ID B6K2G3_SCHJY Unreviewed; 458 AA.
AC B6K2G3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Vacuolar serine protease Isp6 {ECO:0000313|EMBL:EEB07344.1};
GN Name=isp6 {ECO:0000313|JaponicusDB:SJAG_02432};
GN ORFNames=SJAG_02432 {ECO:0000313|EMBL:EEB07344.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB07344.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB07344.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; KE651166; EEB07344.1; -; Genomic_DNA.
DR RefSeq; XP_002173637.1; XM_002173601.2.
DR AlphaFoldDB; B6K2G3; -.
DR STRING; 402676.B6K2G3; -.
DR MEROPS; S08.A54; -.
DR EnsemblFungi; EEB07344; EEB07344; SJAG_02432.
DR GeneID; 7049179; -.
DR JaponicusDB; SJAG_02432; isp6.
DR VEuPathDB; FungiDB:SJAG_02432; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR OMA; RHPDVDY; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:EnsemblFungi.
DR GO; GO:0000747; P:conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0007033; P:vacuole organization; IEA:EnsemblFungi.
DR GO; GO:0031638; P:zymogen activation; IEA:EnsemblFungi.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF05922; Inhibitor_I9; 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; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 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:UP000001744};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..458
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002845020"
FT DOMAIN 75..164
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 201..437
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 402
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 458 AA; 48805 MW; DB9090BA8956C8A9 CRC64;
MTGFFPSIFS AFVAFSAFTS GVLAMPVEGG IRNLVKRRGF KPSAGAERFE GFASADSAPL
LSSSNADTTG LESEYIVLLQ PNTEADSVHR HLQWVKDLSR EDAEMRAVDA SLDGIDVMSS
VKHVYDLSDL GFQGYSGRFS SYVLEQIRQH PDVAIVERDQ VVRVQDQIQQ SNAPWGLARI
SHRETLDADT LTKYEYDSSA GEGVEVYIID TGINTNHTEF EGRAVWGKTI PTGDADVDGN
GHGTHVAGTV ASRAYGVAKK AKVIAVKVLR SNGSGTMSDV ISGIEWAVKD YIRKLVKGKK
NTSIANMSLG GGRSIILDFA VDVAVRSGVS FAVAAGNEDD DACYSSPAAS NLAITVGAST
INDARAYFSN YGDCVDVFAP GLNILSTWIG SNVSTNIISG TSMATPHIAG LAAYLVGLND
TLSVYDIKDL ILDLATKDVL YDIPADTPNL LAYNGISA
//
