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Database: UniProt
Entry: A0A1S3YYA2_TOBAC
LinkDB: A0A1S3YYA2_TOBAC
Original site: A0A1S3YYA2_TOBAC 
ID   A0A1S3YYA2_TOBAC        Unreviewed;       766 AA.
AC   A0A1S3YYA2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Subtilisin-like protease SBT1.9 {ECO:0000313|RefSeq:XP_016456822.1};
GN   Name=LOC107780755 {ECO:0000313|RefSeq:XP_016456822.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016456822.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016456822.1}
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_016456822.1; XM_016601336.1.
DR   AlphaFoldDB; A0A1S3YYA2; -.
DR   SMR; A0A1S3YYA2; -.
DR   STRING; 4097.A0A1S3YYA2; -.
DR   PaxDb; 4097-A0A1S3YYA2; -.
DR   GeneID; 107780755; -.
DR   KEGG; nta:107780755; -.
DR   OMA; SYECSAN; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000084051; Unplaced.
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; IPR022398; Peptidase_S8_His-AS.
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:SF545; SUBTILISIN-LIKE PROTEASE SBT3; 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; PS00137; SUBTILASE_HIS; 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:UP000084051};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..766
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010373729"
FT   DOMAIN          30..114
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          139..580
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          655..757
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        148
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        219
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   766 AA;  82724 MW;  FC8362DCBAEEE831 CRC64;
     MGLPYFHLLF LSWFLSALVF CLLATAQRST YIVHLDKSLM PNIFADHHHW HSSTIDSIKA
     AVPSSVDRFH SAPKLVYSYD NVFHGFSAVL SKDELQALKK SPGFVSAYKD RTVEPQTTHT
     SDFLKLNPSS GLWPASGLGQ DVIIGVLDSG IWPESASFRD DGMPEIPKRW KGICKPGTQF
     NTSLCNRKLI GANYFNKGIL ANDPTVNISM NSARDTDGHG THVASIAAGN FAKGVSHFGY
     APGTARGVAP RARLAVYKFS FNEGTFTSDL IAAMDQAVAD GVDMISISFG FRFIPLYEDS
     ISIASFGAMM KGVLVSASAG NRGPGIGSLN NGSPWILCVA SGHTDRTFAG TLTLGNGLKI
     RGWSLFPARA IVKDSTVIYN KTLADCNSEE LLSQLSDPER TIIICEDNGD FSDQMRIVAR
     ARLKAGIFIS EDPGVFRSAT FPNPGVVINK KEGKQAINYV KNTVDPTATI TFQETYLDVK
     PAPVVAASSA RGPSRSYLGI AKPDILAPGV LILAAYPPNV FATSIGPNIE LSTDYILESG
     TSMAAPHAAG IAAMLKGAHP EWSPSAIRSA MMTTADPLDN TRKPIKDSDI NKAATPLDMG
     AGHVDPNRAL DPGLVYDATP QDYLNLLCSL NFTEEQFKTI ARSSDNHNCS NPSADLNYPS
     FIALYPLEGP FTLLEQKFRR TVTNVGKGAA TYKAKIKAPK NTTVSVSPQT LMFKKKNEKQ
     SYTLTIRYLG DEGQSRNVGS ITWVEENGSH SVRSPIVTSP IIEISS
//
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