ID B6K1Z6_SCHJY Unreviewed; 540 AA.
AC B6K1Z6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Aspartic protease Sxa1 {ECO:0000313|EMBL:EEB07177.1};
GN ORFNames=SJAG_02260 {ECO:0000313|EMBL:EEB07177.1};
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:EEB07177.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB07177.1, 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 A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KE651166; EEB07177.1; -; Genomic_DNA.
DR RefSeq; XP_002173470.1; XM_002173434.2.
DR AlphaFoldDB; B6K1Z6; -.
DR STRING; 402676.B6K1Z6; -.
DR MEROPS; A01.A91; -.
DR EnsemblFungi; EEB07177; EEB07177; SJAG_02260.
DR GeneID; 7050233; -.
DR JaponicusDB; SJAG_02260; -.
DR VEuPathDB; FungiDB:SJAG_02260; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_033751_0_0_1; -.
DR OMA; PIRDVTD; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF79; ASPARTIC PROTEINASE SXA1; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000313|EMBL:EEB07177.1};
KW Protease {ECO:0000313|EMBL:EEB07177.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002845015"
FT DOMAIN 72..434
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 326
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 360..399
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 540 AA; 57313 MW; 698CC30916B4C27D CRC64;
MHSLLGLVLG SILGAAYVNA GPVYKRVNGK PVVSFSLGRA EEDPEFVLDV SNRKRAEQFP
VINSTFDRSG SYFTNLTIGN PSKQYSLVMD TGSPYTWITA SNVTSFNTSE VGLSYTDGLN
TSALREGVCG TYQCYNYTST TLEVTNSSVV GFLSTYGDNT TVVGFNVVDE LDIGGLSLNN
FEFGLGTREF VSEDVPVTGG ILGLSPPISI YGISDTNRLV DFAAPTLLEQ LKTAGIVTST
AFSLSLDSAG GELVIGGYDT DKYTGDMHWL SISNSGSNSY YGVKIASMSI NTANTTSTTS
NSALSNFQKR NTISTSVSIN DIIILDSGTT LVYIPSDALE AIVNAYGGIL DTSSYAYVLC
DSISDEDTIT FQFNNNASFN ISVNDMVFYR DNSQGQGICY LAFIPTTDTY ILGQYFLRQV
YTVYDWDAQL IGLASIQNST SSNVIDIASA VSSIVSTTFS TTYASHTYVS SVDVLSSGSG
EPEATATSQV GVTTSAVHTT YTSPLTATTH TTATGSGAVS YGFRFGVVGA VLLLSCLVMA
//