PSP3_SCHPO
ID PSP3_SCHPO Reviewed; 451 AA.
AC Q9UTS0; P78879;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Subtilase-type proteinase psp3;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=psp3; ORFNames=SPAC1006.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13890.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D89229; BAA13890.1; ALT_INIT; mRNA.
DR EMBL; CU329670; CAB60231.1; -; Genomic_DNA.
DR PIR; T43069; T43069.
DR RefSeq; NP_594848.1; NM_001020277.2.
DR AlphaFoldDB; Q9UTS0; -.
DR SMR; Q9UTS0; -.
DR BioGRID; 279684; 3.
DR STRING; 4896.SPAC1006.01.1; -.
DR MEROPS; S08.032; -.
DR iPTMnet; Q9UTS0; -.
DR MaxQB; Q9UTS0; -.
DR PaxDb; Q9UTS0; -.
DR EnsemblFungi; SPAC1006.01.1; SPAC1006.01.1:pep; SPAC1006.01.
DR GeneID; 2543256; -.
DR KEGG; spo:SPAC1006.01; -.
DR PomBase; SPAC1006.01; psp3.
DR VEuPathDB; FungiDB:SPAC1006.01; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR InParanoid; Q9UTS0; -.
DR OMA; IVMFKPS; -.
DR PhylomeDB; Q9UTS0; -.
DR PRO; PR:Q9UTS0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0000328; C:fungal-type vacuole lumen; ISO:PomBase.
DR GO; GO:0008233; F:peptidase activity; IMP:PomBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:PomBase.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; ISO:PomBase.
DR GO; GO:0031638; P:zymogen activation; IMP:PomBase.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 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 Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Serine protease; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..451
FT /note="Subtilase-type proteinase psp3"
FT /id="PRO_0000027150"
FT DOMAIN 80..161
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 169..451
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 394
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CONFLICT 256
FT /note="A -> T (in Ref. 1; BAA13890)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="AV -> SF (in Ref. 1; BAA13890)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="D -> V (in Ref. 1; BAA13890)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="T -> S (in Ref. 1; BAA13890)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..325
FT /note="FFAV -> SCR (in Ref. 1; BAA13890)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> G (in Ref. 1; BAA13890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 48733 MW; 2F9E3A94E05261C0 CRC64;
MRVSWISGLL LVAHLAPSSA FNPLRFFLDD TFSSGATEEH FMGPSDDGFA LQQPTNYDPS
MPFPLDESAS AAVDAVSNNY IVMFKPSVDK SKLEQHHRWI EHLHEKRSLD FKDVSTFLMK
HTFEIGDAFL GYAGRFSPWL VAELQKHPDI ALVEPDRVMH VMTEQTFAPW GLARVSHRKK
LGFFTMTRYQ YNETAGEGVT AYVIDTGINI EHQDFQGRAT WGATIPTGEG EVDDHGHGTH
VAGTIAGKTF GVSKNAKLVA VKVMRADGTG TVSDIIKGIE FAFKQSKKDK ESIASVVNMS
IGGDASTALD LAVNAAIAGG LFFAVAAGND AEDACGTSPA RVSNAMTVGA STWNDQIASF
SNIGSCVDIF APGSLILSDW IGSNRASMIL SGTSMASPHV AGLAAYFISL DPSLANHPVE
LKKYMLKFAL KDLLNGIPED TPNVLAFNNY E
