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}.
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; 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
//