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Database: UniProt
Entry: A0A061G5B4_THECC
LinkDB: A0A061G5B4_THECC
Original site: A0A061G5B4_THECC 
ID   A0A061G5B4_THECC        Unreviewed;       773 AA.
AC   A0A061G5B4;
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=Subtilase family protein {ECO:0000313|EMBL:EOY24598.1};
GN   ORFNames=TCM_016159 {ECO:0000313|EMBL:EOY24598.1};
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:EOY24598.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY24598.1, 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; CM001881; EOY24598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061G5B4; -.
DR   STRING; 3641.A0A061G5B4; -.
DR   EnsemblPlants; EOY24598; EOY24598; TCM_016159.
DR   Gramene; EOY24598; EOY24598; TCM_016159.
DR   eggNOG; ENOG502QRA7; Eukaryota.
DR   HOGENOM; CLU_000625_4_3_1; -.
DR   InParanoid; A0A061G5B4; -.
DR   OMA; PFPYMED; -.
DR   Proteomes; UP000026915; Chromosome 3.
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:SF812; SUBTILISIN-LIKE PROTEASE SBT4.1; 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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..773
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001598884"
FT   DOMAIN          33..109
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          131..579
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          635..735
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
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        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        528
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   773 AA;  83563 MW;  43062F35095BF65A CRC64;
     MAKKGLIPLL CSLLFAAFLL NSHAANASER KIHVVYMGDR LKGDLSAKRV HYSMLTSVLG
     SSSSAKESLV YSYGNFNAFA AKLTEEEVKT FSEMDGVVRV IPNHILQLHT TRSWDFLGFS
     QSSLGARIEG DVVIGLLDTG IWPEHESFTN QELGAPPSKW KGICQGANFT CNNKIVGARY
     YNSEEWYSDT DFKSPRDSEG HGTHTSSTAA GNRVADASYY GLANGIARGG VPGARIAMYK
     VCWSFGCATA DILAAFDDAI ADGVDIISVS LGFIFALAYD EDPIAIGAFH AMKNGILTSN
     SAGNSGPWPY SVVNFAPWTL TVAASTIDRK FVTRVELGNG MSYAGPSINS FDLHGKSYPL
     IWGGDAANYS AGSNPDLSKY CINGYLNSYR VYGNIVFCEL LWDGTGILEA SGVGTIMASD
     RLKDFAFSFP LPATVISTKD GEQILDYIRS AEYPVATILF GETWSDVMAP YVVSFSSRGP
     NPMNPDILKP DLTAPGVDII AAWSPVAPPS VAYEDPRSVN YNIISGTSMS CPHASGAAAY
     VKAAHPDWSP AAVKSALMTT ATVMDSTKHE DLEFAYGSGQ INPAHAIEPG LVYDANETDY
     INFLCKQGYN TTTIRLITGD NSSVCTSTVI GRAWDLNYPS FSLAVEDGEP ISGVFTRTVT
     NVGSANSTYT VRMYSPSNFS ISVEPQVLSF STVGEKKSYT VTVTGGTISQ QKIMSGAIIW
     TDGDHQYEVR SPVVVYNVLP GYTYFPPQNS KFQEKPTFQG PSMYEKYGVL RRN
//
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