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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//