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Database: UniProt
Entry: S9VS07_SCHCR
LinkDB: S9VS07_SCHCR
Original site: S9VS07_SCHCR 
ID   S9VS07_SCHCR            Unreviewed;       991 AA.
AC   S9VS07;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:EPY50723.1};
GN   ORFNames=SPOG_00736 {ECO:0000313|EMBL:EPY50723.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY50723.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY50723.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
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 S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; KE546992; EPY50723.1; -; Genomic_DNA.
DR   RefSeq; XP_013024367.1; XM_013168913.1.
DR   AlphaFoldDB; S9VS07; -.
DR   STRING; 653667.S9VS07; -.
DR   EnsemblFungi; EPY50723; EPY50723; SPOG_00736.
DR   GeneID; 25035068; -.
DR   eggNOG; KOG1421; Eukaryota.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   OMA; FWGHCVF; -.
DR   OrthoDB; 1779375at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 3.
DR   Gene3D; 2.40.10.120; -; 2.
DR   InterPro; IPR025926; PDZ-like_dom.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR46366; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR   PANTHER; PTHR46366:SF8; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR   Pfam; PF12812; PDZ_1; 2.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SUPFAM; SSF50156; PDZ domain-like; 3.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EPY50723.1};
KW   Protease {ECO:0000313|EMBL:EPY50723.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464}.
FT   DOMAIN          371..447
FT                   /note="PDZ-like"
FT                   /evidence="ECO:0000259|Pfam:PF12812"
FT   DOMAIN          843..918
FT                   /note="PDZ-like"
FT                   /evidence="ECO:0000259|Pfam:PF12812"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  110251 MW;  97EB21BCA56AF82A CRC64;
     MAIKKRARGN SITQENDEKV PRMNGSYEPA ELENQLVETA PSSHLAESGK WKESIARVVR
     SVVSIRFSQV ASFDTDESGT GEASAFIVDA KNGYMLTNRH VVCAGPFIGH AILDNHEEVE
     VYPVYRDPVH DFGFLRFDPK KIRYMNVEQL ELRPDLAKVG TEIRVIGNDA AEKLSILAGW
     ISRVDRNVPD YGELTYCDFN TNYIQAAANA SGGSSGSPVV ERSGNVVALQ AGGHMVAATD
     YFLPLDRPLR ALRCLQNKKP ITRGTIQTQF LIKPFDECSR LGLDTAIEEQ VRGLFPGATS
     MLVVETVLPE GPSHNKLQEG DILLHLNSKY LIDLIELESI LDESIGQDIV LTVQRGNSTV
     DVTCRVQSTH DIAPDRYVEV CGAKFHNLSY QLARQYALPV KGVFISEPAG SFRLEGPEYC
     YLLESVAYKP VPDLDTFINV MKTIPDRSRV AVGYRFIHDK HSLVTDIIEV DRHWAKAFRL
     ASRNDETGFW DFQTLGDPLP AKPNIPCTTS IPKLNVENFG PTADINNCFV KITYYMPIHL
     DGYRKSRKQG TALVLDKNNG IAVTSRCTVP YALGDLTITV ADSIQIPAEV LHLHPTQNLT
     FIKYDPKLLG ETPIKAAKLR NHYVSQGDNV NFFGFNSKSR VVATKTSVTD VITMVIPPNP
     MPRFRAVNFE SITIESGLGS QCGSGVLTDD EGQVVALWLT HYGEQTSRGT DVKYHLGLAS
     PVVLSTLRRL QTDVNPHIRI LNVEFRAIQL AHARSMGLSA ERIQQIETAN EKRHQLFMIT
     HVEANTPRIL TDGDVILTAN GKPVTRVQDI EAEDTEEIEM DILRGGKEMK IKVPTFPTDN
     CETNRVIICW GATIQAPHRA VRLQSEGLPS NVFVTNRSRG SPADQYDLGI AQFITAINGI
     PTPDLESFVR EVRKVRDNSY VRVSTVTFDK VPVVLTIKMN EHYFPTLDLV RDFKAENGWR
     AVQYDEGREE DNPSMGLVIE EDVDTNSAAA D
//
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