ID   A0A061DSJ1_THECC        Unreviewed;       343 AA.
AC   A0A061DSJ1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Senescence-associated gene 12 {ECO:0000313|EMBL:EOX92953.1};
GN   ORFNames=TCM_001814 {ECO:0000313|EMBL:EOX92953.1};
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:EOX92953.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX92953.1, 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 C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   EMBL; CM001879; EOX92953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061DSJ1; -.
DR   MEROPS; C01.104; -.
DR   EnsemblPlants; EOX92953; EOX92953; TCM_001814.
DR   Gramene; EOX92953; EOX92953; TCM_001814.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_1_0_1; -.
DR   InParanoid; A0A061DSJ1; -.
DR   OMA; LTEWEIW; -.
DR   Proteomes; UP000026915; Chromosome 1.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF1032; SENESCENCE-SPECIFIC CYSTEINE PROTEASE SAG12; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..343
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018730128"
FT   DOMAIN          41..98
FT                   /note="Cathepsin propeptide inhibitor"
FT                   /evidence="ECO:0000259|SMART:SM00848"
FT   DOMAIN          125..342
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
SQ   SEQUENCE   343 AA;  37934 MW;  EC9A04000499E440 CRC64;
     MAFKNLQLHQ CICLAFIFIV GALVCEATSR TLQDASMYER HEQWMARYGR VYHDNNEREQ
     RFNIFKENVA HIDSFNRAKD KPYKLGVNQF ADLTNEEFTA SRNRFKGHMC SNKATTFKYE
     NLTALPSTVD WRKKGAVTPI KDQGQCGCCW AFSAVAAMEG VTKLTTGKLI SLSEQELVDC
     DTKGEDQGCQ GGLMDDAFQF IQNNKGLTTE SDYPYKGVDG TCNTNKEANH AAKINGFEDV
     PANSEDALQK AVANQPVSVA IDAGGFKFQF YSGGVFTGDC GTALDHGVTA VGYGVDDDGT
     KYWLVKNSWG TSWGEEGYIR MQRDVDAKEG LCGIAMQASY PTT
//