ID A0A1S3C0J8_CUCME Unreviewed; 764 AA.
AC A0A1S3C0J8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Subtilisin-like protease SBT1.1 {ECO:0000313|RefSeq:XP_008454762.1, ECO:0000313|RefSeq:XP_016901624.1};
GN Name=LOC103495084 {ECO:0000313|RefSeq:XP_008454762.1,
GN ECO:0000313|RefSeq:XP_016901624.1};
GN Synonyms=103495084 {ECO:0000313|EnsemblPlants:MELO3C018316.2.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008454762.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|EnsemblPlants:MELO3C018316.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008454762.1, ECO:0000313|RefSeq:XP_016901624.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR RefSeq; XP_008454762.1; XM_008456540.2.
DR RefSeq; XP_016901624.1; XM_017046135.1.
DR EnsemblPlants; MELO3C018316.2.1; MELO3C018316.2.1; MELO3C018316.2.
DR GeneID; 103495084; -.
DR Gramene; MELO3C018316.2.1; MELO3C018316.2.1; MELO3C018316.2.
DR KEGG; cmo:103495084; -.
DR eggNOG; ENOG502QPRW; Eukaryota.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; Unplaced.
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:SF564; SUBTILISIN-LIKE PROTEASE SBT1.1; 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; 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:UP000089565};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..764
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010813665"
FT DOMAIN 24..109
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 133..604
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 369..457
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 660..761
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 542
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 764 AA; 81317 MW; 76F264A94932DB0D CRC64;
MGFREVWVLS IMLAISSAVV DQQTYIIHMD TTKMVTPNPE QWYTDIIDSV NELSSLDDNE
EASNAAEILY VYKTALSGFA AKLTSKKLHS LSKIPGFLAA TPNELLQLHT THSPQFLGLQ
RDHGLWNFSN LASDIIIGLL DTGIWPEHIS FQDKGLSSVP LKWKGICQTG PRFSSSNCNK
KLIGASAYIK GYEAIVGRLN ETGTFRSPRD SDGHGTHTAS TAAGSIVDNA SFYNQGMGVA
SGMRFTSRIV AYKVCWPLGC ANADILAAMD SAVADGVDVL SLSLGGGSSS FYKDNIAIAA
FGAIQKGVFV SCSAGNSGPS PSTVGNAAPW IMTVAASYTD RTFPTTVKLG NGQVFEGSSL
YYGKSINELP LVYNNTAGDG QETNVCIAGS LDPSMVKGKI VICERGTISR TEKGEQVKLA
GGTGMILINT QFEGEELFAD PHVLPATTLG ASAGKAILDY IASSKTQAKA SIVFEGTKYG
SQAPRVAAFS SRGPSLVGPD VIKPDVTAPG VNILAAWPPI VSPSELASDT RRVMFNIISG
TSMSCPHVSG LAALLKSAHN DWSPAAIKSA LMTTAYVTDS KMSLISDVGQ ANGEPATPFT
FGSGHVDPEK ASDPGLIYDI TPQDYINYLC SLKYNSSQIA LVSRGNLTCS SKRTVVKPGD
LNYPSFSVFM KKKAKKVSIT LKRTVTNVGI TRSDYTVKIN NPKGVTVIVK PEKLSFGSLG
EQLSYKVSFV SLGGKEALDK FSFGSLVWIS GKYAVRSPIV VTWQ
//
