ID F6H1C3_VITVI Unreviewed; 770 AA.
AC F6H1C3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Subtilisin-like protease SBT1.9 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_18s0001g10340 {ECO:0000313|EMBL:CCB45832.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB45832.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; FN595227; CCB45832.1; -; Genomic_DNA.
DR RefSeq; XP_019071844.1; XM_019216299.1.
DR AlphaFoldDB; F6H1C3; -.
DR MEROPS; S08.150; -.
DR PaxDb; 29760-VIT_18s0001g10340-t01; -.
DR EnsemblPlants; Vitvi18g00772_t001; Vitvi18g00772_P001; Vitvi18g00772.
DR Gramene; Vitvi18g00772_t001; Vitvi18g00772_P001; Vitvi18g00772.
DR eggNOG; ENOG502QT5U; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; F6H1C3; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000009183; Chromosome 18.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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:SF514; SUBTILISIN-LIKE PROTEASE; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 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:UP000009183};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..770
FT /note="Subtilisin-like protease SBT1.9"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003340543"
FT DOMAIN 36..121
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 145..584
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 658..762
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
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 770 AA; 82948 MW; C53FF1D1A4C39006 CRC64;
MRCESFDKVV HRLHLILLTW ILLTIQARSM SGERSTYIIH MDKSVMPKVF ATHHHWYSSI
LHAIKTDTPT TSAGLQSTAR LIYTYDHALH GFSALLSSQE LESLRESPGF VSAYRDRAVT
LDTTHTFEFL KLNPVTGLWP ASDYGEDVIV GVIDSGVWPE SPSFKDDGMT QIPARWKGTC
EEGEDFNSSM CNRKLIGARS FIKGLIAANP GIHVTMNSPR DSFGHGTHTS STVAGNYVEG
ASYFGYATGT ARGVAPRARV AMYKVAGEEG LTSDVIAGID QAIADGVDVI SISMGFDYVP
LYEDPIAIAS FAAMEKGVLV SCSAGNAGPL PLGTLHNGIP WILTVAAGTI DRSFTGTLTL
GNGLTITGWT MFPASAVVQN LPLIYDKTLS ACNSSELLSG APYGIIICHN TGYIYGQLGA
ISESEVEAAI FISDDPKLFE LGGLDWPGVV ISPKDAPALI DYAKTGNKPR ATMTFQQTIV
NTKPAPAVAF YTSRGPSPSC PTILKPDVMA PGSLVLAAWV PNRETARIGT GLSLSSDYTM
VSGTSMACPH ASGVAALLRG AHPEWSVAAI RSAIVTTANP YDNTFNHIRD NGLNFTIASP
LAMGAGQIDP NGALDPGLVY DATPQDYVNL LCSMNFTKKQ ILTITRSNTY TCPKTSPDLN
YPSFIALYSQ NDNKSTTVVQ KFQRTVTNVG DGTATYHATV IAPRGSKVTV SPTTLVFEKK
YEKQSYTMSI KYKSDKDGKI SFGWLTWIED DGEHTVRSPI VVSPLVVNHR
//
