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Database: UniProt
Entry: J4KLF3_BEAB2
LinkDB: J4KLF3_BEAB2
Original site: J4KLF3_BEAB2 
ID   J4KLF3_BEAB2            Unreviewed;       570 AA.
AC   J4KLF3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Peptidase S8/S53, subtilisin/kexin/sedolisin {ECO:0000313|EMBL:EJP62104.1};
GN   ORFNames=BBA_08901 {ECO:0000313|EMBL:EJP62104.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP62104.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP62104.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP62104.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; JH725191; EJP62104.1; -; Genomic_DNA.
DR   RefSeq; XP_008602220.1; XM_008603998.1.
DR   AlphaFoldDB; J4KLF3; -.
DR   STRING; 655819.J4KLF3; -.
DR   GeneID; 19891913; -.
DR   HOGENOM; CLU_016268_0_0_1; -.
DR   InParanoid; J4KLF3; -.
DR   OrthoDB; 2491836at2759; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          266..495
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        274
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        322
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        477
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   570 AA;  64221 MW;  AAF2882B1DB3AF6A CRC64;
     MRSLAELIEL SQVERDRTRP VSVKDRYRLC YNLALSAYCL SSAAWRRLRW CKRKTFDANV
     FLHHDSTTGI IHDPTEAYLS CPIEAPLPQL EAGPDLKCDL NLLELGKILV EVRFWRKPDV
     FSEAHGRSWE EGIRRQLGLL ITDHPDLLDS ESPFVDAIKA CLSYEGKVAA KKKTTREFLT
     FFEEHILKPL SILLPDCPGA EEPKEDYLSD VETQREPLTA LPHKREPGPK SARAKEFMSR
     MQKFAISYVN PLSVKSRTPL PEDRSRKVRI AVIDSGISSS DSEIRIALRD SDIGLGLRDR
     RIAGLRNFCG TSVDDCEDYH GHGTTVAKIL LEAAPQAEIY IAKVTNSSTV SDDELHNVRK
     AINWAVQVWD ADIINLSLAM RVESRDIDEA LSHALLPGSK IIFAAAHNNA GHHEGPSWPG
     RKLGIIAIHC TDGDGQPLST NASVGREDYF ATLGLDIPIK EQFATTKSQY VYASGVSYAT
     PIAAGIAANM LEILRHEASH RVNDVKKWFY NGRYMKVLFK AISQRDHRCC FVQPWTFWHE
     IISVSPRYRD VQLRSGDERN IIRVLELLAA
//
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