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Database: UniProt
Entry: A5AKA0_VITVI
LinkDB: A5AKA0_VITVI
Original site: A5AKA0_VITVI 
ID   A5AKA0_VITVI            Unreviewed;       928 AA.
AC   A5AKA0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Subtilisin-like protease SBT3.6 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VITISV_018392 {ECO:0000313|EMBL:CAN80173.1};
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:CAN80173.1};
RN   [1] {ECO:0000313|EMBL:CAN80173.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT   vinifera L.): coping with a highly heterozygous genome.";
RL   PLoS ONE 2:e1326-e1326(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; AM428692; CAN80173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5AKA0; -.
DR   ExpressionAtlas; A5AKA0; baseline.
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; 2.
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:SF820; SUBTILISIN-LIKE PROTEASE; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 2.
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};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..928
FT                   /note="Subtilisin-like protease SBT3.6"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002679304"
FT   DOMAIN          41..119
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          145..591
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          669..758
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   DOMAIN          853..915
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
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        231
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        554
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   928 AA;  99781 MW;  B117FA92AD288E8A CRC64;
     MSSLSLQKKS SSALWFVIVS VLLILHDQVF FPAAVDAKSN VYIVYMGERQ HGNLDLITDG
     HHRMLSEVLG SDEASVESMV YSYKHGFSGF AAKLTEAQAQ MFAELPDVVQ VIPNRLHKLQ
     TTRSWDYLGL PLDSPTSLLH ETKMGDGTII GLLDTGIWPE SEVFSEKGLG PIPSRWNGVC
     ESGELFHGAK ACNRKLIGAR YLIKGLEAEI GQPFNTTENP DYLSPRDWLG HGTHTSTIAG
     GSSVHNVSYN GLGLGTVRGG APRARLAMYK VCWNLYGGVC ADADIFKGID EAIHDGVDVL
     SLSISSDIPL FSHVDQHDGI SIASFHAVVR GIPVVSAAGN SGPSAETVSN TAPWIITVAA
     STMDRLFATH ITLGNNQTIT GEAVYLGKDT GFTNLAYPEV SDLLAPRYCE SLLPNDTFAA
     GNVVLCFTSD SSHIAAESVK KAGGLGVIVA SNVKNDLSSC SQNFPCIQVS NEIGARILDY
     IRSTRHPQVR LSPSRTHLGN PVPTKVASFS SRGPSSIAPA ILKPDIAGPG FQILGAEPSF
     VPTSTKYYLM SGTSMATPHV SGAVALLRAL NREWSPAAIK SAIVTTAWTT DPSGEPVFAE
     GQPMKLADPF DFGGGILNPN GAGNPGLVYD MGKDDCILYL CAMGYNNSAI AKVTGRPTSC
     PCNRPSILDV NLPSITIPNL QYSVSLTRSV TNVGAVDSEY NAVIDPPPGV TIKLEPDRLV
     FNSKIRTITF RVMVSSARRV STGFSFGSLA WSDGEHAIYA DFRPKYQPKF RVVSRIRTGP
     ALLQSGSSPA VGSVNHQWVA VPDGRKLPLN PRGNFLLTQE EASSYPRLED SNTNLGGGLL
     PQFPLIGIST SPVHIVYLGK RQHHDPEFIT NTHHEMLTTV LGSKEASVDS MLYSYRHGFS
     GFAAKLTEAQ AQAVSGNLPC HKDYKFYW
//
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