ID G9P169_HYPAI Unreviewed; 454 AA.
AC G9P169;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=TRIATDRAFT_137451 {ECO:0000313|EMBL:EHK42477.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK42477.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK42477.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:EHK42477.1}.
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DR EMBL; ABDG02000026; EHK42477.1; -; Genomic_DNA.
DR RefSeq; XP_013940816.1; XM_014085341.1.
DR AlphaFoldDB; G9P169; -.
DR SMR; G9P169; -.
DR STRING; 452589.G9P169; -.
DR MEROPS; A01.080; -.
DR GeneID; 25775506; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_2_1; -.
DR OMA; WYGGVQS; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000005426; 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:SF1; ASPARTYL PROTEINASE; 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; 1.
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:UP000005426}.
FT DOMAIN 114..439
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 73..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 330
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 454 AA; 49230 MW; 4248A581CFAC774E CRC64;
MEAIFNVQSK FALERGLSKI KAIRNENYKR HGTKSYVYLL NRFGFEPTKP GPYFQGASFH
QRGLAHPDFH EARGGRVHKK KHLKKKQTPE GATDPNGTET GEVGAEDQQN DSEYLCEVTI
GTPGQKLLLD FDTGSSDLWV FSTELSKSLQ SNHTVFNPKN SSTFKALTGQ KWQISYGDGS
SASGDCGSDD VTVGGLTIKN QTVELASTLA QQFAQGTGDG LLGLAWPSIN TVTTNGKPTP
ANTPVANMIT QEDVPSESEL FTAAFYSERD ANAQSFYTFG YIDQDLVTAS GQQIAWTDVD
NSQGFWMFPS TSSSVNGKAI SQSGNSAIAD TGTTLALVSD DVCDALYKAI PGAKYDDQQQ
GYVFPMSTDV SSLPEFKVSV GNTQFVIQPE DLAFAPADNN NWYGGVQSRG DNPFDILGDV
FLKSVYAIFD QGNQRFGAVP KIQATQNLNP PSNQ
//