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Database: UniProt
Entry: G9NGB8_HYPAI
LinkDB: G9NGB8_HYPAI
Original site: G9NGB8_HYPAI 
ID   G9NGB8_HYPAI            Unreviewed;       873 AA.
AC   G9NGB8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN   ORFNames=TRIATDRAFT_81264 {ECO:0000313|EMBL:EHK50330.1};
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:EHK50330.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK50330.1, 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 S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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:EHK50330.1}.
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DR   EMBL; ABDG02000014; EHK50330.1; -; Genomic_DNA.
DR   RefSeq; XP_013948505.1; XM_014093030.1.
DR   AlphaFoldDB; G9NGB8; -.
DR   STRING; 452589.G9NGB8; -.
DR   GeneID; 25785576; -.
DR   eggNOG; KOG4266; Eukaryota.
DR   HOGENOM; CLU_014424_0_0_1; -.
DR   OMA; GHAYPAR; -.
DR   OrthoDB; 2247221at2759; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00306; Peptidases_S8_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        790..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          582..832
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        589
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        629
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        789
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   873 AA;  98505 MW;  BC89182D40485C64 CRC64;
     MANSGTPANT LAVIQLLVTT FATIRDVTRL LRTEEIDNEL KAFYANVNAN CTLMTRDWSR
     ISKSAYGIDE DLVSRTLSHL GSIITTSSLK PLQGSISSAT CYGGMRAFNQ EWNLIQKQSD
     KSMRIQHVRS CTNFGKTLEE RNRFIQRLNE YEDELQARYP DFQPDWISED LLIKKSIRQP
     SYAVWNAAQS IFKALVACSD CECTPSHEMW AQLGLGTYRK ASLNEEIDMD SGLDFDMFLS
     IKQDWQEAHI LMSEEVKERA VVFQDDSEVK KPQTRKSIAK TKQMRVKRLC EPIAKMRTMA
     AHRLELKVMR DQLFKLRSER STSLVDTTRS PITLEQFLKI GSRSFTERTR RILAVILSYA
     VLYLHDTPWL QHTWSSSHIL FFPTTSSAIP LRPFIQIQLG QYQESRQDPD DLDDPDDLEL
     ENLDPDDLIM HHCPFLVTLA VMLMEVYFAV PFNVLAKRYG YDIAPDAESS VSTRRCVDVE
     LVFKACREEI PENYQFHCAV DKCLDPAAWE DESGNKLDNE ALTLRIYQEI VLPLETELGQ
     AFTSMPIDEL DRIAQELNFP NWDQDDVYEK FIKPSSLNAV SSVKIAILDT GVDLSHPDFE
     ARVDNIKGKY NWLSPNSNKP HVITDRNGHG TFAASLILDY APDAQLYIAK IAESEPSSAG
     IIAKAINHAV STWEVDIISM SFGFPTCNTA DYHELEAALA HAHANRVLLF AAASNSGGKL
     GHAYPARDQH VIAIHSTDTN GNRSAFSPTA MDHDINLATV GEAVESAWPV YLSDETSNPN
     FVKYKSGTSY ATPIAAGIAG FLLLYSRIYL PDKASALKNR QKMQALLRQI AEKERGQTVR
     DGYYFIDLSL YADCLFGKSL DFIDATIRNV LST
//
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