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Database: UniProt
Entry: W9SG16_9ROSA
LinkDB: W9SG16_9ROSA
Original site: W9SG16_9ROSA 
ID   W9SG16_9ROSA            Unreviewed;       768 AA.
AC   W9SG16;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Subtilisin-like protease {ECO:0000313|EMBL:EXC04834.1};
GN   ORFNames=L484_010262 {ECO:0000313|EMBL:EXC04834.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC04834.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; KE345511; EXC04834.1; -; Genomic_DNA.
DR   RefSeq; XP_010105478.1; XM_010107176.1.
DR   AlphaFoldDB; W9SG16; -.
DR   GeneID; 21393557; -.
DR   KEGG; mnt:21393557; -.
DR   eggNOG; ENOG502QSVG; Eukaryota.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
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; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF388; XYLEM SERINE PROTEINASE 1; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000030645};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..768
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004933167"
FT   DOMAIN          35..110
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          135..589
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          385..459
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          660..764
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          203..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        142
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        545
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   768 AA;  81223 MW;  8303288058C5A8F3 CRC64;
     MKTPIFIILQ LSAVLLSICQ LHVAADGRQS QQKRTYIIHM DKSNKPATFD NHFNWYDSSL
     KSVSDSADML YTYNNVIHGF STSLTEKEAQ FLKQQPGVLS VLQENRYELH TTRTPEFLGL
     GRSDALFPAS DKLSEVIVGV LDTGVWPESK SYDDAGLRRV PSSWKGECEV GKNFNSSSCN
     MKLIGARYFS AGYEEAFGPI DEKVESKSPR DDDGHGTHTS TTAAGSTVVE ASLFGFASGT
     ARGMATTARV ATYKVCWLGG CFGSDILAGI DKAIDDGVDV LSLSIGGGLN DYYRDTVAIG
     TFAAVAHGIV VSVSAGNGGP GSGSLSNVAP WLTTVGAGTL DRDFPAYVSL GNGQKYKGVS
     LYSGKPLSEE LVQIVYGRTA NNSTNGNLCL PGSLDSAKVT GKLVVCDRGG NPRAQKGQVV
     KDAGGVGMIL SNTESYGEEL VADAHLLPAV TVGQRTGNLI KTYLRSDANP TATITQGSTQ
     LGIQPSPVVA AFSSRGPNPI TPEILKPDLI APGVNILAGW TGRAGPTGLD TDNRRVSFNI
     VSGTSMSCPH VSGLAALLKA AHPEWSPAAI RSALMTTAYS TYKGGKTISD ISTGSSATPF
     DYGAGHVDPV AALEPGLVYD ATVQDYISFF CALNYSASQI KTVTKGDYTC DHTKKYSLGD
     FNYPSFAVPL ETASSSEGGA DASSTVKYTR TLTNVGEPAT YKVSISSDPS VKISVQPESL
     SFSEAYEKKT YTVTFTANSQ PSGTTSFARL EWSDGKHAVS SPIAFSWT
//
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