLP FAIFGDIALK AAYVIFDSGN KQVGWAQKK
//