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Database: UniProt
Entry: A0A061ETQ2_THECC
LinkDB: A0A061ETQ2_THECC
Original site: A0A061ETQ2_THECC 
ID   A0A061ETQ2_THECC        Unreviewed;       751 AA.
AC   A0A061ETQ2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Subtilisin-like serine endopeptidase family protein {ECO:0000313|EMBL:EOY08181.1};
GN   ORFNames=TCM_022517 {ECO:0000313|EMBL:EOY08181.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY08181.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY08181.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; CM001883; EOY08181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061ETQ2; -.
DR   MEROPS; S08.A13; -.
DR   EnsemblPlants; EOY08181; EOY08181; TCM_022517.
DR   Gramene; EOY08181; EOY08181; TCM_022517.
DR   eggNOG; ENOG502QRA7; Eukaryota.
DR   HOGENOM; CLU_000625_4_3_1; -.
DR   InParanoid; A0A061ETQ2; -.
DR   OMA; GRIVYCV; -.
DR   Proteomes; UP000026915; Chromosome 5.
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:SF397; SUBTILISIN-LIKE PROTEASE SBT4.15; 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:UP000026915};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..751
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001597790"
FT   DOMAIN          39..117
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          141..576
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          650..749
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        149
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        541
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   751 AA;  81583 MW;  9DB786526C745DF0 CRC64;
     MQNIAVKMMH NLLPFAGWLC LALAATLVQG STENERKPYI VYMGEAPHHE ARISVMDKHH
     NLLLKAVGDE NIARESKIYS YGKSINAFAA RLLPDEAKRL SGVDGVISVF ENTRRKLLTT
     RSWDFLGMHE KLKKRNAIAE SNIIVGVLDT GIWPKSPSFN DKGYGPPPAK WKGKCDKGAN
     FTGCNNKVIG ARYYQLDNTY PIMEDPTPVD TDGHGTHTAS TAAGIAVKDS SLYGIAKGTA
     RGGVPSARIA MYKVCWISGC SDMDLLAAYD DAIHDGVDLI SISIGGPPKE FFHDPIAIGA
     FHAMRKGILT SCAGGNEGPM LATVQNVAPW IMTVAASSID RQFTSKIKLG DGTTTSGNGI
     NTFSMKNKMY PFTNGAHATN LTGNYTDRNI SACDYGTMSQ DRVKGKIVYC LGEAGQDYTI
     QLLGGAGTIM ATDAPQDYYF LTLTPAATVV RSKDGDKLDR YINSTKKPQA VIYKSRTVKM
     NAPFVASFSS RGPQLLNRNI LKPDIAAPGL NILAAYTNLR SITGEPSDKR YSAFNFMSGT
     SMACPHASAA AAYVKSMHPD WSPAAIKSAL MTTATPMKIR DKFGELSSGS GQINPIRAIQ
     PGLIYDIDER SYISFLCKQG YNSTTIGLLI GGEQKLDCSS FKPARGTDGL NYPSMHVHLN
     STESRIFAVF YRTVTHVAYG NSEFKAKVTS PKGLSIAVIP NTLKFNRTHQ KQSFKVLVKG
     GLMKNGTEIL SATLEWSNKE HSVKSPILVY K
//
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