ID F6HXV5_VITVI Unreviewed; 771 AA.
AC F6HXV5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Subtilisin-like protease SBT1.4 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_09s0002g01040 {ECO:0000313|EMBL:CCB59280.1};
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:CCB59280.1, 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; FN596494; CCB59280.1; -; Genomic_DNA.
DR RefSeq; XP_002272769.1; XM_002272733.3.
DR AlphaFoldDB; F6HXV5; -.
DR PaxDb; 29760-VIT_09s0002g01040-t01; -.
DR EnsemblPlants; Vitvi09g01502_t001; Vitvi09g01502_P001; Vitvi09g01502.
DR GeneID; 100251409; -.
DR Gramene; Vitvi09g01502_t001; Vitvi09g01502_P001; Vitvi09g01502.
DR KEGG; vvi:100251409; -.
DR eggNOG; ENOG502QZDA; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; F6HXV5; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000009183; Chromosome 9.
DR ExpressionAtlas; F6HXV5; baseline and differential.
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; 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:SF785; SUBTILISIN-LIKE PROTEASE SBT1.4; 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; 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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..771
FT /note="Subtilisin-like protease SBT1.4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003338028"
FT DOMAIN 28..106
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 130..583
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 371..455
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 658..761
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 196..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 541
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 771 AA; 81932 MW; 5AA9804FD344E893 CRC64;
MGIPSSLFSL ILCLSLVSAT LSLDESQTFV VHVSKSHKPS AYATHHHWYS SIVRSLASSG
QPSKILYSYE RAANGFSARL TAAQASELRR VPGVLSVLPD RAHQIHTTRT PHFLGLADNY
GLWPNSDYAD DVIIGVLDTG IWPEIRSFSD SGLSPVPNSW NGVCDTGPDF PASACNRKII
GARAFFKGYE GALGRPMDES VESKSPRDTE GHGTHTASTA AGSVVQDASL FEFAKGEARG
MAVKARIAAY KICWSLGCFD SDILAAMDQA VADGVDIISL SVGATGLAPR YDHDSIAIGA
FGAMDHGVLV SCSAGNSGPD PLTAVNIAPW ILTVGASTID REFPADVVLG DGRIFGGVSI
YSGDPLKDTN LPLVYAGDCG SRFCFTGKLN PSQVSGKIVI CDRGGNARVE KGTAVKMALG
AGMILANTGD SGEELIADSH LLPATMVGQI AGDKIKEYVK SKAFPTATIV FRGTVIGTSP
PAPKVAAFSS RGPNHLTPEI LKPDVIAPGV NILAGWTGSK APTDLDVDPR RVEFNIISGT
SMSCPHVSGL AALLRKAYPK WTPAAIKSAL MTTAYNLDNS GNNIADLATG NQSSPFIHGA
GHVDPNRALY PGLVYDIDAN DYISFLCAIG YDTERIAIFV RRHTTVDCNT EKLHTPGDLN
YPAFSVVFNF DHDPVHQGNE IKLKRVVKNV GSSANAVYEV KVNPPEGIEV DVSPKKLVFS
KENQTASYEV SFTSVESYIG SRFGSIEWSD GTHIVRSPVA VRFHQDAVSS I
//
