SPM1_MAGO7
ID SPM1_MAGO7 Reviewed; 536 AA.
AC P58371; A4QR64; G4N6T0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Subtilisin-like proteinase Spm1;
DE EC=3.4.21.-;
DE AltName: Full=Serine protease of Magnaporthe 1;
DE Flags: Precursor;
GN Name=SPM1; ORFNames=MGG_03670;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hoku1;
RX PubMed=12005067; DOI=10.1271/bbb.66.663;
RA Fukiya S., Kuge T., Tanishima T., Sone T., Kamakura T., Yamaguchi I.,
RA Tomita F.;
RT "Identification of a putative vacuolar serine protease gene in the rice
RT blast fungus, Magnaporthe grisea.";
RL Biosci. Biotechnol. Biochem. 66:663-666(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AB070268; BAB63284.1; -; Genomic_DNA.
DR EMBL; CM001234; EHA49897.1; -; Genomic_DNA.
DR PIR; JC7826; JC7826.
DR RefSeq; XP_003716216.1; XM_003716168.1.
DR AlphaFoldDB; P58371; -.
DR SMR; P58371; -.
DR STRING; 318829.MGG_03670T0; -.
DR MEROPS; S08.052; -.
DR EnsemblFungi; MGG_03670T0; MGG_03670T0; MGG_03670.
DR GeneID; 2676592; -.
DR KEGG; mgr:MGG_03670; -.
DR VEuPathDB; FungiDB:MGG_03670; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR InParanoid; P58371; -.
DR OMA; SNYGKCN; -.
DR OrthoDB; 921536at2759; -.
DR PHI-base; PHI:2117; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IEA:EnsemblFungi.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:EnsemblFungi.
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; 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; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease;
KW Signal; Vacuole; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..147
FT /evidence="ECO:0000250"
FT /id="PRO_0000027165"
FT CHAIN 148..536
FT /note="Subtilisin-like proteinase Spm1"
FT /id="PRO_0000027166"
FT DOMAIN 44..137
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 156..462
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 390
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 536 AA; 57170 MW; 85D112486CD8545B CRC64;
MKSVILLSLA ACAVAAPTAG VETIHDGAAP ILSSSNAEAI PNAYIIKFKK HVDHKSAADH
QMWIQKVHGE REDERLELRK RGLFDSVNDA FTGLKHTYNV GSGFLGYAGH FDEETIEKVR
RHPDVEAIER DTIVHTMRYE EVKKDECNPD LEKGAPWGLS RVSHRESLSF STYNKYLYSA
EGGEGVDAYV IDTGTNIDHV DFEGRAHWGK TIPANDQDID GNGHGTHCSG TVAGKKYGVA
KKAQVYAVKV LKSNGSGTMS DVIAGVDFAA KSHKAQVSAA KDGKRKGFKG SVANMSLGGG
KTTLLDAAVN AAVDAGIHFA VAAGNDNADA CNYSPAAAAK AVTVGASALD DSRAYFSNWG
KCTDIFAPGL NIQSTWIGSK TAINTISGTS MASPHIAGLL AYYLSLQPAS DSEYSLATIT
PEKLKADLIK VGTVGILTDI PKDTPNVLAW NGGGCSNYFE IVSKGGYKAK AQADKSSSLL
DSVTELEKAI EHDFRVISGK VVKEASSMTG QAEKLSEKIH QAVDEELKHF FGEARV
