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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//