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Database: UniProt
Entry: A0A067BZL0_SAPPC
LinkDB: A0A067BZL0_SAPPC
Original site: A0A067BZL0_SAPPC 
ID   A0A067BZL0_SAPPC        Unreviewed;       687 AA.
AC   A0A067BZL0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE            EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN   ORFNames=SPRG_11131 {ECO:0000313|EMBL:KDO23683.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO23683.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO23683.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO23683.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity for peptide
CC         bonds, and a preference for a large uncharged residue in P1.
CC         Hydrolyzes peptide amides.; EC=3.4.21.62;
CC         Evidence={ECO:0000256|ARBA:ARBA00023529};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KK583251; KDO23683.1; -; Genomic_DNA.
DR   RefSeq; XP_012205666.1; XM_012350276.1.
DR   AlphaFoldDB; A0A067BZL0; -.
DR   STRING; 695850.A0A067BZL0; -.
DR   EnsemblProtists; KDO23683; KDO23683; SPRG_11131.
DR   GeneID; 24133200; -.
DR   KEGG; spar:SPRG_11131; -.
DR   VEuPathDB; FungiDB:SPRG_11131; -.
DR   OMA; SPNQWGV; -.
DR   OrthoDB; 380531at2759; -.
DR   Proteomes; UP000030745; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..687
FT                   /note="subtilisin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001633885"
FT   DOMAIN          562..685
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        207
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        350
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   687 AA;  73585 MW;  2A86DF59B0092917 CRC64;
     MKAFLILSTM AAAASAKVAS SVLRALEVDG NADVFVRFAD ASSALEAATI ESNKPLERQE
     VFEILSDATA TGQKSIEAAT AGFEVTPTWI VSGAFIKAAD KALIEKLTLN RAIKSVEQVP
     DMELDPVLSK SNTDTITAPA ASPNQWGVDT VGAPAIWKYT NGSGIVIGSI DTGARHTHLL
     LKDSWRSDRG WYDPYNRTAV PEDLGGHGTH TIGTMTGNRG YGVAPGAQWI ACRGLYVKSG
     SAKALLECLQ FMICPTRTDG THPDCSKGAD TFHPVYEEAI ASIRKAGITP IFANGNEGPA
     CGTTGSPGTY PNVISVGAIG SYSNEPNKLA FFSSKGPGND TGLAYLAGTS MAAPHVAGVV
     ALLKSIKRDL TYDEIYAYLT QTADRALEGE PKEWLVPNAT SNGTDVYPGA PNCGGVDDTK
     WPNNRYGYGR VNVAKILDGG KFASVATPTP VPRTTPPAPI ETNFCTYKKT ALSEWNQGLY
     IDTIKGNKNE GFTIDRVSNV IAAYAPPKED SYCLALTKDA TNTNTATLTK CKGDETQIWN
     VAPCSPGAVS QYFDACDNVK EKSYVKLITK TNKVISEFYS GVYADWVSDS VNELFVYDSN
     AKTLQAASNG QCLDAFRDGD KFGLHTYACD ATNGNQKWII DAANHKIKHA THNNLCLDVD
     PTNPSHAAQV WECHNANTNQ WIDAVKY
//
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